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1
Aguilar, Guillermo, Blanca A. Trejo, Juan M. García, and Carlos Huitrón. "Influence of pH on endo- and exo-pectinase production by Aspergillus sp. CH-Y-1043." Canadian Journal of Microbiology 37, no. 12 (December 1, 1991): 912–17. http://dx.doi.org/10.1139/m91-158.
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Aspergillus sp. CH-Y-1043 grown on pectins with various degrees of esterification produces endo- and exo-pectinases at pH values as low as 2.5. Maximal production was attained at this pH, although fungal growth only approximated 50% of that obtained at higher pH values. Endopectinase was produced at pH 2.5–3.5 when the fungus was grown on low degree esterified pectin. With higher degree esterified pectin this enzyme was produced at all pH values analyzed. Exopectinase production was less affected by pH values. Still, maximal production was also reached at pH 2.5–3.5. Exopectinase was found to be associated to the cell and could be released after incubation at different pH values, whereas endo pectinase was not detected in the cellular fraction. Results confirmed by SDS–PAGE coupled with in situ activity assays in pectin–agarose gels allowed the identification of a protein band corresponding to endopectinase and a band with pectin esterase activity. Stability of Aspergillus sp. CH-Y-1043 pectinases at various pH values was also evaluated. Key words: Aspergillus sp. CH-Y-1043, extreme acidic pH pectinase production, in situ pectinase detection, cell-associated exopectinase.
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Amanat, Fatima, Amna Yaqoob, Asif Ali, and Muhammad Sajjad. "Extracellular Production of Pectinase from Bacteria Isolated from Rotten Apples from Lahore, Pakistan." BioScientific Review 01, no. 03 (September 2019): 37–45. http://dx.doi.org/10.32350/bsr.0103.05.
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Pectins are intricate blends of polysaccharides which make up around 33% of plantcell wall. Despite of their presence in the greater part of plant body and in other sources, commercial production of pectin is extremely difficult. This is a systematic study that aimed to produce pectinase from bacterial species isolated from rotten apple samples. Zymography and enzyme assay through DNS method were performed to check the pectinolytic activity of bacteria isolated from rotten apple samples. Of all five bacterial species (Serratia marcescens, Klebseilla pneumoniea, Pseudomonas aeruginosa and Escherichia coli) maximum enzyme concentration was showed in Pseudomonas aeruginosa and it was 6.2 U/mL. The major achievement of this study was to screen out the most efficient pectinases producing isolate of Serratia marcescens from rotten apples that has never been reported to produce pectinase, previously.
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Roy, Karabi, Sujan Dey, Md Kamal Uddin, Rasel Barua, and Md Towhid Hossain. "Extracellular Pectinase from a Novel Bacterium Chryseobacterium indologenes Strain SD and Its Application in Fruit Juice Clarification." Enzyme Research 2018 (March 21, 2018): 1–7. http://dx.doi.org/10.1155/2018/3859752.
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Pectinase is one of the important enzymes of industrial sectors. Presently, most of the pectinases are of plant origin but there are only a few reports on bacterial pectinases. The aim of the present study was to isolate a novel and potential pectinase producing bacterium as well as optimization of its various parameters for maximum enzyme production. A total of forty bacterial isolates were isolated from vegetable dump waste soil using standard plate count methods. Primary screening was done by hydrolysis of pectin. Pectinase activity was determined by measuring the increase in reducing sugar formed by the enzymatic hydrolysis of pectin. Among the bacterial isolates, the isolate K6 exhibited higher pectinase activity in broth medium and was selected for further studies. The selected bacterial isolate K6 was identified as Chryseobacterium indologenes strain SD. The isolate was found to produce maximum pectinase at 37°C with pH 7.5 upon incubation for 72 hours, while cultured in production medium containing citrus pectin and yeast extract as C and N sources, respectively. During enzyme-substrate reaction phase, the enzyme exhibited its best activity at pH of 8.0 and temperature of 40°C using citrus pectin as substrate. The pectinase of the isolate showed potentiality on different types of fruit juice clarification.
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CHAMANI, Esmaeil, Seyyed Karim TAHAMI, Nasser ZARE, Rasool Asghari-ZAKARIA, Mehdi MOHEBODINI, and Daryl JOYCE. "Effect of Different Cellulase and Pectinase Enzyme Treatments on Protoplast Isolation and Viability in Lilium ledebeourii Bioss." Notulae Botanicae Horti Agrobotanici Cluj-Napoca 40, no. 2 (November 5, 2012): 123. http://dx.doi.org/10.15835/nbha4028055.
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For overcoming interspecific incompatibility, protoplast combination method is a proper procedure for making a new plant withdesired traits. For this purpose, protoplast preparation is a first and important step. Hence, experiments were conducted to evaluatevarious combinations of cellulose, pectinase and their treatment times on protoplast production and protoplast viability in Liliumledebeourii Bioss. The results of experiment revealed that the protoplast yield was significantly affected by different treatment levels.Cellulase at 4% gave the highest numbers of protoplasts at 3.71×105 protoplast/g FW. Pectinase at 1% gave the highest numbers ofprotoplast. For treatment times, the highest yield of protoplast was with leaf explants treated for 24 h. Analysis of variance indicated thatconcentration, time and three-way interaction of cellulase, pectinase and time were significant at p<0.01. Cellulase at 4% and pectinase at0.2% for 24 h gave the highest viability. Interactions of cellulase × pectinase, cellulase × time, pectinase × time and cellulase × pectinase× treatment time were significant at P≤0.05 for protoplast number. The highest and lowest protoplast numbers were produced in mediacontaining 4% cellulase and 1% pectinase for 24 h (6.65×105 protoplast/g FW) and 1% cellulase and 0.2% pectinase for 12 h, respectively.It’s concluded that, the best treatment for isolation of Lilium protoplast was 4% cellulase and 1% pectinase for 24 h.
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Doan, Chien Thang, Chien-Lin Chen, Van Bon Nguyen, Thi Ngoc Tran, Anh Dzung Nguyen, and San-Lang Wang. "Conversion of Pectin-Containing By-Products to Pectinases by Bacillus amyloliquefaciens and Its Applications on Hydrolyzing Banana Peels for Prebiotics Production." Polymers 13, no. 9 (May 4, 2021): 1483. http://dx.doi.org/10.3390/polym13091483.
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The utilization of pectin-containing by-products may be useful in a variety of fields. This study aims to establish the processing of pectin-containing by-products to produce pectinases using Bacillus amyloliquefaciens TKU050 strain. In this study, several kinds of agricultural pectin-containing by-products from banana (banana peel), rice (rice bran), orange (orange peel), coffee (spent coffee grounds), and wheat (wheat bran) were utilized to provide carbon sources for the production of a pectinase by B. amyloliquefaciens TKU050. B. amyloliquefaciens TKU050 expressed the highest pectinase productivity (0.76 U/mL) on 0.5% wheat bran-containing medium at 37°C for four days. A 58 kDa pectinase was purified from the four-day cultured medium fermented under optimized culture conditions with 7.24% of a recovery ratio and 0.51 U/mg of specific activity, respectively. The optimum temperature, optimum pH, thermal stability, and pH stability of the TKU050 pectinase were 50 °C, pH 6, <50 °C, and pH 6–9, respectively. The TKU050 pectinase was inhibited by sodium dodecyl sulfate and Cu2+. The reducing sugar obtained by hydrolyzing banana peel with TKU050 pectinase showed the growth-enhancing effect on the growth of four tested lactic acid bacteria.
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Mulluye, Kelemu, Ameha Kebede, and Negussie Bussa. "Production and Optimization of Pectinase from Pectinolytic Fungi Cultivated on Mango peels and Pectin Subjected to Submerged Fermentation." Biology, Medicine, & Natural Product Chemistry 10, no. 1 (July 1, 2021): 15–21. http://dx.doi.org/10.14421/biomedich.2021.101.15-21.
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Pectinases are the group of enzymes that degrade pectin. This study was conducted with the aim of isolation of efficient pectinase producing pectinolytic fungi from the decomposing mango peels using extracted mango peels pectin as a growth substrate under submerged fermentation, determining optimum pectinase production conditions with regards to some physicochemical parameters. The organisms were screened for the production of pectinase using Pectin agar media, and the two active pectinolytic fungi (P1 and P2) were isolated. pectinase production media was later used for the Lab scale production of pectinase by inoculating p1 and p2 and incubating for 7 days. The enzyme was extracted after seven days of fermentation and every day tested for their pectinolytic activity. P2 showed relatively higher pectinolytic activity and was therefore used for further studies. P2 was inoculated into a broth containing mango pectin under submerged fermentation. Results indicate that a pectin yield of mango peel 17.75%. Different parameters optimization processes were investigated on submerged fermentation namely pH, incubation period, temperature and substrate concentration optima were found 6, 4 days, 35oC and 1.5% respectively. The result suggests that mango peels have high pectin content and can be used for the value-added synthesis of pectinase.
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Prodanovic, Jelena, and Mirjana Antov. "The influence of molecular weight of polyethylene glycol on separation and purification of pectinases from Penicillium cyclopium in aqueous two-phase system." Acta Periodica Technologica, no. 39 (2008): 193–99. http://dx.doi.org/10.2298/apt0839193p.
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In this study the possibility of the partitioning and purification of pectinases from Penicillium cyclopium by their partitioning in polymer/polymer and polymer/salt aqueous two-phase systems was investigated. In the system with 10% (w/w) polyethylene glycol 1500/5% (w/w) dextran 500 000/85% (w/w) crude enzyme, the highest values for partitioning parameters were achieved - the partition coefficient was 2.11, followed by the top phase yield of 85.68% and purification factor 1.28 for the endo-pectinase activity. The partition coefficient, yield in the top phase and purification factor for the exo-pectinase activity in the same system were 1.89, 84.28% and 3.82, respectively. In the system with 10% (w/w) polyethylene glycol 6000/15% (w/w) (NH4)2SO4/75% (w/w) crude enzyme purification factor 37.85 for exo-pectinase, and 19.52 for endo-pectinase in the bottom phase were obtained.
8
ONGARATTO, Ricardo Schmitz, and Luiz Antonio VIOTTO. "Efeito do tratamento enzimático sobre a viscosidade e os teores de fibra e pectina em suco de pitanga (Eugenia uniflora L.)." Brazilian Journal of Food Technology 18, no. 3 (September 2015): 231–38. http://dx.doi.org/10.1590/1981-6723.5514.
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Resumo O objetivo deste trabalho foi avaliar o efeito do tratamento enzimático, utilizando enzimas comerciais, sobre o comportamento reológico e o teor de fibras e pectina do suco de pitanga. Foram avaliadas diferentes combinações de pectinase (Pectinex Ultra SP-L) e celulase (Cellubrix-L), totalizando 0,1%, em massa, de enzima. Os resultados encontrados indicaram baixo valor de pectina (<0,003%) e significativa redução no teor de fibras após tratamento enzimático, sendo que a aplicação combinada de 0,025% de pectinase com 0,075% de celulase provocou a maior redução no teor de fibras e, consequentemente, menor viscosidade do suco. Ao mesmo tempo, uma aplicação igual ou superior a 0,05% de Pectinex Ultra SP-L foi necessária para resultar nas menores concentrações de pectina. A aplicação combinada de celulase e pectinase resultou em suco com menor viscosidade, cujo comportamento reológico foi próximo ao Newtoniano. No entanto, o modelo Lei da Potência seria o mais indicado para uso em modelagens matemáticas.
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Oumer, Oliyad Jeilu, and Dawit Abate. "Screening and Molecular Identification of Pectinase Producing Microbes from Coffee Pulp." BioMed Research International 2018 (2018): 1–7. http://dx.doi.org/10.1155/2018/2961767.
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Application of enzymes in biotechnological process has expanded considerably in recent years. In food and related industry, major importance was being attached to the use of enzymes in upgrading quality, increasing yields of extractive processes, product stabilization, and improvement of flavor and byproduct utilization. Pectinases or pectinolytic enzymes are today one of the upcoming enzymes of the commercial sector. It has been reported that microbial pectinases account for 25% of the global food enzymes sales. For this reason, this study was undertaken with aims of screening microorganisms for the pectinase activity from coffee pulp samples and molecular identification of the potential pectinolytic isolates. In the present investigation, in total, ninety-five (95) isolates were identified from thirty coffee pulp samples. Based on characterization on the selective growth media, the isolates were grouped as actinomycete (21.06%), bacteria (65.26%), and fungi (13.68%). Among these, 31.58% showed colonies surrounded by clear zones which indicate the presence of pectinase activity. After rigorous screening steps, the isolates with high potential pectinase activity were identified molecularly by sequencing 16S rDNA region of the isolates. Based on the molecular identifications, about 70% of the isolates are under genus Bacillus.
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-, Shilpa, Mandheer Kaur, and Yogita Jadon. "Isolation and Screening of Pectinase Producing Bacteria from Soil Sample." CGC International Journal of Contemporary Technology and Research 3, no. 2 (July 17, 2021): 166–70. http://dx.doi.org/10.46860/cgcijctr.2021.06.31.166.
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The vast majority of the industrial use of enzymes is covered from microorganisms. Microorganisms are favoured in industry because of their several advantages for example rapid growth, short life expectancy and simplicity in doing genetic alterations. Microbial enzymes are thus amply provided, very much standardized and promoted by many companies. Among various enzymes, Pectinases hold an exceptional place because of its different uses in various sectors like food, textile and biofuel industries.A total of 25% of total enzyme market is being shared by Pectinase alone.The current study was carried out to evaluate the pectinase activity of the pectinolytic bacteria. 40 Bacterial strains were isolated from different soil samples and screened for Pectinase production. Primary and Secondary screening showed 3 potential isolates I38 , I39 and I40 showing pectin degradation on Vincent’s media. Further, extracellular pectinase was partially purified by ammonium sulphate precipitation and dialysis. Sequential ammonium sulphate saturations from 20-80% i.e. (20, 40, 60 and 80%) showed 60% ammonium sulphate was optimum for precipitation of intracellular enzyme whereas 80% was optimum for extracellular enzyme.
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Berutu, Cocok Ana Maryani, Fahrurrozi Fahrurrozi, and Anja Meryandini. "Pectinase Production and Clarification Treatments of Apple (Malus Domestica) Juice." ANNALES BOGORIENSES 21, no. 2 (February 28, 2018): 63. http://dx.doi.org/10.14203/ab.v21i2.311.
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Pectinases are a group of an enzyme that break down pectin, a polysaccharide that is found in plant cell walls. Today, the application of pectinolytic enzymes plays an important role in food technology for the maceration of fruits and vegetables, including for the extraction and clarification of juice. This research aimed to produce pectinase enzyme for clarifying of apple juice. A microbial culture was selected from cocoa bean fermentation samples and identified as Bacillus sp.. The highest enzyme activity was investigated after 48 hours of incubation. Citrus pectin as the carbon source and peptone as the nitrogen source was found as the best component for pectinase production. The optimum condition of pectinase activity was observed at pH 5, temperature 40 °C and the crude enzyme had the higher activity at one hour storage. Apple juice was treated with the enzyme at different concentrations (0%, 0.5%, 1%, 2%, 4%). Apple juice clarification was evaluated for its percent clarity and viscosity. The result showed that enzyme treatment at 4% in apple juice promoted juice clarification and decreased pH and viscosity. In conclusion, the quality of apple juice can be improved by enzymatic treatment using pectinase.
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Berutu, Cocok Ana Maryani, Fahrurrozi Fahrurrozi, and Anja Meryandini. "Pectinase Production and Clarification Treatments of Apple (Malus Domestica) Juice." ANNALES BOGORIENSES 21, no. 2 (December 22, 2017): 63. http://dx.doi.org/10.14203/ann.bogor.2017.v21.n2.63-68.
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Pectinases are a group of an enzyme that break down pectin, a polysaccharide that is found in plant cell walls. Today, the application of pectinolytic enzymes plays an important role in food technology for the maceration of fruits and vegetables, including for the extraction and clarification of juice. This research aimed to produce pectinase enzyme for clarifying of apple juice. A microbial culture was selected from cocoa bean fermentation samples and identified as Bacillus sp.. The highest enzyme activity was investigated after 48 hours of incubation. Citrus pectin as the carbon source and peptone as the nitrogen source was found as the best component for pectinase production. The optimum condition of pectinase activity was observed at pH 5, temperature 40 °C and the crude enzyme had the higher activity at one hour storage. Apple juice was treated with the enzyme at different concentrations (0%, 0.5%, 1%, 2%, 4%). Apple juice clarification was evaluated for its percent clarity and viscosity. The result showed that enzyme treatment at 4% in apple juice promoted juice clarification and decreased pH and viscosity. In conclusion, the quality of apple juice can be improved by enzymatic treatment using pectinase.
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Antov, Mirjana, Draginja Pericin, and Stana Pejin. "Pectinases partitioning in aqueous two-phase systems: An integration of the systems poly(ethylene glycol)crude dextran and poly(ethylene glycol)ammonium sulphate." Journal of the Serbian Chemical Society 69, no. 4 (2004): 299–307. http://dx.doi.org/10.2298/jsc0404299a.
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The partitioning of pectinases in the poly(ethylene glucol)4000/ammonium sulpohate system was studied and also its application for enzymes extraction from the top phase of the poly(ethylene glucol)4000/crude dextran system. Almost complete one-sided partition of endo-pectinase and exo-pectinase to the bottom phase of the polymer/salt system was achieved at a tie-line length of 37.16 %. The concentration factors were 1.73 and 3.25, respectively. The highest total endo- and exo-pectinase yields (72.41 % and 69.46 % respectively) were obtained by integration of the polymer/polymer system at a tie-line of 8.61 % and a high phase volume ratio and the polymer/salt system at a tie-line of 30.23%and a low phase volume ratio. Integration of the partitioning at a high tie-line length in the polymer/polimer and a low tie-line length in the polymer/salt system resulted in a total concentration factor of 1.5 and a purification of 1.66 fold for exo-pectinase. The addition of phosphate to this integrated system improved the total concentration factor and purification fold of the activity to 1.73 and 2.14, respectively.
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Shrestha, Sarita, Janak Raj Khatiwada, Xiaodong Zhang, Chonlong Chio, Aristide Laurel Mokale Kognou, Feifei Chen, Sihai Han, Xuatong Chen, and Wensheng Qin. "Screening and Molecular Identification of Novel Pectinolytic Bacteria from Forest Soil." Fermentation 7, no. 1 (March 15, 2021): 40. http://dx.doi.org/10.3390/fermentation7010040.
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Pectinases are a group of enzymes with broad application, including in plant fiber processing, pectic wastewater treatment, paper pulping, fruit juice extraction, and clarification. With an increasing industrial demand for these enzymes, it is useful to isolate organisms that produce large amounts of pectinase and possess wide ranges of stability factors like temperature and pH. In this study, 17 out of 29 bacteria (58.62%) from forest soil samples were pectinolytic. However, only four bacteria (S-5, S-10, S-14, and S-17) showed high pectin hydrolysis zones (ranging from 0.2 cm to 1.7 cm). These four bacteria were identified based on colony morphology, microscopic characterization, biochemical characteristics, and 16S rDNA sequencing. They were designated as Streptomyces sp. (S-5, S-14), Cellulomonas sp. (S-10), and Bacillus sp. (S-17). Interestingly, bacteria showed cellulase and xylanase activity in addition to pectinase. The quantitative assay for pectinase activity of the four isolates provided proof that they are pectinase producers and can be considered potential candidates for industrial uses. The crude enzyme extracts of these bacteria are applicable in oil and juice extraction from sesame seeds and apples, respectively.
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KC, Sudeep, Jitendra Upadhyaya, Dev Raj Joshi, Binod Lekhak, Dhiraj Kumar Chaudhary, Bhoj Raj Pant, Tirtha Raj Bajgai, et al. "Production, Characterization, and Industrial Application of Pectinase Enzyme Isolated from Fungal Strains." Fermentation 6, no. 2 (June 9, 2020): 59. http://dx.doi.org/10.3390/fermentation6020059.
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Pectinases are the group of enzymes that catalyze the degradation of pectic substances. It has wide applications in food industries for the production and clarification of wines and juices. The aim of this study was to isolate, screen and characterize pectinase from fungi isolated from various soil samples and evaluate its application in juice clarification. Fungal strains were isolated and screened primarily using 1% citruspectin incorporated potato dextrose agar (PDA) and secondarily using pectinase screening agar medium (PSAM) for pectinolytic organisms. The enzyme was produced by submerged state fermentation and assayed using the dinitro salicylic acid (DNS) method. From 20 different soil samples, 55 fungal isolates were screened primarily and, among them, only 14 isolates were subjected for secondary screening. Out of 14, only four strains showed the highest pectinolytic activity. Among four strains, Aspergillus spp. Gm showed the highest enzyme production at a 48-h incubation period, 1% substrate concentration, and 30 °C temperature. The thermal stability assessment resulted that the activity of pectinase enzyme declines by 50% within 10 min of heating at 60 °C. The optimum temperature, pH, and substrate concentration for the activity of enzyme was 30 °C (75.4 U/mL), 5.8 (72.3 U/mL), and 0.5% (112.0 U/mL), respectively. Furthermore, the yield of the orange juice, the total soluble solid (TSS), and clarity (% transmittance) was increased as the concentration of the pectinase increased, indicating its potential use in juice processing. Overall, the strain Aspergillus spp. Gm was identified as a potent strain for pectinase production in commercial scale.
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Teixeira, Amito José, Leonardo Menoncin Weschenfelder, Angela Antunes, Jamile Zeni, Geciane Toniazzo Backes, and Rogério Luis Cansian. "Commercial and non-commercial pectinase and cellulase on the enzymatic hydrolysis efficacy of rice husk and Tifton 85 hay." Acta Scientiarum. Animal Sciences 41, no. 1 (April 8, 2019): 45100. http://dx.doi.org/10.4025/actascianimsci.v41i1.45100.
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The aim of this study was to evaluate the action of commercial and non-commercial cellulase and pectinase on rice husk and Tifton 85 hay hydrolyses. The hydrolysis kinetics of the substrates with commercial cellulase and pectinase were evaluated and the hydrolysis at different temperature and agitation conditions was maximized using experimental design. The combined use of commercial and non-commercial enzymes under optimized conditions was evaluated. The pre-treatment of the residues was also investigated by milling and different concentrations of NaOH. Finally, the effect of the hydrolysis on the bromatological composition of the residues was evaluated. The best hydrolysis times of rice husk and Tifton 85 hay were 10 and 12h for commercial cellulase, 12 and 14h for non-commercial cellulase, 10 and 14h for commercial pectinase and 16 and 20h for non-commercial pectinase, respectively. The highest hydrolysis values were obtained using commercial cellulase with 1:50 (w:v enzyme:water) dilution rate, at 45ºC and 300 rpm agitation for both substrates, reaching 20.6% maximum percentage for Tifton 85 hay and 11.6% for rice husk. The combined use of commercial enzymes did not increase hydrolysis percentage. The pre-treatment using 7.5% NaOH and 0.5 mm grain size significantly increased the rice husk and Tifton 85 hay hydrolyses (60-80%), either using commercial cellulase or pectinase enzymes. The use of non-commercial enzymes provided 18-30% hydrolysis obtained from commercial ones. Bromatological analyzes indicated a reduction in neutral detergent fiber and acid detergent fiber content for rice husk and Tifton 85 hay when using pectinases and commercial cellulases.
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Mohan, Nayana, and Archana Prabhat. "Isolation, Production and Application of Bacterial Pectinase for Industrial Use." Indian Journal of Nutrition and Dietetics 55, no. 4 (October 9, 2018): 442. http://dx.doi.org/10.21048/ijnd.2018.55.4.22116.
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Production of microbial enzymes at the industrial scale and their commercialization has gained a lot of focus and importance. Some of the industrially important enzymes from microbial origin include lipases, amylases, proteases, xylynases, pectinases etc. The objective of the study was production and application of bacterial pectinase for industrial use (clarification of fruit juices). Here the isolation of microorganism and characterization was done, then pectinase assay was performed and finally fruit juice was clarified using this enzyme. Here decayed orange peel was used as the sample and it was collected from a local market, South Kalamsseri- Cochin. The collected decayed orange part was subjected to serial dilution in order to isolate the organism. The dilutions were then plated on appropriate media (pecin agar media) and spread plate was performed. After the incubation time, colonies with zone were obtained which showed the production of pectinase enzyme. These isolated colonies were then inoculated to the petri plate containing pectin agar media and streak plate was performed. After 24 h incubation, the isolated colonies were subjected to Gram’s staining. It was Gram negative bacilli. The biochemical characterization (IMViC test) was done and VP Citrate tests were positive. Then the colonies were inoculated in Pectinase Production Broth. After 24 h incubation, the media was centrifuged for the isolation of enzymes. The enzyme assay was done by titration technique and the enzyme activity was found to be 0.78 U. This isolated enzyme was used for the clarification of apple juice and lime juice. According to the findings obtained from the study, the clarification of fruit juice by the use of bacterial pectinase is most cost effective and yield good results for industrial use.
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Gonzalez, Samantha Lemke, Regina Cristina Aparecida Lima, Eliana Beleski Borba Carneiro, Mareci Mendes de Almeida, and Neiva Deliberali Rosso. "Pectin methylesterase activity determined by different methods and thermal inactivation of exogenous pme in mango juice." Ciência e Agrotecnologia 35, no. 5 (October 2011): 987–94. http://dx.doi.org/10.1590/s1413-70542011000500017.
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Pectin methylesterase (PME) hydrolyzes methyl ester groups in pectin chains to form carboxylic groups, releasing methanol and H3O+. The aim of this study was to determine PME activity in samples of pectinases by UV-VIS spectroscopy, to measure the acid and methanol produced in the reaction of pectin with pectinase and to verify the thermal inactivation of exogenous PME in mango juice. The activity of PME in samples of pectinase was determined by potentiometry, UV-VIS spectroscopy, and by the action of alcohol oxidase. The reaction showed greater activity at pH 4.0 to 4.5 and at a temperature of 45° C. PME activity determined by UV-VIS spectroscopy with bromophenol blue indicator showed a good correlation with the activity determined by potentiometry and with alcohol oxidase. The results showed that bromophenol blue indicators can be used to determine PME activity in samples of pectinases where the optimum pH is located in the acidic range. The thermal inactivation of exogenous PME in mango juice occurred at 75° C for 20 min of exposure.
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BROWN, ROBERT L., ZHI-YUAN CHEN, THOMAS E. CLEVELAND, PETER J. COTTY, and JEFFERY W. CARY. "Variation in In Vitro α-Amylase and Protease Activity Is Related to the Virulence of Aspergillus flavus Isolates." Journal of Food Protection 64, no. 3 (March 1, 2001): 401–4. http://dx.doi.org/10.4315/0362-028x-64.3.401.
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Variation in the ability of Aspergillus flavus isolates to spread between cotton boll locules was previously shown to be at least partially related to variation in the production of a specific polygalacturonase (pectinase P2C). To determine if non-pectolytic hydrolase differences between low- and high-virulence isolates exist and, thus, could also potentially contribute to virulence differences, the present investigation was undertaken. Two A. flavus isolates, AF12 with low virulence and lacking pectinase P2C and AF13 with high virulence and producing pectinase P2C, were compared for production of nonpectolytic hydrolases after growth in 10% potato dextrose broth. Activity of amylases, cellulases, xylanases, and proteases was quantified using the radial diffusion/cup plate technique followed by differential staining. Culture filtrates also were subjected to native polyacrylamide gel electrophoresis. Both isolates produced amylases, proteases, and xylanases, whereas cellulases were not detected for either. AF13 produced more amylase than AF12, and this difference was supported by amylase isoform differences between isolates on native polyacrylamide gel electrophoresis gels. AF13 also produced more protease than AF12; however, isoform differences between isolates were inconclusive. These variations in other hydrolytic activities (besides pectinases)may contribute to virulence differences in cotton bolls between AF12 and AF13.
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Anele, Uchenna, Hossam Azzaz, Ahmed Kholif, Hussein Murad, Nasr El-Bordeny, Hossam Ebeid, and Noha Hassaan. "PSX-1 A newly developed pectinase from Aspergillus terreus enhanced feed utilization and milk production of Damascus goats fed pectin-rich diet." Journal of Animal Science 98, Supplement_4 (November 3, 2020): 451. http://dx.doi.org/10.1093/jas/skaa278.785.
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Abstract A newly developed pectinase from Aspergillus terreus was compared with a commercially available pectinase at 600 IU/kg feed. Thirty (one-week postpartum) Damascus goats stratified by previous milk production, body weight and parity were divided into three experimental treatments. Does were fed a basal diet containing concentrates, orange silage, sugar beet pulp and wheat straw at 50:20:20:10, respectively with (a newly developed pectinase or commercial pectinase) or without a supplement (control treatment). No difference (P >0.05) was noted for feed intake but the newly developed pectinase increased (P < 0.01) nutrient digestibility, diet nutritive value and milk production efficiency more than the other treatments. Out of all the blood parameters, only serum glucose was affected by the treatments with highest (P = 0.025) value noted for the new pectinase. Similarly, the new pectinase increased daily milk production (P < 0.005) and the concentrations of milk components compared to the other two treatments. Additionally, pectinase (both the commercial and new) inclusion increased (P < 0.05) the concentrations of total conjugated linoleic acid and unsaturated/saturated fatty acids ratio, and decreased atherogenic index (P = 0.01) compared with control treatment. It is concluded that the supplementation of the diet of lactating goats with pectinase at 600 IU/kg feed will enhance feed digestion and milk production. The newly developed pectinase performed better than the commercial pectinase.
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Anab-Atulomah, Chidiebere, and Ejikeme Nwachukwu. "Bio-Scouring of Cotton using Protease and Pectinase from Bacillus subtilis Isolated from Market Waste." Path of Science 7, no. 7 (July 31, 2021): 3001–6. http://dx.doi.org/10.22178/pos.72-3.
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The bio-scouring of cotton using protease and pectinase produced from Bacillus subtilis was investigated. Protease and pectinase were produced from Bacillus subtilis in a liquid medium using the submerged fermentation technique. Both enzymes were purified, and their scouring potential was tested on raw cotton fabrics. Pectinase was more effective than protease under optimised conditions. The optimum scouring temperature for both enzymes was between 40 °C and 50 °C, with pectinase bio-scoured fabric showing 15.5% weight loss while protease bio-scoured fabric had 14.3% weight loss. The optimum pH for pectinase scouring was pH 9 with 14.8% weight loss in the fabric, while the optimum pH for protease scoured fabric was pH 7 with 12.3% weight loss in fabric. After 120 minutes of bio-scouring, maximum weight loss was recorded for both pectinase and protease treated fabrics. The application of protease and pectinase for cotton fabric scouring revealed that they could be used as bio-scouring agents to treat textile materials.
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Abdullah, Roheena, Iqra Farooq, Afshan Kaleem, Mehwish Iqtedar, and Tehreema Iftikhar. "Pectinase production from Aspergillus niger IBT-7 using solid state fermentation." Bangladesh Journal of Botany 47, no. 3 (October 28, 2018): 473–78. http://dx.doi.org/10.3329/bjb.v47i3.38714.
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Different fungal strains were isolated from the local soil, fruits and vegetables on the basis of pectin hydrolysis. All the isolated strains were identified through microscopic studies and screened for pectinase production using solid state fermentation. The fungal strain identified as Aspergillus niger IBT-7 showed the highest pectinase production. The selected strain was further subjected to optimization through different physical and nutritional parameters to enhance the production of pectinase. Amongst seven different media tested M1 containing rice bran, moistened with Czapek’s nutrient medium showed the highest pectinase production. During optimization maximum pectinase production was achieved after 72 hrs of incubation at 30 ml of moisture content, pH 5.0 and 30°C. Xylose (1.5%) and yeast extract (1%) proved to be best supplemented carbon and nitrogen sources, respectively which gave the highest pectinase production (39.1 U/ml/min).
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Heidarizadeh, Mohammad, Parisa Fathi Rezaei, and Saleh Shahabivand. "Novel pectinase from Piriformospora indica, optimization of growth parameters and enzyme production in submerged culture condition." Turkish Journal of Biochemistry 43, no. 3 (January 24, 2018): 289–95. http://dx.doi.org/10.1515/tjb-2017-0192.
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AbstractBackground:Pectinases are one of the upcoming enzymes in food processing industries and they hydrolyze pectin substances.Objectives:This study was done to examine the production of pectinase byPiriformospora indicain submerged fermentation (SmF) along with growth parameters.Materials and methods:The fungusP. indicawas cultured on Kafer medium supplemented with pectin for 0–12 days and fungus growth, number of spores, total protein content, and pectinase activity were investigated.Results:Firstly, pectinase secretion byP. indicawas confirmed by cup-plate assay. The maximum dry cell weight (10.21 g/L), growth yield (0.65 g/g), specific growth rate (0.56 day−1) and pectinase activity (10.47 U/mL) on pectin containing medium (P+) were achieved after 6 day of culture. In the case of pectin free medium (P−) all the parameters were less than P+medium. The pectinase production byP. indicaon P+was 2.7 times higher than P−. The optimum pH and temperature for maximum polygalacturonase activity were 5 and 50°C, respectively.Conclusions:For the first time, the work confirmed pectinase secretion byP. indicafungus and it could be a good source for pectinase production. Moreover, optimum pH 5, make it a potential candidate for future application in fruit juice industries.
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GA, Mousa. "Fungal Pectinase Production Optimization and its Application in Buffaloe’s Diets Degradation." International Journal of Zoology and Animal Biology 3, no. 1 (2020): 1–12. http://dx.doi.org/10.23880/izab-16000199.
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Pectinase production for improving buffalo’s diets digestion is the main objective of this work. Effects of fungal strains and different cultivation conditions on pectinase production have been studied. In vitro batch culture technique was used for investigate impact of the produced pectinase compared with commercial pectinase (SMIZYME ® ) on rumen fermentation parameters and diet degradation. Penicillium chrysogenum exhibited the highest pectinase activity at 3 days of incubation period , initial pH 4 of the growth medium, yeast extract as a sole nitrogen source and pomegranate peel as a carbon source at a concentration of 15 % (W/V). Three (g/kg) of the both enzymes supplementation significantly increased treated diet’s dry matter (DM), neutral detergent fiber (NDF), acid detergent fiber (ADF) degradability with increase total gas production ( TGP) and short chain fatty acids (SCFA) concentration. The enlargement of pectinase production locally will lead to animal production improvement, encourage self-reliance and reduce the cost of enzymes importation.
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Vatanparast, M., V. Hosseininaveh, M. Ghadamyari, and S. Minoo Sajjadian. "Plant cell wall degrading enzymes, pectinase and cellulase, in the digestive system of the red palm weevil, Rhynchophorus ferrugineus (Coleoptera: Curculionidae)." Plant Protection Science 50, No. 4 (November 14, 2014): 190–98. http://dx.doi.org/10.17221/43/2013-pps.
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In digestion, the red palm weevil, Rhynchophorus ferrugineus, has been adapted to overcome the plant cell wall barrier, specially lignocellulosic and pectic compounds, by producing cellulase and pectinase enzymes. Partial biochemical characterisations of cellulase and pectinase were determined in the larval digestive system of the pest. Larval midgut extract showed an optimum activity for cellulase and pectinase against carboxyl methyl cellulose and pectin at pH 6.0 and 7.0, respectively. Larval midgut cellulase and pectinase were more stable at pH 4.0–8.0 and pH 6.0–8.0 than in highly acidic and alkaline condition, respectively. However, cellulase and pectinase showed to be more stable at pH 6.0 and 7.0, respectively, when the incubation time increased. Maximum activity for cellulase and pectinase incubated at different temperatures was observed at 50°C. Cellulase and pectinase activity significantly decreased in the presence of EDTA and SDS. On the contrary, Ca<sup>2+</sup>, Mg<sup>2+</sup>,and Na<sup>+</sup> significantly affect pectinase activity and K<sup>+</sup> did not affect the enzyme activities. Ca<sup>2+</sup> and Mg<sup>2+</sup> increased cellulase activity as well. K<sub>M </sub>and V<sub>max</sub> for pectinase activity were 0.92 mg/ml and 290 units/mg. Zymogram analyses revealed the presence of one form of pectin methyl esterase and one form of cellulase in the larval digestive system.
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Igbasan, F. A., W. Guenter, and B. A. Slominski. "The effect of pectinase and α-galactosidase supplementation on the nutritive value of peas for broiler chickens." Canadian Journal of Animal Science 77, no. 3 (September 1, 1997): 537–39. http://dx.doi.org/10.4141/a97-036.
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A total of 192 3-d-old male broiler chickens (Arbor Acres) were randomly assigned to six dietary treatments with eight replicates of four birds each per treatment. The treatments consisted of five levels (0, 50, 75, 100 and 125 U kg−1) of pectinase enzyme and a combination of pectinase (50 U kg−1) and α-galactosidase (6250 U kg−1) enzymes. The performance trial lasted for 2 wk. At the end of 2 wk, excreta were collected on three diets to determine nitrogen-corrected apparent metabolizable energy (AMEn). Growth rate, feed intake and feed conversion of birds fed pea diets supplemented with graded levels of pectinase enzyme were not different from their counterparts fed a diet without pectinase supplementation; however, growth rate tended to be improved (P = 0.11). Also, the AMEn values of these diets were not affected. Compared with the control diet, addition of a combination of pectinase and α-galactosidase tended to improve growth rate (P = 0.06). Key words: Peas, pectinase, α -galactosidase, broiler chicken
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Gupta, Ankita, Gaurav Tiwari, Ruchi Tiwari, Rishabh Srivastava, and A. K. Rai. "Enteric coated HPMC capsules plugged with 5-FU loaded microsponges: a potential approach for treatment of colon cancer." Brazilian Journal of Pharmaceutical Sciences 51, no. 3 (September 2015): 591–605. http://dx.doi.org/10.1590/s1984-82502015000300011.
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The work was aimed at developing novel enteric coated HPMC capsules (ECHC) plugged with 5 Florouracil (5-FU) loaded Microsponges in combination with calcium pectinate beads. Modified quasi-emulsion solvent diffusion method was used to formulate microsponges based on 32 factorial design and the effects of independent variables (volume of organic solvent and Eudragit RS100 content) on the dependent variables (Particle size, %EE & % CDR) were determined. The optimized microsponges (F4) were characterized by SEM, PXRD, TGA and were plugged along with calcium pectinate beads in HPMC capsules and the HPMC capsules were further coated with enteric polymer Eudragit L 100 (Ed-L100) and/ or Eudrgit S 100 (Ed-S 100) in different proportions. In vitro release study of ECHC was performed in various release media sequentially SGF for 2 h, followed by SIF for the next 6 h and then in SCF (in the presence and absence of pectinase enzyme for further 16 h). Drug release was retarded on coating with EdS-100 in comparison to blend of EdS-100: EdL-100 coating. The percentage of 5-FU released at the end of 24 h from ECHC 3 was 97.83 ± 0.12% in the presence of pectinase whereas in control study it was 40.08 ± 0.02% drug. The optimized formulation was subjected to in vivo Roentgenographic studies in New Zealand white rabbits to analyze the in vivo behavior of the developed colon targeted capsules. Pharmacokinetic studies in New Zealand white rabbits were conducted to determine the extent of systemic exposure provided by the developed formulation in comparison to 5-FU aqueous solutions. Thus, enteric coated HPMC capsules plugged with 5-FU loaded microsponges and calcium pectinate beads proved to be promising dosage form for colon targeted drug delivery to treat colorectal cancer.
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Yi, J., and Y. Ding. "Dual effects of whey protein isolates on the inhibition of enzymatic browning and clarification of apple juice." Czech Journal of Food Sciences 32, No. 6 (November 27, 2014): 601–9. http://dx.doi.org/10.17221/69/2014-cjfs.
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The inhibition was studied of enzymatic browning occurring in apple juice by whey protein isolates as compared to ascorbic acid and l-cysteine. A further comparison of different filter-aid pretreatments, such as whey protein isolates (WPI), pectinase and whey protein isolates – pectinase pretreatments, alone and combined with ultrafiltration was also made. The results indicated that WPI demonstrated a concentration-dependent inhibitory activity on polyphenoloxidase (PPO). At lower concentrations (0.005–0.01 g/l), the suppression effect of WPI on PPO activity was higher than that of both ascorbic acid and l-cysteine. WPI exhibited intermediate inhibition on PPO activity at the concentrations of 0.01–0.1 g/l, as compared to ascorbic acid and l-cysteine. The comparison of different clarification treatments suggested that WPI acted more effectively on clarification than pectinase. In addition, combined WPI-pectinase pretreatment significantly increased the clarity of apple juice, indicating a synergistic effect between WPI and pectinase. The subsequent ultrafiltration after WPI and pectinase pretreatments alone or combined could further improve the clarity and colour and reduce the turbidity of clear apple juice with non-significant influence on its typical characteristics.
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Islam, S., B. Feroza, AKMR Alam, and S. Begum. "Pectinase production by Aspergillus niger isolated from decomposed apple skin." Bangladesh Journal of Scientific and Industrial Research 48, no. 1 (June 22, 2013): 25–32. http://dx.doi.org/10.3329/bjsir.v48i1.15410.
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Pectinase activity among twelve different fungal strains, Aspergillus niger IM09 was identified as a potential one to produce maximal level 831 U/g at pH 4.0. Media composition, incubation temperature, incubation time, substrate concentration, aeration, inoculum size, assay temperature and nitrogen sources were found to effect pectinase activity. Moisture content did not affect the activity significantly. Media composition was varied to optimize the enzyme production in solid state fermentation. It was observed that the highest pectinase activity of 831.0 U/g was found to produce in presence of yeast extract as a nitrogen source in combination with ammonium sulfate in assay media. Aeration showed positive significant effects on pectinase production 755 U/g at 1000 ml flasks. The highest pectinase production was found at 2 g pectin (521 U/g) used as a substrate. Pectinolytic activity was found to have undergone catabolite repression with higher pectin concentration (205 U/g at 5 g pectin). The incubation period to achieve maximum pectinase activity by the isolated strain Aspergillus niger IM09 was 3 days, which is suitable from the commercial point of view. DOI: http://dx.doi.org/10.3329/bjsir.v48i1.15410 Bangladesh J. Sci. Ind. Res. 48(1), 25-32, 2013
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Degani, Ofir. "Synergism between Cutinase and Pectinase in the Hydrolysis of Cotton Fibers’ Cuticle." Catalysts 11, no. 1 (January 9, 2021): 84. http://dx.doi.org/10.3390/catal11010084.
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Scouring is one of the initial steps in the processing of natural textile fibers (e.g., cotton), performed to remove waxes and pectins, together with spinning oils and other impurities of the plant cell cuticle. Traditional chemical bleaching with boiling NaOH led to harsh removal of the entire fabric’s cuticle waxy layer accompanied by an unwanted alkaline waste. Extracellular lytic enzymes such as lipases, cellulases and pectinases play an essential role in host plant-pathogen interactions. They degrade the plant cuticle and tissue and enable pathogen invasion. Such enzymes, specifically cutinase and pectinase, have been considered potential bio-scouring agents to degrade the cotton fabric cuticle’s outer layer at low temperature and alleviate environmental pollution. In this work, the combined effect of cutinase, pectin lyase, or polygalacturonase on the scouring of cotton fabrics was studied using evaporative light-scattering reverse-phase HPLC and GC-MS analysis of the reaction components, and measuring changes in the cotton fabrics’ properties. The traditional method of cotton fabrics’ scouring with NaOH resulted in decreased pectin content and increased cellulose fibers accessibility, evaluated by specific staining. Treating the cotton fibers’ cuticle with cutinase led to the acidification of the reaction mixture, a decrease in enzyme-specific activity, and elevation in hexadecanoic acid and octadecanoic acids in the reaction fluid. These two saturated fatty acids are the main wax constituents of raw cotton fabrics, identified using GC-MS after dichloromethane reflux overnight. Treating cotton fabrics with each of the three enzymes, cutinase, pectin lyase, or polygalacturonase, increased their pectin removal, as measured by high concentrations of D-galacturonic acid and other pectin constituents in the reaction fluid. A synergistic effect was found in the combined treatment of cutinase and pectin lyase in the hydrolysis of the cotton fibers’ cuticle. This effect was expressed in high water absorbency of the treated fibers, increased fabric weight loss and sharp elevation of a cutin and pectin monomer’s related peaks (retention time [RT] = 4.1 min and 2.9, 4.5 min, respectively). A model was suggested for the synergistic action between cutinase and pectin lyase. It assumes that the cuticle’s digestion by cutinase results in the enlargement and formation of outer layer micropores, which enables the rapid penetration of pectinase into the inner pectin layer.
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Degani, Ofir. "Synergism between Cutinase and Pectinase in the Hydrolysis of Cotton Fibers’ Cuticle." Catalysts 11, no. 1 (January 9, 2021): 84. http://dx.doi.org/10.3390/catal11010084.
Full textAbstract:
Scouring is one of the initial steps in the processing of natural textile fibers (e.g., cotton), performed to remove waxes and pectins, together with spinning oils and other impurities of the plant cell cuticle. Traditional chemical bleaching with boiling NaOH led to harsh removal of the entire fabric’s cuticle waxy layer accompanied by an unwanted alkaline waste. Extracellular lytic enzymes such as lipases, cellulases and pectinases play an essential role in host plant-pathogen interactions. They degrade the plant cuticle and tissue and enable pathogen invasion. Such enzymes, specifically cutinase and pectinase, have been considered potential bio-scouring agents to degrade the cotton fabric cuticle’s outer layer at low temperature and alleviate environmental pollution. In this work, the combined effect of cutinase, pectin lyase, or polygalacturonase on the scouring of cotton fabrics was studied using evaporative light-scattering reverse-phase HPLC and GC-MS analysis of the reaction components, and measuring changes in the cotton fabrics’ properties. The traditional method of cotton fabrics’ scouring with NaOH resulted in decreased pectin content and increased cellulose fibers accessibility, evaluated by specific staining. Treating the cotton fibers’ cuticle with cutinase led to the acidification of the reaction mixture, a decrease in enzyme-specific activity, and elevation in hexadecanoic acid and octadecanoic acids in the reaction fluid. These two saturated fatty acids are the main wax constituents of raw cotton fabrics, identified using GC-MS after dichloromethane reflux overnight. Treating cotton fabrics with each of the three enzymes, cutinase, pectin lyase, or polygalacturonase, increased their pectin removal, as measured by high concentrations of D-galacturonic acid and other pectin constituents in the reaction fluid. A synergistic effect was found in the combined treatment of cutinase and pectin lyase in the hydrolysis of the cotton fibers’ cuticle. This effect was expressed in high water absorbency of the treated fibers, increased fabric weight loss and sharp elevation of a cutin and pectin monomer’s related peaks (retention time [RT] = 4.1 min and 2.9, 4.5 min, respectively). A model was suggested for the synergistic action between cutinase and pectin lyase. It assumes that the cuticle’s digestion by cutinase results in the enlargement and formation of outer layer micropores, which enables the rapid penetration of pectinase into the inner pectin layer.
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Yaqoob, Amna, Fatima Amanat, Asif Ali, and Muhammad Sajjad. "Isolation and Screening of Pectinolytic Bacterial Strains using Rotten Apples from Lahore, Pakistan." BioScientific Review 01, no. 03 (September 2019): 23–36. http://dx.doi.org/10.32350/bsr.0103.04.
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Pectinases are pectin degrading enzymes predominantly used as biocatalysts in various industries such as wine extraction, fruit juice extraction, and making of paper pulp. Large scale production of pectinases using biological systems (bacteria, fungi, plants) is a common method used in the industry. In the current study, different bacterial isolates obtained from rotten apples were used for pectinase production and their pectinolytic activity was investigated. Five bacterial strains were isolated on the growth medium containing 0.3% KH2PO4, 0.6% Na2HPO4, 0.2% NH4Cl, 0.5% NaCl, 1% Pectin, 1.5% Agar, 1mM CaCl2, and 10mM MgSO4. The isolates of five samples A, B, C, D and E were then biochemically characterized as Serratia marcescens, Klebseilla pneumoniea, Pseudomonas aeruginosa and Escherichia coli, respectively. They were also identified at the molecular level through 16S rRNA gene sequencing.
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Madika, Abubakar, Ulem Asagha Eugene, Musa Bishir, Mamunu Abdulkadir Sulaiman, and Ibrahim Mohammed Hussaini. "SCREENING OF ASPERGILLUS NIGER ISOLATED FROM SOIL FOR PECTINASE PRODUCTION." FUDMA JOURNAL OF SCIENCES 4, no. 2 (July 2, 2020): 244–49. http://dx.doi.org/10.33003/fjs-2020-0402-165.
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This study was conducted to screen for pectinase production by Aspergillus niger isolated from soil samples collected from three different locations within Ahmadu Bello University, Zaria, namely; botanical garden, refuse dump and sheep pen sites. A total of fifteen (15) soil samples were collected from different locations and used for isolation by a cultural method. Isolates suspected to be Aspergillus niger were further identified by microscopic examination of the lactophenol cotton blue stained-preparation and slide culture technique. The isolates were then screened in a pectin-containing medium for their pectinase activity. The isolates were further subjected to pectinase production using citrus pectin as the substrate under submerged fermentation conditions. Seven (7) isolates were confirmed to be Aspergillus niger with percentage occurrence of 60% each from sheep pen (SP) and refuse dumpsites (RD), and 20% from the botanical garden (BG). Aspergillus niger RD3 produced the highest zone of pectin hydrolysis (53 ± 1.1 mm) while isolate RD5 produced the lowest (35 ± 3.1 mm). Under submerged fermentation conditions, Aspergillus niger SP5 had the highest pectinase activity of 2.92 U/mL while isolate RD4 had the lowest pectinase activity of 1.29 U/mL. Aspergillus niger can be readily isolated from various soil types with the highest frequency in soils from sheep pen and refuse dumpsites. All the Aspergillus niger isolates demonstrated the potential for pectinase production. The study reveals the potential of various Aspergillus niger isolates from different soil in the production of pectinase.
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Sethi, Bijay, Amrita Satpathy, Subodh Tripathy, Sidarth Parida, Sameer Kumar Singdevsachan, and Bikash Behera. "Production of ethanol and clarification of apple juice by pectinase enzyme produced from Aspergillus terreus NCFT 4269.10." International Journal of Biological Research 4, no. 1 (May 22, 2016): 67. http://dx.doi.org/10.14419/ijbr.v4i1.6134.
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Aspergillus terreus NCFT 4269.10 was evaluated by liquid static surface fermentation (LSSF), shaking fermentation (ShF) and solid state fermentation (SSF) for the production of pectinase. Among various substrates tested, banana peels supported maximum production of pectinase i.e. 1000 ± 141.42 U/ml. The biomass of A. terreus was maximum with wheat bran (0.55±0.07g/50ml). Pectinase produced by A. terreus displayed higher specific activity when wheat bran was used as the sole source of carbon and energy. After successful fermentation, crude enzyme was purified to electrophoretic homogeneity with a specific activity of 1846.50 U/mg from an initial specific activity of 1282.05 U/mg. The cell free-dialyzed-enzyme containing 107100 U was purified to 1.44 fold with an overall enzyme yield of 35.70%.Immobilization study revealed that the production of pectinase was increased up to third cycle and decreased thereafter when further pectinase production was carried out by immobilized spores of A. terreus.
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Oumer, Oliyad Jeilu, and Dawit Abate. "Comparative Studies of Pectinase Production byBacillus subtilis strain Btk 27in Submerged and Solid-State Fermentations." BioMed Research International 2018 (December 4, 2018): 1–10. http://dx.doi.org/10.1155/2018/1514795.
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The request for enzymes in the global market is expected to rise at a fast pace in recent years. With this regard, there has been a great increase in industrial applications of pectinase owing to their significant biotechnological uses. This study was undertaken with main objectives of meeting the growing industrial demands of pectinase, by improving the yield without increasing the cost of production. In addition, this research highlights the underestimated potential of agroresidues for the production of biotechnologically important products. In this study, the maximum pectinase production attained was using wheat bran, among the tested agroresidues. The production of pectinase was improved from 10.1 ± 1.4 U/ml to 66.3 ± 1.2 U/ml in submerged fermentation whereas it was in solid state fermentation from 800.0 ± 16.2 U/g to 1272.4 ± 25.5 U/g. The maximum pectinase production was observed using YEP (submerged fermentation) and wheat bran (solid state fermentation) at initial pH of 6.5, at 37°C and by supplementing the medium with 3 mM MgSO4.7H2O.
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Belleri, L., E. Brunelli, M. Crippa, M. Golia, O. Vanoni, and L. Alessio. "Occupational exposure to pectinase." Allergy 57, no. 8 (August 2002): 755. http://dx.doi.org/10.1034/j.1398-9995.2002.23720.x.
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Lusihanne, Chrismita B., and Maria Herawati. "Effect of Concentration of Pectinase on Clarification and Ascorbic Acid of Lemon Ginger Drink." Jurnal Akademika Kimia 9, no. 3 (August 28, 2020): 133–38. http://dx.doi.org/10.22487/j24775185.2020.v9.i3.pp133-138.
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Lemon ginger drink is a herbal drink which contains many antioxidant and ascorbic acid that good for health. However, the murky appearance of the lemon ginger drink causes a lack of consumer interest especially young people in consuming this beverage. The murky in the lemon ginger drink is due to pectin content. Therefore, clarification is needed with the aid of a pectinase enzyme. The concentration of pectinase used in this study were 0; 0.04; 0.06; 0.08; 0.1; 0.1; and 0.12%; then incubated at 500 oC temperatures for 4 hours. The results showed that the proper concentration of pectinase in the clarification of lemon ginger drink was 0.08%. The concentration of the pectinase does not affect the ascorbic acid level of the lemon ginger drink.
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Gasani, Okta Novalia, Azizah Azizah, Siswanto Siswanto, Rudju Winarsa, and Kahar Muzakhar. "Pectinase Production by Using Coffee Pulp Substrate as Carbon and Nitrogen Source." Key Engineering Materials 884 (May 2021): 165–70. http://dx.doi.org/10.4028/www.scientific.net/kem.884.165.
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About thirty-five percent of coffee pulp waste is pectin. It may potentially be a source to be used in the bioprocessing industry. For example, it can be used as a substrate to produce pectinase from microorganisms under solid-state fermentation (SSF). In this investigation, an isolated fungus VTM4 with density 107 spores/mL was grown on coffee pulp medium-based, and after 0-168 hours incubation at 30 °C, pectinase activity was detected. The activity was measured based on reducing sugar released by crude pectinase against 0.5% alkali extract pectin substrate in 20 mM buffer acetate pH 5. The highest reducing sugar produced was 223.34 µg/mL after 72 hours of incubation at 30 °C. The optimum pH on enzyme activity was 4 with the maximum activity 0.747 U/mL and was stable (more than 80%) at a pH range of 4-5.5. The results revealed that the coffee substrate could be utilized as a carbon and nitrogen source to produce pectinase. Further research on purification and characterization of the enzyme to improve pectinase yield production was needed.
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Yulianti, Dyan, and Maria Marina Herawati. "Produksi Enzim Pektinase dari Limbah Kulit Pisang oleh Kapang Aspergillus niger dan Aplikasinya Terhadap Klarifikasi Minuman Fungsional Jahe Lemon." Jurnal Teknologi dan Industri Pertanian Indonesia 12, no. 2 (October 1, 2020): 86–92. http://dx.doi.org/10.17969/jtipi.v12i2.17891.
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Pectinase enzymes are commercial enzymes that can damage pectin by breaking down polygalacturonate acid into monogalacturonate acid through the release of glycosidic bonds. Pectinase enzymes can be produced from a variety of microorganisms, especially from types of mold such as Aspergillus niger using waste as a substrate like a banana peel. Lemon ginger drink is a functional beverage innovation made from ginger with the addition of lemon to add a refreshing sensation. However, the cloudy, pale, and sedimentary appearance in lemon ginger drink causes a lack of interest in consumers, especially young people. When consuming functional drinks such as lemon ginger, there is turbidity caused by polysaccharides such as pectin. Therefore, enzymatic clarification using pectinase is an effective way to reduce pectin in this drink. This study aims to find out the concentration of Aspergillus niger in producing pectinase enzymes from banana peel waste and its application to the clarification of lemon ginger drinks. The method used in this study was a randomized design group (RAK) consisting of 1 factor, the treatment of concentrations of Aspergillus niger 0 mL, 1 mL, 2 mL, 4 mL, and 6 mL. Then followed by the application of pectinase enzymes produced in the clarification of lemon ginger drink, concentration of 0%; 0,08%; 0,10%; 0,12%; 0,16%; 0,20%; and 0.24%. The Data obtained is analyzed using a printing analysis (ANOVA), and if there is influence, then proceed using BNJ test at a real level of 5%. The results showed that the concentration of Aspergillus niger suspension is best in producing pectinase enzymes of 6 mL, with the enzyme activity of 1.83 U/ml. Then the application of pectinase enzyme in the clarification of lemon ginger drink with a concentration of 0.16% better in improving lower clarity and viscosity of the resulting lemon ginger drink.
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Meena, B., V. G. Sowmeya, Archa B. Praveen, A. Swetha, D. Naga Sarath Chandra, and M. Kavitha. "Pectin Degradation in Fruit Juices by Pectinase from Meyerozyma sp. VITPCT75 Isolated from Phyllanthus emblica." Journal of Pure and Applied Microbiology 15, no. 2 (June 1, 2021): 926–35. http://dx.doi.org/10.22207/jpam.15.2.51.
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This study aimed to identify and characterize a pectinase-producing novel yeast from the fermented juice of Phyllanthus emblica and apply the enzyme for fruit juice clarification. Among the five pectinase-producing yeasts, isolate-1 exhibited the highest pectinase activity and was further used in this study. Based on morphological, physiological, and 18SrRNAanalyses, isolate-1 was recognized as a new strain sharing 99% sequence homology with other Meyerozyma strains and was thus designated as Meyerozyma sp. VITPCT75. The strain produced pectinase optimally at a temperature and pH of 25oC and 7, respectively. Maximum pectinase production was observed after 4-days incubation. The enzyme exhibited optimum activity at the temperature of 25 °C and pH 7.0. The enzyme was more stable at a temperature and pH of 20 °C and 7, respectively. Storage stability studies revealed that the enzyme was stable at -20 °C. The cell-free supernatant was partially purified using ammonium sulfate and solvent precipitation. Acetone at a concentration of 20% assured an adequate partial purification. The molecular weight of pectinase was determined as 6 kDa. The enzymatic metal ion preference-related studies revealed that Ca²z, Kz, Cu²z, Fe²z, and Ba²z ions enhanced, Ni²z ions moderately inhibited, and Mn²z ions intensely inhibited the enzymatic activity. Neither Na+ and Mg2+ ions nor EDTA affected the enzyme activity. When subjected to fruit juice clarification, the enzyme significantly reduced the viscosity of the juice.
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Mahto, Ram Balak, Mukesh Yadav, Soumya Sasmal, and Biswnath Bhunia. "Optimization of Process Parameters for Production of Pectinase using Bacillus Subtilis MF447840.1." Recent Patents on Biotechnology 13, no. 1 (February 1, 2019): 69–73. http://dx.doi.org/10.2174/1872208312666180917094428.
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Background: Pectinase enzyme has immense industrial prospects in the food and beverage industries. </P><P> Objective: In our investigation, we find out the optimum process parameters suitable for better pectinase generation by Bacillus subtilis MF447840.1 using submerged fermentation. </P><P> Method: 2% (OD600 nm = 0.2) of pure Bacillus subtilis MF447840.1 bacterial culture was inoculated in sterile product production media. The production media components used for this study were 1 g/l of pectin, 2 g/l of (NH4)2SO4, 1 g/l of NaCl, 0.25 g/l of K2HPO4, 0.25 g/l of KH2PO4 and 1 g/l of MgSO4 for pectinase generation. We reviewed all recent patents on pectinase production and utilization. The various process parameters were observed by changing one variable time method. </P><P> Results: The optimum fermentation condition of different parameters was noticed to be 5% inoculums, 25% volume ratio, temperature (37°C), pH (7.4) and agitation rate (120 rpm) following 4 days incubation. </P><P> Conclusion: Maximum pectinase generation was noticed as 345 ± 12.35 U following 4 days incubation.
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Li, Ming, Hong Xin Wang, Xin Sun, and Fu Ping Lu. "Research on Alkaline Pectinase for Hemp Degumming." Advanced Materials Research 821-822 (September 2013): 355–59. http://dx.doi.org/10.4028/www.scientific.net/amr.821-822.355.
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Alkaline pectinase has a broad application prospect in textile field. In hemp degumming, enzymatic degumming is preferred because of the better fiber quality and less environmental pollution. In this thesis, we used the recombinant strain Bacillus subtilis TCCC11485 constructed in our laboratory to express high-yield alkaline pectinase. The optimal conditions of the alkaline pectinase for hemp degumming were determined by single factor experiments as: bath ratio 1:36, pH 8, 45°C, enzyme activity 600 U/mL, degumming for 6 h. Under the above conditions, the residual gum content of fiber is 32.76%. Further, the scanning electron microscopy (SEM) was also used to compare quality of the hemp fibers produced by enzymatic-, chemical-degumming. The results showes that the fibers are in higher quality by alkaline pectinase degumming, suggesting the prospect of commercial applications in domestic textile industry.
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Liu, Guo Liang, Qi Lu Cui, Ruo Yao Ding, Zheng Fan Li, Xiao Min Zhong, and Chong Wen Yu. "Research on the Oxidation Degumming of Ramie with Alkaline Pectinase and Sodium Percarbonate." Applied Mechanics and Materials 121-126 (October 2011): 573–77. http://dx.doi.org/10.4028/www.scientific.net/amm.121-126.573.
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The application of the alkaline pectinase and sodium percarbonate in the degumming of ramie was studied in this paper. According to the tests such as the fiber fineness, the single fiber tenacity and the fiber surface properties, alkaline pectinase and sodium percarbonate on the properties of degummed ramie fiber was discussed. The results showed that the effect of the degumming of ramie was associated with temperature, concentration of alkaline pectinase, time and pH value. When the temperature is 60°C, the time is 3 hours, the concentration of alkaline pectinase is 3g/L and pH 8.5, the tenacity of fiber is the highest, the fineness is the finest. Due to the application of sodium percarbonate in the inactivation process, the properties of degummed ramie fiber have been further improved and the gum of the fiber surface has been further reduced.
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Robles, Castillo-Israel, and Lizardo. "Utilization of Cooking-type ‘Saba’ Banana in the Development of Ready-to-Drink Juice with Improved Quality and Nutritional Properties." Beverages 5, no. 2 (April 9, 2019): 31. http://dx.doi.org/10.3390/beverages5020031.
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The ‘Saba’ banana cultivar is one of the most abundantly grown fruit crops in the Philippines. However, large postharvest losses were posed due to the rapid deterioration and challenges in marketing. This study was conducted to develop a ready-to-drink (RTD) beverage using the cooking-type banana cultivar [Musa acuminata × balbisiana Colla (ABB Group) ‘Saba’]. The pulp was subjected to treatment with α-amylase and pectinase enzyme concentrations ranging from 0.25% to 1.00% to facilitate juice extraction. The effect of α-amylase and pectinase enzyme combinations on juice yield, color and clarity was determined. The highest juice yield (69.83%) and clarity (72.56% by transmittance at 660 nm) were achieved using 1.00% α-amylase: 1.00% pectinase and 0.5% α-amylase: 1.00% pectinase enzyme treatments, respectively. The juice treated with 0.5% α-amylase: 1.00% pectinase was used in the formulation of the RTD beverage. Physico-chemical and sensory properties of the product were analyzed. The developed RTD ‘Saba’ juice with acceptable sensory characteristics had 11.45 cP viscosity, 0.33% titratable acidity, 5.38% protein, 1660 ppm potassium, 40 ppm sodium and 460 ppm calcium. Results showed that the cooking-type banana cultivar ‘Saba’ can be utilized in the development of the RTD beverage with enhanced sensory and nutritional quality.
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Antov, Mirjana, Draginja Pericin, and Biljana Trbojevic. "The effect of sulphates on partitioning of pectinases in aqueous two-phase systems." Acta Periodica Technologica, no. 35 (2004): 179–86. http://dx.doi.org/10.2298/apt0435179a.
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The effect of various sulphate salts on the partitioning of endo-pectinase and exo-pectinase in aqueous two-phase systems, composed of polyethylene glycol and dextran, was studied. Presence of ammonium sulphate and sodium sulphate at concentration 15 mmol/l in the system polyethylene glycol 4000/crude dextran, at tie-line length 7.44%, increased partition coefficient of endo-pectinase 1.25 and 1.2 fold, respectively. Ammonium sulphate at 15 mmol/l and sodium sulphate at 5 mmol/l enhanced partition coefficient for exo-pectinase for about 60% in comparison to the system without salts. Addition of magnesium and sodium sulphate to a final concentration of 0.3 mmol/l in the system containing polyethylene glycol 6000/dextran 500 000, at tie-line length 6.26%, increased the partition coefficient of endo activity for 95% and 32%, respectively. Both salts at the same concentration increased partition coefficient of exo activity 1.5 and 3 times, respectively, in comparison to the system without salts.
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Channe, P. S., and J. G. Shewale. "Immobilization of pectinase fromSclerotium rolfsii." Folia Microbiologica 40, no. 1 (February 1995): 118–22. http://dx.doi.org/10.1007/bf02816535.
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Said, S., M. J. V. Fonseca, and V. Si�ssere. "Pectinase production by Penicillium frequentans." World Journal of Microbiology & Biotechnology 7, no. 6 (November 1991): 607–8. http://dx.doi.org/10.1007/bf00452841.
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Li, Zongquan, Qin Liu, Jiansong Chen, and Yingjuan Fu. "Enhancement of colloidal particle and lignin removal from pre-hydrolysis liquor by pectinase pre-treatment – Study on model substances." BioResources 14, no. 1 (November 26, 2018): 409–20. http://dx.doi.org/10.15376/biores.14.1.409-420.
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Removal of colloidal particle and lignin from pre-hydrolysis liquor (PHL) is important for the subsequent processing and utilization of the saccharides in the PHL. Cationic polymers treatment is a common method for the purpose, and pectinase pre-treatment of PHL can improve the efficiency of the treatment with cationic polymers. To investigate the mechanism of pectinase pre-treatment for improvement of the cationic polymer efficiency, polygalacturonic acid (PGA) was added in the colloidal lignin and dissolved lignin model substances systems, respectively, and the effects of polygalacturonic acid (PGA) and its pectinase pre-treatment on the removal of colloidal and dissolved lignin in the following cationic polymer treatment process were studied. The results showed that the presence of PGA caused the increase of negative charge density of the colloidal lignin and dissolved lignin systems, which lowered the efficiency of the cationic polymers and negatively affected the removal of both the colloidal lignin and the dissolved lignin. After pectinase treatment, the PGA present in the colloidal and dissolved lignin system was degraded and the negative effects on the cationic polymers were eliminated, and the efficiency of the cationic polymers was improved. Compared to the colloidal lignin and dissolved lignin systems with PGA, less cationic polymers were needed for the same systems with pectinase treatment to obtain the similar lignin removal level.
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Wan+g, Qiang, Xuerong Fan, Zhaozhe Hua, Weidong Gao, and Jian Chen. "Degradation kinetics of pectins by an alkaline pectinase in bioscouring of cotton fabrics." Carbohydrate Polymers 67, no. 4 (February 2007): 572–75. http://dx.doi.org/10.1016/j.carbpol.2006.06.031.
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Fatima, Mehreen, and Kainat Saeed. "Analysis and Estimation of Lycopene Extracted from Tomatoes." BioScientific Review 2, no. 2 (June 11, 2020): 23–32. http://dx.doi.org/10.32350/bsr/2020/22/717.
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Lycopene is a carotenoid without provitamin-A activity which functions as an important antioxidant. It is a carotenoid present in human blood and other tissues. The intake of dietary lycopene reduces the risk of many diseases such as eye diseases, diabetes, and cardiovascular diseases. Tomatoes are a major source of lycopene. This study aims at finding a suitable method of extraction and estimation of lycopene from tomatoes. Pectinase, pectinase and ultrasound waves, solid state extraction and spectrometric measurements were used for the said purpose. It was deduced that by using these methods a good quantity of active lycopene can be extracted from red and raw (green) tomatoes which can be used further for therapeutic purposes. These are fast methods to extract lycopene in which pectinase is also extracted simultaneously, thus reducing the cost of buying commercial pectinase. These methods can be used on a small and/or large scale for the preparation of therapeutic medicine as well as for waste management, since vegetable waste can also be used for lycopene extraction. Further alterations can also be made to increase the efficiency of lycopene extraction.