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1

Lévêque, Emmanuel, Štefan Janeček, Bernard Haye e Abdel Belarbi. "Thermophilic archaeal amylolytic enzymes". Enzyme and Microbial Technology 26, n. 1 (gennaio 2000): 3–14. http://dx.doi.org/10.1016/s0141-0229(99)00142-8.

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2

Bohdziewicz, Jolanta. "Ultrafiltration of technical amylolytic enzymes". Process Biochemistry 31, n. 2 (gennaio 1996): 185–91. http://dx.doi.org/10.1016/0032-9592(95)00047-x.

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3

DOYLE, EVELYN M., CATHERINE T. KELLY e WILLIAM M. FOGARTY. "The amylolytic enzymes of Penicillium amagasakiense". Biochemical Society Transactions 16, n. 2 (1 aprile 1988): 181–82. http://dx.doi.org/10.1042/bst0160181.

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Muller, Robert, e Evelyne Canterranne. "Activity of Amylolytic Enzymes in Thick Mashes". Journal of the American Society of Brewing Chemists 52, n. 2 (aprile 1994): 56–61. http://dx.doi.org/10.1094/asbcj-52-0056.

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Prado, Tayrone F., Aldi F. S. França, Maria Lúcia G. Meirinhos, Hugo J. M. C. Peron, Reginaldo N. Ferreira, Leonardo G. Oliveira e Daniel S. Corrêa. "Animal performance and carcass characteristics from confined lambs fed on concentrate feed and additives". Anais da Academia Brasileira de Ciências 87, n. 4 (30 ottobre 2015): 2255–63. http://dx.doi.org/10.1590/0001-3765201520140415.

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ABSTRACT The number of sheep flocks in Brazil is increasing. It is known that lambs must be slaughtered when young for producing quality meat. The current study evaluated the inclusion of protected methionine, protected lysine, lysophospholipid and amylolytic enzymes in a diet to lambs and their effects on weight gain and quantitative carcass traits at slaughtering. Eighty non-castrated male crossbred Dorper x Santa Inês lambs, 20.57 ± 4.33 kg live weight, were used. The feedlot lasted 64 days and 60 animals were slaughtered. There were no differences for live weight, daily feed intake, feed conversion and average daily weight gain at the first 28 days of feedlot. From the 28th day lysophospholipid treatment presented the highest live weight. Lysophospholipid and amylolytic enzyme presented the best performance in average daily gain, followed by protected methionine, control and protected lysine. Lysophospholipid treatment presented higher daily feed intake rates than protected lysine and protected methionine. Feed conversion was lower for amylolytic enzyme and higher for control. No changing in carcass traits was reported due to additives. Better performance may be achieved with feedlot lambs fed on diets with the addition of amylolytic enzyme and lysophospholipid at the finishing phase.
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Ona, John Ikuba, Peter J. Halling e Mercedes Ballesteros. "Enzyme hydrolysis of cassava peels: treatment by amylolytic and cellulolytic enzymes". Biocatalysis and Biotransformation 37, n. 2 (11 gennaio 2019): 77–85. http://dx.doi.org/10.1080/10242422.2018.1551376.

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7

Hagenimana, Vital, Ronald E. Simard e Louis-P. Vézina. "Amylolytic Activity in Germinating Sweetpotato (Ipomoea batatas L.) Roots". Journal of the American Society for Horticultural Science 119, n. 2 (marzo 1994): 313–20. http://dx.doi.org/10.21273/jashs.119.2.313.

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In vitro activity measurements indicate that storage sweetpotato roots contain high amounts of extractable amylolytic enzymes. These storage roots also have a very high starch content, a characteristic indicating that the in vitro measurements estimate potential amylolytic activity rather than actual physiological activity. We are interested in optimizing the use of endogenous amylases when processing sweetpotato roots and have undertaken a study to identify physiological parameters that control in vivo starch breakdown. Sweetpotato roots were allowed to germinate for 35 days in controlled conditions. Using a combination of in vitro activity measurements and immunochemical detection, the spatial distribution and changes in activity levels for the three major amylolytic enzymes in storage sweetpotato roots—α-amylase, β-amylase, and starch phosphorylase—have been followed. After 6 days, α-amylase protein increased in the outer starchy parenchymatous tissues surrounding the cambium layers, a result suggesting a de novo synthesis of the enzyme in cambium or laticifers layers. β-Amylase was abundant throughout the root at all times, and its high levels did not directly affect starch degradation rates. Starch phosphorylase protein level remained constant, while its extractable activity increased. Starch content decreased during sweetpotato seed root germination. However, the amount of starch that disappeared during germination was low compared with the calculated starch hydrolysis potential estimated by amylolytic activity measurements.
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8

Izyan, Nurul Syafiqa, Dg Nurdayana Azman, Nur Amalina Mohd Saad, Suhaila Mohd Sauid e Fazlena Hamzah. "Effect of Tacca Starch Loading on Production of Amylolytic Enzymes from Ragi Tapai". Materials Science Forum 987 (aprile 2020): 118–23. http://dx.doi.org/10.4028/www.scientific.net/msf.987.118.

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The study was done to determine the effect of Tacca starch loading on production of amylolytic enzyme from Ragi Tapai. In this study, Ragi Tapai was used as a starter to produce amylolytic enzyme. The fermentation was done in a solid state fermentation with the presence of Tacca leontopetaloides starch as the carbon source. The analysis of total sugar was conducted using DNS method and amylolytic enzyme was determined using Lowry method. The mixture was fermented and incubated for 24, 48, 72 and 96h. The result revealed that the optimum production of amylase was found at 48 h of incubation with amylase activity of 1.91 U/ml/min and 1.42 mg/ml for total protein. The study shows that increment amount of the Tacca starch in cultivation medium, increase the production of the amylase and total protein content. The highest enzyme activity was obtained at 4% of Tacca starch loading with amylase activity and total protein content of 2.14 U/ml/min and 1.42 mg/ml respectively. The study indicated that growth promoters in Tacca starch capable to enhance the activity of microbial consortium in Ragi Tapai for production of the amylolytic enzyme.
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9

Hamilton, Lynn M., Catherine T. Kelly e William M. Fogarty. "Review: cyclodextrins and their interaction with amylolytic enzymes". Enzyme and Microbial Technology 26, n. 8 (maggio 2000): 561–67. http://dx.doi.org/10.1016/s0141-0229(00)00141-1.

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10

Madi, E., G. Antranikian, K. Ohmiya e G. Gottschalk. "Thermostable Amylolytic Enzymes from a New Clostridium Isolate". Applied and Environmental Microbiology 53, n. 7 (1987): 1661–67. http://dx.doi.org/10.1128/aem.53.7.1661-1667.1987.

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11

Doyle, Evelyn M., Catherine T. Kelly e William M. Fogarty. "Production of the amylolytic enzymes of Penicillium expansum". Biochemical Society Transactions 19, n. 3 (1 agosto 1991): 270S. http://dx.doi.org/10.1042/bst019270s.

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12

Wojciechowski, Piotr M., Antoni Koziol e Andrzej Noworyta. "Iteration model of starch hydrolysis by amylolytic enzymes". Biotechnology and Bioengineering 75, n. 5 (2001): 530–39. http://dx.doi.org/10.1002/bit.10092.

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13

Zahovic, Ida, Zorana Roncevic, Jovana Grahovac, Sinisa Dodic, Aleksandar Jokic e Jelena Dodic. "The effect of cultivation technique on enzymes production from sugar beet pulp by Neurospora crassa". Acta Periodica Technologica, n. 50 (2019): 338–45. http://dx.doi.org/10.2298/apt1950338z.

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This study is concerned with the effect of different cultivation techniques on enzymes production from sugar beet pulp by strain Neurospora crassa isolated from the environment. Cultivation of selected producing microorganism was carried out under the same process conditions using five techniques. Bioprocess efficacy was estimated based on amylolytic, cellulolytic and xylanolytic activity of prepared enzymes mixtures. The obtained results indicate that the selection of cultivation technique had a statistically significant effect on the production of examined hydrolytic enzymes. It was confirmed that solid state cultivation with spontaneous aeration is the best cultivation technique for the production of amylolytic, cellulolytic and xylanolytic enzymes from sugar beet pulp by Neurospora crassa. Submerged cultivation of producing strain with spontaneous aeration resulted in the lowest production of all investigated enzymes under applied experimental conditions. The obtained results are the basis for further research aimed to increase the enzymes yield and activity of their mixture.
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Rahman, Fatur, Ismiati Ismiati e Arbai Nurhasanah. "Distribusi Bakteri Penghasil Enzim Ekstraseluler Pada Saluran Pencernaan Lobster Mutiara (Panulirus ornatus)". JURNAL SAINS TEKNOLOGI & LINGKUNGAN 5, n. 2 (26 dicembre 2019): 71. http://dx.doi.org/10.29303/jstl.v5i2.129.

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The activity of the digestive function of animals is influenced by the secretion of extracellular enzymes from bacteria in the digestive tract. This study aims to evaluate the distribution of bacteria producing protease enzyme, amylase and lipase from the digestive tract of pearl lobster, Panulirus ornatus. Bacterial isolates that have extracellular enzyme activity are based on their ability to form clear zones in the test media. The results showed that of 51 bacterial isolates from the digestive tract of P. ornatus, proteolytic bacteria were 27.45%, amylolytic bacteria were 23.53% and lipolytic bacteria were 21.77%. Based on bacterial dominance in the gastrointestinal segment, namely the cardiac, piloric and intestinal sections, it was dominated by amylolytic bacteria at 33.33%, proteolytic at 37.50% and lipolytic at 29.41%. The activity of proteolytic, amylolytic and lipolytic bacteria based on the highest clear zone diameter was achieved respectively by SP5 isolates of 12 mm, SK10 isolates of 21 mm and SU15 isolates of 20 mm. The three bacterial isolates were potential as probiotic aquacultur candidates
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Gęsicka, Aleksandra, Monika Borkowska, Wojciech Białas, Paulina Kaczmarek e Ewelina Celińska. "Production of Raw Starch-Digesting Amylolytic Preparation in Yarrowia lipolytica and Its Application in Biotechnological Synthesis of Lactic Acid and Ethanol". Microorganisms 8, n. 5 (12 maggio 2020): 717. http://dx.doi.org/10.3390/microorganisms8050717.

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Sustainable economy drives increasing demand for raw biomass-decomposing enzymes. Microbial expression platforms exploited as cellular factories of such biocatalysts meet requirements of large-volume production. Previously, we developed Yarrowia lipolytica recombinant strains able to grow on raw starch of different plant origin. In the present study, we used the most efficient amylolytic strain as a microbial cell factory of raw-starch-digesting (RSD) amylolytic preparation composed of two enzymes. The RSD-preparation was produced in fed-batch bioreactor cultures. Concentrated and partly purified preparation was then tested in simultaneous saccharification and fermentation (SSF) processes with thermotolerant Kluyveromyces marxianus for ethanol production and Lactobacillus plantarum for production of lactic acid. These processes were conducted as a proof-of-concept that application of the novel RSD-preparation supports sufficient starch hydrolysis enabling microbial growth and production of targeted molecules, as the selected strains were confirmed to lack amylolytic activity. Doses of the preparation and thermal conditions were individually adjusted for the two processes. Additionally, ethanol production was tested under different aeration strategies; and lactic acid production process was tested in thermally pre-treated substrate, as well. Conducted studies demonstrated that the novel RSD-preparation provides satisfactory starch hydrolyzing activity for ethanol and lactic acid production from starch by non-amylolytic microorganisms.
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16

Crabb, Douglas W., e Jay Shetty. "Improving the Properties of Amylolytic Enzymes by Protein Engineering". Trends in Glycoscience and Glycotechnology 15, n. 82 (2003): 115–26. http://dx.doi.org/10.4052/tigg.15.115.

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17

Guzmán‐Maldonado, Horacio, Octavio Paredes‐López e Costas G. Biliaderis. "Amylolytic enzymes and products derived from starch: A review". Critical Reviews in Food Science and Nutrition 35, n. 5 (settembre 1995): 373–403. http://dx.doi.org/10.1080/10408399509527706.

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18

Park, Yong K., e Edna H. Azuma. "Screening of yeast strains capable of hyperproducing amylolytic enzymes". Biotechnology Letters 12, n. 5 (maggio 1990): 373–76. http://dx.doi.org/10.1007/bf01024434.

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19

Ciesarová, Zuzana, Daniela Šmogrovičová, Ján Šajbidor e Peter Magdolen. "Characterization of yeast amylolytic enzymes by HPLC maltooligosaccharides determination". Biotechnology Techniques 9, n. 12 (dicembre 1995): 869–72. http://dx.doi.org/10.1007/bf00158538.

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20

González, C. F., J. I. Fariña e L. I. C. de Figueroa. "Optimized amylolytic enzymes production in Saccharomycopsis fibuligera DSM-70554". Enzyme and Microbial Technology 42, n. 3 (febbraio 2008): 272–77. http://dx.doi.org/10.1016/j.enzmictec.2007.10.005.

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Kabachyi, P. I., e T. V. Kortunova. "Enzymes of the amylolytic complex in germinating wheat seeds". Chemistry of Natural Compounds 24, n. 5 (1988): 640. http://dx.doi.org/10.1007/bf00633399.

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22

Korompokis, Konstantinos, Niels De Brier e Jan A. Delcour. "Differences in endosperm cell wall integrity in wheat (Triticum aestivum L.) milling fractions impact on the way starch responds to gelatinization and pasting treatments and its subsequent enzymatic in vitro digestibility". Food & Function 10, n. 8 (2019): 4674–84. http://dx.doi.org/10.1039/c9fo00947g.

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23

Cheawchanlertfa, Pattsarun, Sawannee Sutheeworapong, Piroon Jenjaroenpun, Thidathip Wongsurawat, Intawat Nookaew, Supapon Cheevadhanarak, Akihiko Kosugi et al. "Clostridium manihotivorum sp. nov., a novel mesophilic anaerobic bacterium that produces cassava pulp-degrading enzymes". PeerJ 8 (16 novembre 2020): e10343. http://dx.doi.org/10.7717/peerj.10343.

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Background Cassava pulp is a promising starch-based biomasses, which consists of residual starch granules entrapped in plant cell wall containing non-starch polysaccharides, cellulose and hemicellulose. Strain CT4T, a novel mesophilic anaerobic bacterium isolated from soil collected from a cassava pulp landfill, has a strong ability to degrade polysaccharides in cassava pulp. This study explored a rarely described species within the genus Clostridium that possessed a group of cassava pulp-degrading enzymes. Methods A novel mesophilic anaerobic bacterium, the strain CT4T, was identified based on phylogenetic, genomic, phenotypic and chemotaxonomic analysis. The complete genome of the strain CT4T was obtained following whole-genome sequencing, assembly and annotation using both Illumina and Oxford Nanopore Technology (ONT) platforms. Results Analysis based on the 16S rRNA gene sequence indicated that strain CT4T is a species of genus Clostridium. Analysis of the whole-genome average amino acid identity (AAI) of strain CT4T and the other 665 closely related species of the genus Clostridium revealed a separated strain CT4T from the others. The results revealed that the genome consisted of a 6.3 Mb circular chromosome with 5,664 protein-coding sequences. Genome analysis result of strain CT4T revealed that it contained a set of genes encoding amylolytic-, hemicellulolytic-, cellulolytic- and pectinolytic enzymes. A comparative genomic analysis of strain CT4T with closely related species with available genomic information, C. amylolyticum SW408T, showed that strain CT4T contained more genes encoding cassava pulp-degrading enzymes, which comprised a complex mixture of amylolytic-, hemicellulolytic-, cellulolytic- and pectinolytic enzymes. This work presents the potential for saccharification of strain CT4T in the utilization of cassava pulp. Based on phylogenetic, genomic, phenotypic and chemotaxonomic data, we propose a novel species for which the name Clostridium manihotivorum sp. nov. is suggested, with the type strain CT4T (= TBRC 11758T = NBRC 114534T).
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Oluoch, Kevin Raymond, Patrick Wafula Okanya, Rajni Hatti-Kaul, Bo Mattiasson e Francis Jakim Mulaa. "Protease-, Pectinase- and Amylase- Producing Bacteria from a Kenyan Soda Lake". Open Biotechnology Journal 12, n. 1 (30 aprile 2018): 33–45. http://dx.doi.org/10.2174/1874070701812010033.

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Background:Alkaline enzymes are stable biocatalysts with potential applications in industrial technologies that offer high quality products.Objective:The growing demand for alkaline enzymes in industry has enhanced the search for microorganisms that produce these enzymes.Methods:Eighteen bacterial isolates from Lake Bogoria, Kenya, were screened for alkaline proteases, pectinases and amylases; characterized and subjected to quantitative analysis of the enzymes they produced.Results:The screening analysis ranked 14, 16 and 18 of the bacterial isolates as potent producers of alkaline proteases, pectinases and amylases, respectively. The isolates were classified into two groups: Group 1 (16 isolates) were facultatively alkaliphilicB. haloduranswhile group 2 (2 isolates) were obligately alkaliphilicB. pseudofirmus. Further analysis revealed that group 1 isolates were divided into two sub-groups, with sub-group I (4 isolates) being a phenotypic variant sub-population of sub-group II (12 isolates). Variation between the two populations was also observed in their enzymatic production profilese.g. sub-group I isolates did not produce alkaline proteolytic enzymes while those in sub-group II did so (0.01-0.36 U/ml). Furthermore, they produced higher levels of the alkaline pectinolytic enzyme polygalacturonase (0.12-0.46 U/ml) compared to sub-group II isolates (0.05-0.10 U/ml), which also produced another pectinolytic enzyme - pectate lyase (0.01 U/ml). No clear distinction was however, observed in the production profiles of alkaline amylolytic enzymes by the isolates in the two sub-populations [0.20-0.40 U/ml (amylases), 0.24-0.68 U/ml (pullulanases) and 0.01-0.03 U/ml (cyclodextrin glycosyl transferases)]. On the other hand, group 2 isolates were phenotypically identical to one another and also produced similar amounts of proteolytic (0.38, 0.40 U/ml) and amylolytic [amylases (0.06, 0.1 U/ml), pullulanases (0.06, 0.09 U/ml) and cyclodextrin glycosyl transferases (0.01, 0.02 U/ml)] enzymes.Conclusion:The facultatively alkaliphilicB. haloduransand obligately alkaliphilicB. pseudofirmusisolates are attractive biotechnological sources of industrially important alkaline enzymes.
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Ranwala, Anil P., e William B. Miller. "307 Characterization of Amylolytic Activities of Tulip Bulb Scales". HortScience 34, n. 3 (giugno 1999): 495D—495. http://dx.doi.org/10.21273/hortsci.34.3.495d.

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Amylolytic activities extracted from scales of tulip (Tulipa gesneriana L. cv. Apeldoorn) bulbs stored at 4 °C for 6 weeks under moist conditions were characterized. Anion exchange chromatography of enzyme extract on DEAE-Sephacel revealed three peaks of amylolytic activity. Three enzymes showed different electrophoretic mobilties on nondenaturing polyacrylamide gels. The most abundant amylase activity was purified extensively with phenyl-agarose chromatography, gel filtration on Sephacryl S-200, and chromatofocusing on polybuffer exchanger PBE 94. The purified amylase was determined to be an endoamylase based on substrate specificity and end product analysis. The enzyme had a pH optimum of 6.0 and a temperature optimum of 55 °C when soluble starch was used as the substrate. The apparent Km value for soluble starch was 1.28 mg/ml. The inclusion of 2 mM CaCl2 in the reaction mixture resulted in a 1.4-fold increase in the enzyme activity. The presence of calcium ions also enhanced the thermo-stability of the enzyme at higher temperatures. The enzyme was able to hydrolyze soluble starch, amylose, amylopectin, and beta-limit dextrin, but it had no activity against pullulan, inulin, maltose, or p-nitrophenyl alpha-glucopyranoside. Only maltooligosaccharides, having a degree of polymerization of 7 or more, were hydrolyzed to a significant extent by the enzyme. Exhaustive hydrolysis of soluble starch with the enzyme yielded a mixture of maltose and matlooligosaccharides. This amylase activity was not inhibited by alpha- or beta-cyclodextrin upto a concentration of 10 mM. Maltose at a 50 mM concentration partially inhibited the enzyme activity, whereas glucose had no effect at that concentration.
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Putri, Redila Aprilivia, Nursyirwani Nursyirwani e Feliatra Feliatra. "ABILITY OF AMILOLYTIC BACTERIA (Bacillus paramycoides and Enterobacter cloacae) IN DEGRADING ORGANIC MATERIALS OF MANGROVE LITTLE". Asian Journal of Aquatic Sciences 4, n. 2 (23 agosto 2021): 98–105. http://dx.doi.org/10.31258/ajoas.4.2.98-105.

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This study aims to find out that Bacillus paramycoides and Enterobacter cloacae bacteria can produce amylase enzymes and have the ability to degrade organic matter, especially mangrove litter. From this study it was found that the optimal growth of B.paramycoides and E. cloacae bacteria occurred at 12th hour. The results of measurements and calculations of absorbance values ​​at 630 10.238 x 108 cells/mL (B. paramycoides) and 12.030 x 108 cells/mL (E. cloacae) using the spectrophotometric method. Meanwhile, with the TPC method at 12 hours, the number of bacterial cells was 2.08 x 108 CFU's/ml (B. paramycoides) and 2.44 x 108 CFU's/ml (E. cloacae). The ability to produce the largest amylolytic bacterial amylase enzyme also occurred at 12 hours as much as 0.306 mg/mL (B.paramycoides) with an increase of 0.046 mg/mL and 0.243 mg/mL (E. cloacae) with an increase of 0.028 mg/mL. The bacteria that have the highest amylase enzyme ability is E.cloacae as evidenced by the diameter of the clear zone of 10.10 mm. Testing the ability of amylolytic bacteria in degrading mangrove litter was carried out by adding amylase enzyme as much as 0%, 50% and 100%. Amylolytic bacteria can degrade organic matter by hydrolyzing starch contained in mangrove litter. The most degraded starch content was in the 100% enzyme treatment, which was 1.021 mg/mL (B. paramycoides) and 1.189 mg/mL (E.cloacae).
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Hmidet, Noomen, Ali Bougatef e Moncef Nasri. "Fish Amylolytic Enzymes: Biochemical Characterization and Application for Oligosaccharides Production". Natural Products Journal 3, n. 2 (1 maggio 2013): 125–30. http://dx.doi.org/10.2174/2210315511303020007.

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Chen, Wanping, Ting Xie, Yanchun Shao e Fusheng Chen. "Phylogenomic Relationships between Amylolytic Enzymes from 85 Strains of Fungi". PLoS ONE 7, n. 11 (15 novembre 2012): e49679. http://dx.doi.org/10.1371/journal.pone.0049679.

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SORRIVAS, V., D. B. GENOVESE e J. E. LOZANO. "EFFECT OF PECTINOLYTIC AND AMYLOLYTIC ENZYMES ON APPLE JUICE TURBIDITY". Journal of Food Processing and Preservation 30, n. 2 (28 marzo 2006): 118–33. http://dx.doi.org/10.1111/j.1745-4549.2006.00054.x.

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Kuek, C., e D. K. Kidby. "Determination of Glucoamylase in Culture Filtrates Containing Other Amylolytic Enzymes". Starch - Stärke 37, n. 5 (1985): 161–62. http://dx.doi.org/10.1002/star.19850370505.

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Gašperík, Juraj, Ľubomír Kováč e Olga Mináriková. "Purification and characterization of the amylolytic enzymes of Saccharomycopsis fibuligera". International Journal of Biochemistry 23, n. 1 (gennaio 1991): 21–25. http://dx.doi.org/10.1016/0020-711x(91)90004-7.

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Saha, Badal C., Robert W. Silman e rodney J. Bothast. "Amylolytic enzymes produced by a color variant strain ofAureobasidium pullulans". Current Microbiology 26, n. 5 (maggio 1993): 267–73. http://dx.doi.org/10.1007/bf01575916.

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McMullan, P. M., M. C. Therrien e J. Noll. "Effect of diclofop and HOE-6001 on amylolytic enzyme activities of malt". Canadian Journal of Plant Science 72, n. 2 (1 aprile 1992): 435–38. http://dx.doi.org/10.4141/cjps92-049.

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Research was conducted to determine the effect of diclofop or HOE-6001 on barley alpha-amylase level and diastatic power of malt from seven barley genotypes. Neither herbicide consistently decreased alpha-amylase level or diastatic power of barley malt. However, alpha-amylase level of the genotype Manley was decreased by all herbicide treatments in 1989. Results indicate that these herbicides should not affect the enzyme potential of barley.Key words: Diclofop, HOE-6001, amylolytic enzymes, alpha-amylase, diastatic power
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JANDEROVÁ, B., F. PŮTA e O. BENDOVÁ. "Utilization of yeasts producing amylolytic enzymes and preparations of new strains." Kvasny Prumysl 35, n. 7 (1 luglio 1989): 208–10. http://dx.doi.org/10.18832/kp1989029.

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Guerra, Nelson P., e Lorenzo Pastrana Castro. "Modelling the Effects of Ageing Time of Starch on the Enzymatic Activity of Three Amylolytic Enzymes". Scientific World Journal 2012 (2012): 1–13. http://dx.doi.org/10.1100/2012/402439.

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The effect of increasing ageing time (t) of starch on the activity of three amylolytic enzymes (Termamyl, San Super, and BAN) was investigated. Although all the enzymatic reactions follow michaelian kinetics,vmaxdecreased significantly (P<0.05) andKMincreased (although not always significantly) with the increase int. The conformational changes produced in the starch chains as a consequence of the ageing seemed to affect negatively the diffusivity of the starch to the active site of the enzymes and the release of the reaction products to the medium. A similar effect was observed when the enzymatic reactions were carried out with unaged starches supplemented with different concentrations of gelatine [G]. The inhibition in the amylolytic activities was best mathematically described by using three modified forms of the Michaelis-Menten model, which included a term to consider, respectively, the linear, exponential, and hyperbolic inhibitory effects oftand [G].
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36

Gandra, J. R., E. R. Oliveira, C. S. Takiya, T. A. Del Valle, F. P. Rennó, R. H. T. B. Goes, R. S. R. Leite et al. "Amylolytic activity and chemical composition of rehydrated ground maize ensiled with α-amylase or glucoamylase". Journal of Agricultural Science 157, n. 5 (luglio 2019): 449–55. http://dx.doi.org/10.1017/s0021859619000698.

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Abstract (sommario):
AbstractA completely randomized experiment was designed to evaluate the effects of α-amylase (AMY) and glucoamylase (GLU) on total losses, fermentative profile, chemical composition and amylolytic activity of rehydrated maize. Eighty-four experimental silos of rehydrated maize [0.33 litres/kg ground maize, 4-mm theoretical particle size, and 625 g/kg dry matter (DM)] were assigned to the following treatments: (1) control (CON), no enzyme addition; (2) GLU added at 300 µl/kg of ground maize (as-fed); and (3) AMY added at 300 µl/kg of ground maize. Seven silos from each treatment were opened after 7, 14, 21 and 28 days. Differences among treatments were evaluated through orthogonal contrasts (CON v. enzymes, and AMY v. GLU). Time effects were decomposed using polynomial regression. Glucoamylase silage exhibited greater total losses than AMY. Enzymes increased acetate and lactic acid concentrations and decreased ethanol concentration. Regardless of treatment, gas, effluent and total fermentative losses linearly increased, whereas DM recovery linearly decreased with higher storage length. Glucoamylase silage had lower ammonia nitrogen and higher lactic acid concentrations than AMY. Enzyme treatments decreased silage neutral detergent fibre content and increased in vitro DM degradation. Glucoamylase silage exhibited a more moderate starch content and greater in vitro DM degradation than AMY. Storage time linearly decreased DM, starch and fibre content of rehydrated maize. In vitro degradation of DM linearly increased as the storage length increased. This study showed evidence that enzymes with amylolytic activity, particularly GLU, improve the fermentative profile and DM degradation of rehydrated maize silage.
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37

Rodríguez-Saavedra, Carolina, Romina Rodríguez-Sanoja, Daniel Guillén, Carmen Wacher e Gloria Díaz-Ruiz. "Streptococcus infantarius 25124 isolated from pozol produces a high molecular weight amylopullulanase, a key enzyme for niche colonization". Amylase 5, n. 1 (1 gennaio 2021): 1–12. http://dx.doi.org/10.1515/amylase-2021-0001.

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Abstract (sommario):
Abstract Pozol is a beverage made with maize dough that is prepared after boiling the kernels in limewater, causing a decrease in soluble sugars, with starch being the main fermentable carbohydrate in the dough. Previously, Streptococcus infantarius ssp. infantarius 25124 (Sii-25124) was identified as the most amylolytic bacteria isolated in this product. Analysis of Sii-25124 amylolytic enzymes revealed two amylases, a cytoplasmic α-amylase of 55.7 kDa and an extracellular amylopullulanase of 246.3 kDa, with two catalytic domains, one typical of an α-amylase and another typical of a pullulanase/glycogen debranching enzyme. Characterization of the joint activity of both enzymes using Sii-25124 cell lysate supernatant demonstrated stability between 30 °C and 45°C, and pH stability in a range between 6.8 and 8.0. The joint activity of Sii-25124 amylases showed a fast production of reducing sugars when starch was used as the substrate. In contrast, reducing sugar production from amylopectin was lower, but it steadily increased throughout the reaction time. The amylopullulanase produced by Sii-25124 hydrolyzes the starch in the dough to produce low molecular weight oligosaccharides, which may be transported into Sii-25124 cells, so that intracellular α-amylase hydrolyzes them to mono- and disaccharides. Amylopullulanase production by Sii-25124 could be an example of a specialized enzyme that successfully dominates starchy food fermentation.
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38

Andrade, Carolina M. M. C., Nei Pereira Jr. e Garo Antranikian. "Extremely thermophilic microorganisms and their polymer-hidrolytic enzymes". Revista de Microbiologia 30, n. 4 (dicembre 1999): 287–98. http://dx.doi.org/10.1590/s0001-37141999000400001.

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Abstract (sommario):
Thermophilic and hyperthermophilic microorganisms are found as normal inhabitants of continental and submarine volcanic areas, geothermally heated sea-sediments and hydrothermal vents and thus are considered extremophiles. Several present or potential applications of extremophilic enzymes are reviewed, especially polymer-hydrolysing enzymes, such as amylolytic and hemicellulolytic enzymes. The purpose of this review is to present the range of morphological and metabolic features among those microorganisms growing from 70oC to 100°C and to indicate potential opportunities for useful applications derived from these features.
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39

Xu, Ya, Cheng-Heng Liao, Li-Li Yao, Xu Ye e Bang-Ce Ye. "GlnR and PhoP Directly Regulate the Transcription of Genes Encoding Starch-Degrading, Amylolytic Enzymes in Saccharopolyspora erythraea". Applied and Environmental Microbiology 82, n. 23 (16 settembre 2016): 6819–30. http://dx.doi.org/10.1128/aem.02117-16.

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Abstract (sommario):
ABSTRACTStarch-degrading enzymes hydrolyze starch- and starch-derived oligosaccharides to yield glucose. We investigated the transcriptional regulation of genes encoding starch-degrading enzymes in the industrial actinobacteriumSaccharopolyspora erythraea. We observed that most genes encoding amylolytic enzymes (one α-amylase, one glucoamylase, and four α-glucosidases) were regulated by GlnR and PhoP, which are global regulators of nitrogen and phosphate metabolism, respectively. Electrophoretic mobility shift assays and reverse transcription-PCR (RT-PCR) analyses demonstrated that GlnR and PhoP directly interact with their promoter regions and collaboratively or competitively activate their transcription. Deletion ofglnRcaused poor growth on starch, maltodextrin, and maltose, whereas overexpression ofglnRandphoPincreased the total activity of α-glucosidase, resulting in enhanced carbohydrate utilization. Additionally, transcript levels of amylolytic genes and total glucosidase activity were induced in response to nitrogen and phosphate limitation. Furthermore, regulatory effects of GlnR and PhoP on starch-degrading enzymes were conserved inStreptomyces coelicolorA3(2). These results demonstrate that GlnR and PhoP are involved in polysaccharide degradation by mediating the interplay among carbon, nitrogen, and phosphate metabolism in response to cellular nutritional states. Our study reveals a novel regulatory mechanism underlying carbohydrate metabolism, and suggests new possibilities for designing genetic engineering approaches to improve the rate of utilization of starch in actinobacteria.IMPORTANCEThe development of efficient strategies for utilization of biomass-derived sugars, such as starch and cellulose, remains a major technical challenge due to the weak activity of associated enzymes. Here, we found that GlnR and PhoP directly regulate the transcription of genes encoding amylolytic enzymes and present insights into the regulatory mechanisms of degradation and utilization of starch in actinobacteria. Two nutrient-sensing regulators may play important roles in creating a direct association between nitrogen/phosphate metabolisms and carbohydrate utilization, as well as modulate the C:N:P balance in response to cellular nutritional states. These findings highlight the interesting possibilities for designing genetic engineering approaches and optimizing the fermentation process to improve the utilization efficiency of sugars in actinobacteria via overexpression of theglnRandphoPgenes and nutrient signal stimulation.
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40

Zainal ariffin, Zaidah. "Aspergillus sydowii Strain SCAU066 and Aspergillus versicolor Isolate BAB-6580: Potential Source of Xylanolytic, Cellulolytic and Amylolytic Enzymes". Science Letters 14, n. 2 (1 giugno 2020): 15. http://dx.doi.org/10.24191/sl.v14i2.9539.

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Abstract (sommario):
Fungi is known to produce a wide range of biologically active metabolites and enzymes. Enzymes produced by fungi are utilized in food and pharmaceutical industries because of their rich enzymatic profile. Filamentous fungi are particularly interesting due to their high production of extracellular enzymes which has a large industrial potential. The aim of this study is to isolate potential soil fungi species that are able to produce functional enzymes for industries. Five Aspergillus species were successfully isolated from antibiotic overexposed soil (GPS coordinate of N3.093219 E101.40269) by standard microbiological method. The isolated fungi were identified via morphological observations and molecular tools; polymerase chain reactions, ITS 1 (5’- TCC GTA GGT GAA CCT GCG G3’) forward primer and ITS 4 (5’-TCC TCC GCT TAT TGA TAT GC-3’) reverse primer. The isolated fungi were identified as Aspergillus sydowii strain SCAU066, Aspergillus tamarii isolate TN-7, Aspergillus candidus strain KUFA 0062, Aspergillus versicolor isolate BAB-6580, and Aspergillus protuberus strain KAS 6024. Supernatant obtained via submerged fermentation of the isolated fungi in potato dextrose broth (PDB) and extracted via centrifugation was loaded onto specific media to screen for the production of xylanolytic, cellulolytic and amylolytic enzymes. The present findings indicate that Aspergillus sydowii strain SCAU066 and Aspergillus versicolor isolate BAB-6580 have great potential as an alternative source of xylanolytic, cellulolytic and amylolytic enzymes.
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41

Sills, A. Michael, Chandra J. Panchal, Inge Russell e Graham G. Stewart. "Production of Amylolytic Enzymes by Yeasts and Their Utilization in Brewing". Critical Reviews in Biotechnology 5, n. 2 (gennaio 1987): 105–15. http://dx.doi.org/10.3109/07388558709086971.

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42

Klingerman, C. M., W. Hu, E. E. McDonell, M. C. DerBedrosian e L. Kung. "An evaluation of exogenous enzymes with amylolytic activity for dairy cows". Journal of Dairy Science 92, n. 3 (marzo 2009): 1050–59. http://dx.doi.org/10.3168/jds.2008-1339.

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43

Legin, Estelle, Christine Ladrat, Anne Godfroy, Georges Barbier e Francis Duchiron. "Thermostable amylolytic enzymes of thermophilic microorganisms from deep-sea hydrothermal vents". Comptes Rendus de l'Académie des Sciences - Series III - Sciences de la Vie 320, n. 11 (novembre 1997): 893–98. http://dx.doi.org/10.1016/s0764-4469(97)80874-8.

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44

Annous, B. A., e H. P. Blaschek. "Regulation and localization of amylolytic enzymes in Clostridium acetobutylicum ATCC 824." Applied and Environmental Microbiology 56, n. 8 (1990): 2559–61. http://dx.doi.org/10.1128/aem.56.8.2559-2561.1990.

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45

Jensen, Bo, Jorgen Olsen e Knud Allermann. "Purification of extracellular amylolytic enzymes from the thermophilic fungus Thermomyces lanuginosus". Canadian Journal of Microbiology 34, n. 3 (1 marzo 1988): 218–23. http://dx.doi.org/10.1139/m88-041.

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Abstract (sommario):
When grown in static culture it appears as if Thermomyces lanuginosus has a biphasic secretion of the extracellular starch-degrading activity. This could be due to the presence of at least two different amylases. By ion-exchange chromatography on DEAE-Trisacryl an α-amylase (EC 3.2.1.1) and a glucoamylase (EC 3.2.1.3) were separated and purified from the extracellular protein from 14-day-old static cultures grown on soluble starch. The hydrolysis of soluble starch by the purified glucoamylase resulted in only glucose as the end product, whereas the α-amylase gave maltose as the smallest end product. The molecular weights and isoelectric points of the enzymes were for glucoamylase 70 000 – 76 000 and pH 4.0, and for α-amylase 54 000 – 57 000 and pH 3.4. An α-glucosidase (EC 3.2.1.20) with a molecular weight of 44 000 – 48 000 and an isoelectric point at pH 3.8 was eluted close to the α-amylase fraction on the DEAE-Trisacryl column.
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46

Rempel, Alan, Tainara Machado, Helen Treichel, Eliane Colla, Ana Cláudia Margarites e Luciane Maria Colla. "Saccharification of Spirulina platensis biomass using free and immobilized amylolytic enzymes". Bioresource Technology 263 (settembre 2018): 163–71. http://dx.doi.org/10.1016/j.biortech.2018.04.114.

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47

Rodrigues, Éllen Francine, Aline Matuella Moreira Ficanha, Rogério Marcos Dallago, Helen Treichel, Christian Oliveira Reinehr, Tainara Paula Machado, Greice Borges Nunes e Luciane Maria Colla. "Production and purification of amylolytic enzymes for saccharification of microalgal biomass". Bioresource Technology 225 (febbraio 2017): 134–41. http://dx.doi.org/10.1016/j.biortech.2016.11.047.

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48

Giuberti, Gianluca, Gabriele Rocchetti e Luigi Lucini. "Interactions between phenolic compounds, amylolytic enzymes and starch: an updated overview". Current Opinion in Food Science 31 (febbraio 2020): 102–13. http://dx.doi.org/10.1016/j.cofs.2020.04.003.

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49

Farias, Ticiane Carvalho, Haroldo Yukio Kawaguti e Maria Gabriela Bello Koblitz. "Microbial amylolytic enzymes in foods: Technological importance of the Bacillus genus". Biocatalysis and Agricultural Biotechnology 35 (agosto 2021): 102054. http://dx.doi.org/10.1016/j.bcab.2021.102054.

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50

Okunwaye, T., P. O. Uadia, B. O. Okogbenin, E. A. Okogbenin, D. C. Onyia e J. U. Obibuzor. "Amylase-Producing Fungi and Bacteria Associated with Some Food Processing Wastes". Nigerian Journal of Biotechnology 38, n. 1 (27 luglio 2021): 74–82. http://dx.doi.org/10.4314/njb.v38i1.9.

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Abstract (sommario):
Amylases are enzymes that catalyze the hydrolysis of glycosidic bonds present in starch to release simple sugars. They are one of the most important enzymes in numerous commercial processes. In this investigation, fungal and bacterial strains from the following agro-industrial wastes were isolated and screened for amylolytic ability: soil from oil palm plantation, shea seed, date fruit, coconut meat, cassava effluent, cassava peel, cassava tubers, yam and potato tubers, starch medium, parboiled water from noodles and rice. The results revealed the presence of Geotrichum, Aspergillus, Penicillium, Trichoderma, Rhizopus and Fusarium spp. Five major genera of bacterial species namely Corynebacterium, Pseudomonas, Lactobacillus, Micrococcus and Bacillus were isolated and screened for amylase activity. Cassava soil had the highest heterotrophic bacterial count of 5.7 x105cfu/g and coconut meat waste had the lowest heterotrophic bacterial count of 1.3 x105cfu/g. All isolated microorganisms had the amylolytic ability. The fungal isolates had higher amylase activity when compared with the bacterial isolates. This investigation reveals organisms with high amylase activity.
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