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Articoli di riviste sul tema "Cellulose"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 25 luglio 2025

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1

Deng, Yijie, and Shiao Y. Wang. "Sorption of Cellulases in Biofilm Enhances Cellulose Degradation by Bacillus subtilis." Microorganisms 10, no. 8 (2022): 1505. http://dx.doi.org/10.3390/microorganisms10081505.

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Biofilm commonly forms on the surfaces of cellulosic biomass but its roles in cellulose degradation remain largely unexplored. We used Bacillus subtilis to study possible mechanisms and the contributions of two major biofilm components, extracellular polysaccharides (EPS) and TasA protein, to submerged biofilm formation on cellulose and its degradation. We found that biofilm produced by B. subtilis is able to absorb exogenous cellulase added to the culture medium and also retain self-produced cellulase within the biofilm matrix. The bacteria that produced more biofilm degraded more cellulose c

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2

Kumar, Amit. "Dissolving pulp production: Cellulases and xylanases for the enhancement of cellulose accessibility and reactivity." Physical Sciences Reviews 6, no. 5 (2021): 111–29. http://dx.doi.org/10.1515/psr-2019-0047.

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Abstract Dissolving pulps are high-grade cellulose pulps that have minimum amount of non-cellulosic impurities. Dissolving pulps are the basic source for the manufacturing of several cellulosic products such as viscose, lyocell, cellulose acetates, cellulose nitrates, carboxymethyl-cellulose, etc. Dissolving pulps are mainly manufactured by pre-hydrolysis kraft and acid sulphite pulping. A high reactivity of dissolving pulps is desirable for its eco-friendly utilization for several purposes. Several approaches including mechanical, chemical, ultrasonic, and enzymatic treatments have been emplo

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3

Hetzler, Stephan, Daniel Bröker, and Alexander Steinbüchel. "Saccharification of Cellulose by Recombinant Rhodococcus opacus PD630 Strains." Applied and Environmental Microbiology 79, no. 17 (2013): 5159–66. http://dx.doi.org/10.1128/aem.01214-13.

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ABSTRACTThe noncellulolytic actinomyceteRhodococcus opacusstrain PD630 is the model oleaginous prokaryote with regard to the accumulation and biosynthesis of lipids, which serve as carbon and energy storage compounds and can account for as much as 87% of the dry mass of the cell in this strain. In order to establish cellulose degradation inR. opacusPD630, we engineered strains that episomally expressed six different cellulase genes fromCellulomonas fimiATCC 484 (cenABC,cex,cbhA) andThermobifida fuscaDSM43792 (cel6A), thereby enablingR. opacusPD630 to degrade cellulosic substrates to cellobiose

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4

Hall, J., G. W. Black, L. M. A. Ferreira, et al. "The non-catalytic cellulose-binding domain of a novel cellulase from Pseudomonas fluorescens subsp. cellulosa is important for the efficient hydrolysis of Avicel." Biochemical Journal 309, no. 3 (1995): 749–56. http://dx.doi.org/10.1042/bj3090749.

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A genomic library of Pseudomonas fluorescens subsp. cellulosa DNA, constructed in lambda ZAPII, was screened for carboxymethyl-cellulase activity. The pseudomonad insert from a recombinant phage which displayed elevated cellulase activity in comparison with other cellulase-positive clones present in the library, was excised into pBluescript SK- to generate the plasmid pC48. The nucleotide sequence of the cellulase gene, designated celE, revealed a single open reading frame of 1710 bp that encoded a polypeptide, defined as endoglucanase E (CelE), of M(r) 59663. The deduced primary structure of

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5

Brumm, Phillip, Phillip Brumm, Dan Xie, et al. "Hydrolysis of Cellulose by Soluble Clostridium Thermocellum and Acidothermus Cellulolyticus Cellulases." Journal of Enzymes 1, no. 1 (2018): 5–19. http://dx.doi.org/10.14302/issn.2690-4829.jen-18-2025.

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The goal of this work was to clone, express, characterize and assemble a set of soluble thermostablecellulases capable of significantly degrading cellulose. We successfully cloned, expressed, and purified eleven Clostridium thermocellum (Cthe) cellulases and eight Acidothermuscellulolyticus(Acel) cellulases. The performance of the nineteen enzymes was evaluated on crystalline (filter paper) and amorphous (PASC) cellulose. Hydrolysis products generated from these two substrates were converted to glucose using beta-glucosidase and the glucose formed was determined enzymatically. Ten of the eleve

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6

Chatterjee, Soumya, Sonika Sharma, Rajesh Kumar Prasad, et al. "Cellulase Enzyme based Biodegradation of Cellulosic Materials: An Overview." South Asian Journal of Experimental Biology 5, no. 6 (2016): 271–82. http://dx.doi.org/10.38150/sajeb.5(6).p271-282.

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Cellulose, a macromolecule of β -D- anhydroglucopyranose units linked by β (1,4)-glycosidic bonds, is the world’s most abundant organic polymer and is the main component of plant biomass that provides stability. Due to its sta-ble fibrous property, it has become one of the most important commercial raw materials for many industries. However, accumulation of waste cellulose due to natural and/or anthropogenic sources is a matter of concern in terms of environmental pollution. Wastes cellulosic substrates can be utilized as sources of energy through controlled hydrolysis using cellulases- a comp

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7

Pratama, Rahadian, I. Made Artika, Tetty Chaidamsari, Herti Sugiarti, and Soekarno Mismana Putra. "Isolation and Molecular Cloning of Cellulase Gene from Bovine Rumen Bacteria." Current Biochemistry 1, no. 1 (2017): 29–36. http://dx.doi.org/10.29244/cb.1.1.29-36.

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Cellulases are the enzymes that hydrolyze cellulosic biomass and are produced by the microorganisms that grow over cellulosic matters. The objective of this research was to isolate and clone cellulase gene from cellulose-degrading bacteria of bovine rumen. Cellulose-degrading bacteria was isolated from rumen fluid using a selective medium. Total RNA was isolated from selected colony having cellulose degrading activity and was used as a template for cDNA construction using reverse transcriptase polymerase chain reaction (RT-PCR) technique. The resulted cDNA was employed as a template for PCR am

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8

Maji, Poulami, Megha Maji, Paramita Ghosh, and Prashant Shukla. "Cellulase-producing Microorganisms from Diverse Ecosystem: A Review." UTTAR PRADESH JOURNAL OF ZOOLOGY 46, no. 2 (2025): 25–38. https://doi.org/10.56557/upjoz/2025/v46i24760.

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Cellulose is the most abundant organic matter present on the planet. It is made up of glucose molecules which is the ultimate energy currency. Still, cellulose is utilized by most the animals as energy source as they lack necessary enzymes for degradation of the molecule. The animals who are able to utilize cellulose based materials as source of energy are able to do so due to cellulase producing gut microflora. Cellulases are enzymes which are used by certain organisms to breakdown the cellulose. Very small number of organisms are able to produce different types of cellulases which can break

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9

Li, Xia, Xiaoyan Geng, Lu Gao, et al. "Optimized expression of a hyperthermostable endoglucanase from Pyrococcus horikoshii in Arabidopsis thaliana." BioResources 14, no. 2 (2019): 2812–26. http://dx.doi.org/10.15376/biores.14.2.2812-2826.

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Manufacturing microbial cellulase in plants is an attractive strategy for the cost-effective production of cellulosic ethanol, especially the expression of thermostable cellulase, which causes no negative effects on plant growth and development. The beta-1,4-endogenous cellulase from Pyrococcus horikoshii (EGPh) is considered one of the most promising glycosyl hydrolase in the biofuel and textile industry for its hyperthermostability and its capability to hydrolyze crystalline celluloses, which has been researched extensively during recent years. In this study, the coding sequence of EGPh was

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10

Mizuno, Masahiro, Shuji Kachi, Eiji Togawa, et al. "Structure of Regenerated Celluloses Treated with Ionic Liquids and Comparison of their Enzymatic Digestibility by Purified Cellulase Components." Australian Journal of Chemistry 65, no. 11 (2012): 1491. http://dx.doi.org/10.1071/ch12342.

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In this study, regenerated celluloses were prepared from microcrystalline cellulose (MCC) by treatment with three ionic liquids (ILs) having 1-ethyl-3-methylimidazolium (Emim) as the cation, and the IL N-(2-methoxyethyl)-N,N-diethyl-N-methylammonium alanine ([N221ME][Ala]), where the amino acid moiety is the anion. The crystal form of cellulose was transformed from cellulose I to cellulose II by dissolution with an IL and regeneration with anti-solvent. However, the crystallinity of the regenerated cellulose was different; the disordered chain region was increased in the order of [N221ME][Ala]

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11

Bu, Yingjie, Bassam Alkotaini, Bipinchandra K. Salunke, Aarti R. Deshmukh, Pathikrit Saha, and Beom Soo Kim. "Direct ethanol production from cellulose by consortium of Trichoderma reesei and Candida molischiana." Green Processing and Synthesis 8, no. 1 (2019): 416–20. http://dx.doi.org/10.1515/gps-2019-0009.

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Abstract Industrial cellulosic ethanol production is a challenge due to the high cost of cellulases for hydrolysis when lignocellulosic materials are used as feedstock. In this study, direct ethanol production from cellulose was performed by consortium of Trichoderma reesei and Candida molischiana. Cellulose was hydrolyzed by a fully enzymatic saccharification process using Trichoderma reesei cellulases. The produced reducing sugar was further utilized by Candida molischiana for ethanol production. Because the optimal temperature for the cellulase system is approximately 50°C, the effect of te

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12

Lynd, Lee R., Paul J. Weimer, Willem H. van Zyl, and Isak S. Pretorius. "Microbial Cellulose Utilization: Fundamentals and Biotechnology." Microbiology and Molecular Biology Reviews 66, no. 3 (2002): 506–77. http://dx.doi.org/10.1128/mmbr.66.3.506-577.2002.

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SUMMARY Fundamental features of microbial cellulose utilization are examined at successively higher levels of aggregation encompassing the structure and composition of cellulosic biomass, taxonomic diversity, cellulase enzyme systems, molecular biology of cellulase enzymes, physiology of cellulolytic microorganisms, ecological aspects of cellulase-degrading communities, and rate-limiting factors in nature. The methodological basis for studying microbial cellulose utilization is considered relative to quantification of cells and enzymes in the presence of solid substrates as well as apparatus a

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13

Kashcheyeva, Ekaterina I., Yulia A. Gismatulina, Galina F. Mironova, et al. "Properties and Hydrolysis Behavior of Celluloses of Different Origin." Polymers 14, no. 18 (2022): 3899. http://dx.doi.org/10.3390/polym14183899.

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The present paper is a fundamental study on the physicochemical properties and hydrolysis behavior of cellulose samples differing in origin: bacterial, synthetic, and vegetal. Bacterial cellulose was produced by Medusomyces gisevii Sa-12 in an enzymatic hydrolyzate derived from oat-hull pulp. Synthetic cellulose was obtained from an aqueous glucose solution by electropolymerization. Plant-based cellulose was isolated by treatment of Miscanthus sacchariflorus with dilute NaOH and HNO3 solutions. We explored different properties of cellulose samples, such as chemical composition, degree of polym

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14

Tokuda, Gaku, and Hirofumi Watanabe. "Hidden cellulases in termites: revision of an old hypothesis." Biology Letters 3, no. 3 (2007): 336–39. http://dx.doi.org/10.1098/rsbl.2007.0073.

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The intestinal flagellates of termites produce cellulases that contribute to cellulose digestion of their host termites. However, 75% of all termite species do not harbour the cellulolytic flagellates; the endogenous cellulase secreted from the midgut tissue has been considered a sole source of cellulases in these termites. Using the xylophagous flagellate-free termites Nasutitermes takasagoensis and Nasutitermes walkeri , we successfully solubilized cellulases present in the hindgut pellets. Zymograms showed that the hindguts of these termites possessed several cellulases and contained up to

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15

Bharambe, S. D., Kunvar Gyanendra Kumar, R. P. Singh, and A. S. Pawar. "Physiological and biochemical characterization cellulolytic bacteria." International Journal of Environment, Agriculture and Biotechnology 9, no. 6 (2024): 015–18. http://dx.doi.org/10.22161/ijeab.96.2.

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Several efficient cellulase producing microorganisms were isolated. The purpose was to identify and characterize those isolates displaying the greatest cellulase activity for the possible use in the large scale biorefining. Cellulases are inducible enzymes that are synthesized by a large number of microorganisms during their growth on cellulosic materials. Cellulases have attracted much interest because of the diversity of their applications. Cellulases are used in the various industrial process, including textile and laundry, food, feed, leather, pulp and paper. The biochemical characterizati

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16

Poomai, Nutt, Wilailak Siripornadulsil, and Surasak Siripornadulsil. "Cellulase Enzyme Production from Agricultural Waste by Acinetobacter sp. KKU44." Advanced Materials Research 931-932 (May 2014): 1106–10. http://dx.doi.org/10.4028/www.scientific.net/amr.931-932.1106.

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Due to a high ethanol demand, the approach for effective ethanol production is important and has been developed rapidly worldwide. Several agricultural wastes are highly abundant in celluloses and the effective cellulase enzymes do exist widely among microorganisms. Accordingly, the cellulose degradation using microbial cellulase to produce a low-cost substrate for ethanol production has attracted more attention. In this study, the cellulase producing bacterial strain has been isolated from rich straw and identified by 16S rDNA sequence analysis as Acinetobacter sp. KKU44. This strain is able

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17

Liu, Jun, and Huiren Hu. "The role of cellulose binding domains in the adsorption of cellulases onto fibers and its effect on the enzymatic beating of bleached kraft pulp." BioResources 7, no. 1 (2012): 878–92. http://dx.doi.org/10.15376/biores.7.1.878-892.

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The adsorption of cellulases onto fibers may be one of the most important factors affecting the enzymatic reaction between cellulases and fibers. This study investigated the adsorption kinetics involved, using isothermal adsorption equations. Cellulose binding domains (CBDs) were isolated from a commercial cellulase, and their role in the adsorption and enzymatic reaction was evaluated. Approximately 13% to 24% of the refining energy was saved after northern bleached softwood kraft pulp samples were pretreated with full cellulase, CBDs, or cellulase lacking CBDs under optimal conditions. The a

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18

Liu, Wenjin, Xiao-Zhou Zhang, Zuoming Zhang, and Y. H. Percival Zhang. "Engineering of Clostridium phytofermentans Endoglucanase Cel5A for Improved Thermostability." Applied and Environmental Microbiology 76, no. 14 (2010): 4914–17. http://dx.doi.org/10.1128/aem.00958-10.

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ABSTRACT A family 5 glycoside hydrolase from Clostridium phytofermentans was cloned and engineered through a cellulase cell surface display system in Escherichia coli. The presence of cell surface anchoring, a cellulose binding module, or a His tag greatly influenced the activities of wild-type and mutant enzymes on soluble and solid cellulosic substrates, suggesting the high complexity of cellulase engineering. The best mutant had 92%, 36%, and 46% longer half-lives at 60°C on carboxymethyl cellulose, regenerated amorphous cellulose, and Avicel, respectively.

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19

Ilić, Nevena, Marija Milić, Sunčica Beluhan, and Suzana Dimitrijević-Branković. "Cellulases: From Lignocellulosic Biomass to Improved Production." Energies 16, no. 8 (2023): 3598. http://dx.doi.org/10.3390/en16083598.

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Cellulases are enzymes that are attracting worldwide attention because of their ability to degrade cellulose in the lignocellulosic biomass and transform it into highly demanded bioethanol. The enzymatic hydrolysis of cellulose by cellulases into fermentable sugars is a crucial step in biofuel production, given the complex structure of lignocellulose. Due to cellulases’ unique ability to hydrolyze the very recaltricant nature of lignocellulosic biomass, the cellulase market demand is rapidly growing. Although cellulases have been used in industrial applications for decades, constant effort is

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20

KIPPER, Kalle, Priit VÄLJAMÄE, and Gunnar JOHANSSON. "Processive action of cellobiohydrolase Cel7A from Trichoderma reesei is revealed as ‘burst’ kinetics on fluorescent polymeric model substrates." Biochemical Journal 385, no. 2 (2005): 527–35. http://dx.doi.org/10.1042/bj20041144.

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Reaction conditions for the reducing-end-specific derivatization of cellulose substrates with the fluorogenic compound, anthranilic acid, have been established. Hydrolysis of fluorescence-labelled celluloses by cellobiohydrolase Cel7A from Trichoderma reesei was consistent with the active-site titration kinetics (burst kinetics), which allowed the quantification of the processivity of the enzyme. The processivity values of 88±10, 42±10 and 34±2.0 cellobiose units were found for Cel7A acting on labelled bacterial cellulose, bacterial microcrystalline cellulose and endoglucanase-pretreated bacte

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21

Ma, Yuan Yuan, Xin Wang, Han Ze Wang, Kun Zhang, and Min Hua Zhang. "The Expression In Vitro and Application on Cellulose Degradation of LeEXP2." Advanced Materials Research 183-185 (January 2011): 790–94. http://dx.doi.org/10.4028/www.scientific.net/amr.183-185.790.

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Cellulosic ethanol has become a hotspot in recent years. However, its crystal structure makes the efficiency of cellulosic degradation by cellulase very low. Traditional ways to disrupt of connection between microfiber consumes a deal of energy and would pollute the environment as well. Plant expansin is known to loosen the plant cell wall, and might provide a synergistic effect on the activities of cellulase. Whereas, the expression level of expansin in plants has been a limit to the functional study and application in cellulose degradation. Thus, it is essential to screen expansin proteins f

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22

Wang, Hongliang, Fabio Squina, Fernando Segato, et al. "High-Temperature Enzymatic Breakdown of Cellulose." Applied and Environmental Microbiology 77, no. 15 (2011): 5199–206. http://dx.doi.org/10.1128/aem.00199-11.

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ABSTRACTCellulose is an abundant and renewable biopolymer that can be used for biofuel generation; however, structural entrapment with other cell wall components hinders enzyme-substrate interactions, a key bottleneck for ethanol production. Biomass is routinely subjected to treatments that facilitate cellulase-cellulose contacts. Cellulases and glucosidases act by hydrolyzing glycosidic bonds of linear glucose β-1,4-linked polymers, producing glucose. Here we describe eight high-temperature-operating cellulases (TCel enzymes) identified from a survey of thermobacterial and archaeal genomes. T

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23

Wu, Bin, Yue Zhao, and Pei Ji Gao. "A new approach to measurement of saccharifying capacities of crude cellulase." BioResources 1, no. 2 (2006): 189–200. http://dx.doi.org/10.15376/biores.1.2.189-200.

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A practical, quantitative approach has been designed, which makes it possible to accurately estimate the saccharifying activities of crude cellulase preparations for insoluble cellulosics. The challenge in activity determination imposed by changes in hydrolysis time and concentration of cellulase and cellulosics on the assay could be overcome by selection of the specific conversion percentage of cellulose as a function of cellulase concentration, that is, the hydrolysis percentage of filter paper by unit cellulase per minute, as the objective function with respect to different concentrations o

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24

Liang, Youyun, Tong Si, Ee Lui Ang, and Huimin Zhao. "Engineered Pentafunctional Minicellulosome for Simultaneous Saccharification and Ethanol Fermentation in Saccharomyces cerevisiae." Applied and Environmental Microbiology 80, no. 21 (2014): 6677–84. http://dx.doi.org/10.1128/aem.02070-14.

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ABSTRACTSeveral yeast strains have been engineered to express different cellulases to achieve simultaneous saccharification and fermentation of lignocellulosic materials. However, successes in these endeavors were modest, as demonstrated by the relatively low ethanol titers and the limited ability of the engineered yeast strains to grow using cellulosic materials as the sole carbon source. Recently, substantial enhancements to the breakdown of cellulosic substrates have been observed when lytic polysaccharide monooxygenases (LPMOs) were added to traditional cellulase cocktails. LPMOs are repor

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Zhou, Qingxin, Jintao Xu, Yanbo Kou та ін. "Differential Involvement of β-Glucosidases from Hypocrea jecorina in Rapid Induction of Cellulase Genes by Cellulose and Cellobiose". Eukaryotic Cell 11, № 11 (2012): 1371–81. http://dx.doi.org/10.1128/ec.00170-12.

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ABSTRACTAppropriate perception of cellulose outside the cell by transforming it into an intracellular signal ensures the rapid production of cellulases by cellulolyticHypocrea jecorina. The major extracellular β-glucosidase BglI (CEL3a) has been shown to contribute to the efficient induction of cellulase genes. Multiple β-glucosidases belonging to glycosyl hydrolase (GH) family 3 and 1, however, exist inH. jecorina. Here we demonstrated that CEL1b, like CEL1a, was an intracellular β-glucosidase displayingin vitrotransglycosylation activity. We then found evidence that these two major intracell

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Kudanga, T., and E. Mwenje. "Extracellular cellulase production by tropical isolates of Aureobasidium pullulans." Canadian Journal of Microbiology 51, no. 9 (2005): 773–76. http://dx.doi.org/10.1139/w05-053.

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Cellulase production by Aureobasidium pullulans from the temperate regions has remained speculative, with most studies reporting no activity at all. In the current study, tropical isolates from diverse sources were screened for cellulase production. Isolates were grown on a synthetic medium containing cell walls of Msasa tree (Brachystegia sp.) as the sole carbon source, and their cellulolytic activities were measured using carboxymethyl cellulose and α-cellulose as substrates. All isolates studied produced carboxymethyl cellulase (endoglucanase) and alpha-cellulase (exoglucanase) activity. En

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Nicomrat, Duongruitai, and Jirasak Tharajak. "Synergistic Effects of Cellulase-Producing Microorganisms for Future Bioconversion of Lignocellulosic Biomass." Applied Mechanics and Materials 804 (October 2015): 255–58. http://dx.doi.org/10.4028/www.scientific.net/amm.804.255.

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Lignocellulosic biomass can nowadays be bioconverted to value-added biofuels by numerous cellulases purified from diverse microbes. In nature, complex microbial communities produce multifunctional cellulase systems with broader substrate utilization and act sequentially in the synergistic action by subsequently converting cellulose into an utilizable energy source and glucose. This research was to apply cellulase producing isolates based on their possible synergistic action to degrade complex cellulose containing biomass. In the study, the microorganism species, isolated species from durian pe

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Igarashi, Kiyohiko, Takayuki Uchihashi, Anu Koivula, et al. "Traffic Jams Reduce Hydrolytic Efficiency of Cellulase on Cellulose Surface." Science 333, no. 6047 (2011): 1279–82. http://dx.doi.org/10.1126/science.1208386.

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A deeper mechanistic understanding of the saccharification of cellulosic biomass could enhance the efficiency of biofuels development. We report here the real-time visualization of crystalline cellulose degradation by individual cellulase enzymes through use of an advanced version of high-speed atomic force microscopy. Trichoderma reesei cellobiohydrolase I (TrCel7A) molecules were observed to slide unidirectionally along the crystalline cellulose surface but at one point exhibited collective halting analogous to a traffic jam. Changing the crystalline polymorphic form of cellulose by means of

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Yadav, Vikas, Bruce J. Paniliatis, Hai Shi, Kyongbum Lee, Peggy Cebe, and David L. Kaplan. "Novel In Vivo-Degradable Cellulose-Chitin Copolymer from Metabolically Engineered Gluconacetobacter xylinus." Applied and Environmental Microbiology 76, no. 18 (2010): 6257–65. http://dx.doi.org/10.1128/aem.00698-10.

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ABSTRACT Despite excellent biocompatibility and mechanical properties, the poor in vitro and in vivo degradability of cellulose has limited its biomedical and biomass conversion applications. To address this issue, we report a metabolic engineering-based approach to the rational redesign of cellular metabolites to introduce N-acetylglucosamine (GlcNAc) residues into cellulosic biopolymers during de novo synthesis from Gluconacetobacter xylinus. The cellulose produced from these engineered cells (modified bacterial cellulose [MBC]) was evaluated and compared with cellulose produced from normal

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Ndukwe, Nelly A., J. Boitumelo M. Sibiya, and J. Pieter H. Van Wyk. "Saccharification of Sawdust with Aspergillus Niger Cellulase." Journal of Solid Waste Technology and Management 46, no. 3 (2020): 321–27. http://dx.doi.org/10.5276/jswtm/2020.321.

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Accumulated sawdust is a major waste product produced by numerous active sawmills around the Lagos Lagoon in Nigeria. The potential of this wood waste as a resource for bio-product development through the hydrolysis of its cellulose component into glucose, a fermentable sugar is not yet appreciated. Not only is the environment exposed to this organic pollutant but the health of humans is also at risk. The cellulose content of wood sawdust from five different tropical tree species dumped along the Lagos lagoon has been saccharified with cellulase from Aspergillus niger. In order to increase the

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Poole, D. M., A. J. Durrant, G. P. Hazlewood, and H. J. Gilbert. "Characterization of hybrid proteins consisting of the catalytic domains of Clostridium and Ruminococcus endoglucanases, fused to Pseudomonas non-catalytic cellulose-binding domains." Biochemical Journal 279, no. 3 (1991): 787–92. http://dx.doi.org/10.1042/bj2790787.

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The N-terminal 160 or 267 residues of xylanase A from Pseudomonas fluorescens subsp. cellulosa, containing a non-catalytic cellulose-binding domain (CBD), were fused to the N-terminus of the catalytic domain of endoglucanase E (EGE') from Clostridium thermocellum. A further hybrid enzyme was constructed consisting of the 347 N-terminal residues of xylanase C (XYLC) from P. fluorescens subsp. cellulosa, which also constitutes a CBD, fused to the N-terminus of endoglucanase A (EGA) from Ruminococcus albus. The three hybrid enzymes bound to insoluble cellulose, and could be eluted such that cellu

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Bae, Jungu, Kouichi Kuroda, and Mitsuyoshi Ueda. "Proximity Effect among Cellulose-Degrading Enzymes Displayed on the Saccharomyces cerevisiae Cell Surface." Applied and Environmental Microbiology 81, no. 1 (2014): 59–66. http://dx.doi.org/10.1128/aem.02864-14.

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ABSTRACTProximity effect is a form of synergistic effect exhibited when cellulases work within a short distance from each other, and this effect can be a key factor in enhancing saccharification efficiency. In this study, we evaluated the proximity effect between 3 cellulose-degrading enzymes displayed on theSaccharomyces cerevisiaecell surface, that is, endoglucanase, cellobiohydrolase, and β-glucosidase. We constructed 2 kinds of arming yeasts through genome integration: ALL-yeast, which simultaneously displayed the 3 cellulases (thus, the different cellulases were near each other), and MIX-

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33

Touijer, Hanane, Najoua Benchemsi, Mohamed Ettayebi, Abdellatif Janati Idrissi, Bouchra Chaouni, and Hicham Bekkari. "Thermostable Cellulases from the Yeast Trichosporon sp." Enzyme Research 2019 (April 17, 2019): 1–6. http://dx.doi.org/10.1155/2019/2790414.

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Objectives. Identification of cellulolytic microorganisms is of great interest to the hydrolysis of cellulosic biomass. This study focuses on the identification of cellulolytic yeasts and the optimization of cellulase activities produced by the best performing isolate. Results. 30 cellulolytic yeast isolates were selected. Enzymes produced by an isolate from the Trichosporon genus showed the property to hydrolyze different substrates: carboxymethyl cellulose (CMC), cellulose fiber, and filter paper (FP). The optimum measured temperature was 55°C for CMCase and 60°C for FPase. The optimal pH wa

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34

Touijer, Hanane, Najoua Benchemsi, Muhammad Irfan, et al. "Statistical Optimization and Purification of Cellulase Enzyme Production from Trichosporon insectorum." Fermentation 10, no. 9 (2024): 453. http://dx.doi.org/10.3390/fermentation10090453.

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Abstract (sommario):

Enzymatic degradation of cellulosic biomass represents the most sustainable and environmentally friendly method for producing liquid biofuel, widely utilized in various commercial processes. While cellulases are predominantly produced by bacteria and fungi, the enzymatic potential of cellulase-producing yeasts remains significantly less explored. In this study, the yeast strain Trichosporon insectorum, isolated from the gut of the coprophagous beetle Gymnopleurus sturmii, was utilized for cellulase production in submerged fermentation. A central composite design was employed to optimize cellul

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35

Yang, Songlin, Minghua Hu, Runxin Wu, et al. "Genetic Evidence of SpGH9A3 in Leaf Morphology Variation of Spathiphyllum ‘Mojo’." Genes 15, no. 9 (2024): 1132. http://dx.doi.org/10.3390/genes15091132.

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Leaves play a crucial role as ornamental organs in Spathiphyllum, exhibiting distinct differences across various Spathiphyllum varieties. Leaf development is intricately linked to processes of cell proliferation and expansion, with cell morphology often regulated by plant cell walls, primarily composed of cellulose. Alterations in cellulose content can impact cell morphology, subsequently influencing the overall shape of plant organs. Although cellulases have been shown to affect cellulose levels in plant cells, genetic evidence linking them to the regulation of leaf shape remains limited. Thi

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36

Wang, Na, Zhihua Yan, Na Liu, Xiaorong Zhang, and Chenggang Xu. "Synergy of Cellulase Systems between Acetivibrio thermocellus and Thermoclostridium stercorarium in Consolidated-Bioprocessing for Cellulosic Ethanol." Microorganisms 10, no. 3 (2022): 502. http://dx.doi.org/10.3390/microorganisms10030502.

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Anaerobes harbor some of the most efficient biological machinery for cellulose degradation, especially thermophilic bacteria, such as Acetivibrio thermocellus and Thermoclostridium stercorarium, which play a fundamental role in transferring lignocellulose into ethanol through consolidated bioprocessing (CBP). In this study, we compared activities of two cellulase systems under varying kinds of hemicellulose and cellulose. A. thermocellus was identified to contribute specifically to cellulose hydrolysis, whereas T. stercorarium contributes to hemicellulose hydrolysis. The two systems were assay

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Ahmed, Mohamed, Soad El-Zayat, and Magdi El-Sayed. "Cellulolytic activity of cellulose-decomposing fungi isolated from Aswan hot desert soil, Egypt." Journal of Biological Studies 1, no. 2 (2018): 35–48. http://dx.doi.org/10.62400/jbs.v1i2.9.

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Fungi are well known agents for decomposition of organic matter in common and of cellulosic material, in particular; therefore they considered as the main cellulose producing microorganisms. The present study was aimed to isolate and screen the ability of cellulolytic fungal strains from desert soil living under environmental stress to produce cellulolytic enzymes. Forty-three fungal strains in addition to two varieties were isolated from different sites at Aswan University campus and were able to degrade the cellulose with variable extents. Fungal species were grouped as high, moderate and lo

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38

Singh, Nivisti, Bishop Bruce Sithole та Roshini Govinden. "Optimisation of β-Glucosidase Production in a Crude Aspergillus japonicus VIT-SB1 Cellulase Cocktail Using One Variable at a Time and Statistical Methods and its Application in Cellulose Hydrolysis". International Journal of Molecular Sciences 24, № 12 (2023): 9928. http://dx.doi.org/10.3390/ijms24129928.

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Pulp and paper mill sludge (PPMS) is currently disposed of into landfills which are reaching their maximum capacity. Valorisation of PPMS by enzymatic hydrolysis using cellulases is an alternative strategy. Existing commercial cellulases are expensive and contain low titres of β-glucosidases. In this study, β-glucosidase production was optimised by Aspergillus japonicus VIT-SB1 to obtain higher β-glucosidase titres using the One Variable at a Time (OVAT), Plackett Burman (PBD), and Box Behnken design (BBD)of experiments and the efficiency of the optimised cellulase cocktail to hydrolyse cellul

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39

Feng, Yue, Hui-Qin Liu, Run-Cang Sun, and Jian-Xin Jiang. "Enzymatic hydrolysis of cellulose from steam-pretreated Lespedeza stalk (Lespedeza crytobotrya) with four Trichoderma cellulases." BioResources 6, no. 3 (2011): 2776–89. http://dx.doi.org/10.15376/biores.6.3.2776-2789.

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Abstract (sommario):

The hydrolytic potential of cellulases produced by Trichoderma viride, Trichoderma pseudokoningii, Trichoderma koningii, and Trichoderma reesei with addition of exogenous β-glucosidase was evaluated on cellulose of steam-pretreated Lespedeza. The T. viride enzyme achieved the highest glucose conversion (90.09%), while T. pseudokoningii cellulase achieved the highest ratio of cellobiose to glucose (4.94%) at the end of hydrolysis. Enzymatic adsorption on the substrate was evaluated on filter paper activity and β-glucosidase activity in the corresponding digest with the obtained T. cellulases. T

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40

Mingardon, Florence, Angï¿½lique Chanal, Ana M. Lï¿½pez-Contreras, Cyril Dray, Edward A. Bayer, and Henri-Pierre Fierobe. "Incorporation of Fungal Cellulases in Bacterial Minicellulosomes Yields Viable, Synergistically Acting Cellulolytic Complexes." Applied and Environmental Microbiology 73, no. 12 (2007): 3822–32. http://dx.doi.org/10.1128/aem.00398-07.

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ABSTRACT Artificial designer minicellulosomes comprise a chimeric scaffoldin that displays an optional cellulose-binding module (CBM) and bacterial cohesins from divergent species which bind strongly to enzymes engineered to bear complementary dockerins. Incorporation of cellulosomal cellulases from Clostridium cellulolyticum into minicellulosomes leads to artificial complexes with enhanced activity on crystalline cellulose, due to enzyme proximity and substrate targeting induced by the scaffoldin-borne CBM. In the present study, a bacterial dockerin was appended to the family 6 fungal cellula

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Caspi, Jonathan, Yoav Barak, Rachel Haimovitz, et al. "Effect of Linker Length and Dockerin Position on Conversion of a Thermobifida fusca Endoglucanase to the Cellulosomal Mode." Applied and Environmental Microbiology 75, no. 23 (2009): 7335–42. http://dx.doi.org/10.1128/aem.01241-09.

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ABSTRACT We have been developing the cellulases of Thermobifida fusca as a model to explore the conversion from a free cellulase system to the cellulosomal mode. Three of the six T. fusca cellulases (endoglucanase Cel6A and exoglucanases Cel6B and Cel48A) have been converted in previous work by replacing their cellulose-binding modules (CBMs) with a dockerin, and the resultant recombinant “cellulosomized” enzymes were incorporated into chimeric scaffolding proteins that contained cohesin(s) together with a CBM. The activities of the resultant designer cellulosomes were compared with an equival

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42

Mamat Razali, Nur Amira, Noriean Azraaie, Nurul Aimi Mohd Zainul Abidin, Nur Ain Ibrahim, Fauziah Abdul Aziz, and Saadah Abdul Rahman. "Effect of Chemical Treatment on Crystalline Cellulose: Changes in Crystallinity and Functional Groups of Cellulose." Advanced Materials Research 1087 (February 2015): 35–39. http://dx.doi.org/10.4028/www.scientific.net/amr.1087.35.

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Abstract (sommario):

Cellulosic material derived from Merbau (Intsia bijuga) was extracted at atmospheric pressure. In the initial stage the sample was delignified using peroxyacetic acid to remove the amorphous. In the second stage the samples were double bleached using hydrogen peroxide (H2O2) and sodium Hydroxide (NaOH). From the X-Ray Diffraction (XRD) data it is evident that both acid and alkali bleached celluloses have rich cellulose I structure. The results are supported by FTIR study in which all samples shown typical spectra of cellulose.

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43

Metreveli, Eka, Tamar Khardziani, and Vladimir Elisashvili. "The Carbon Source Controls the Secretion and Yield of Polysaccharide-Hydrolyzing Enzymes of Basidiomycetes." Biomolecules 11, no. 9 (2021): 1341. http://dx.doi.org/10.3390/biom11091341.

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In the present study, the polysaccharide-hydrolyzing secretomes of Irpex lacteus (Fr.) Fr. (1828) BCC104, Pycnoporus coccineus (Fr.) Bondartsev and Singer (1941) BCC310, and Schizophyllum commune Fr. (1815) BCC632 were analyzed in submerged fermentation conditions to elucidate the effect of chemically and structurally different carbon sources on the expression of cellulases and xylanase. Among polymeric substrates, crystalline cellulose appeared to be the best carbon source providing the highest endoglucanase, total cellulase, and xylanase activities. Mandarin pomace as a growth substrate for

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44

Uchiyama, Taku, Takayuki Uchihashi, Akihiko Nakamura, et al. "Convergent evolution of processivity in bacterial and fungal cellulases." Proceedings of the National Academy of Sciences 117, no. 33 (2020): 19896–903. http://dx.doi.org/10.1073/pnas.2011366117.

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Abstract (sommario):

Cellulose is the most abundant biomass on Earth, and many microorganisms depend on it as a source of energy. It consists mainly of crystalline and amorphous regions, and natural degradation of the crystalline part is highly dependent on the degree of processivity of the degrading enzymes (i.e., the extent of continuous hydrolysis without detachment from the substrate cellulose). Here, we report high-speed atomic force microscopic (HS-AFM) observations of the movement of four types of cellulases derived from the cellulolytic bacteriaCellulomonas fimion various insoluble cellulose substrates. Th

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45

Samejima, Masahiro, Takeshi Ohkubo, Kiyohiko Igarashi, et al. "The behaviour of Phanerochaete chrysosporium cellobiose dehydrogenase on adsorption to crystallineand amorphous celluloses." Biotechnology and Applied Biochemistry 25, no. 2 (1997): 135–41. http://dx.doi.org/10.1111/j.1470-8744.1997.tb00425.x.

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Abstract (sommario):

The adsorption of cellobiose dehydrogenase (CDH) to cellulose has been previously reported. However, the structural type of cellulose on to which CDH is adsorbed has not been investigated. In the present study we have compared the behaviour of CDH when it adsorbs on the highly crystalline cellulose microfibrils from Valonia macrophysa and on the completely amorphous cellulose prepared from a solution of Avicel in the SO2/amine system. The isotherms of CDH adsorption to both Valonia and amorphous celluloses fit well with the Langmuir adsorption theory. However, the maximum adsorption of CDH to

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46

Hildebrand, Amanda, Edyta Szewczyk, Hui Lin, Takao Kasuga, and Zhiliang Fan. "Engineering Neurospora crassa for Improved Cellobiose and Cellobionate Production." Applied and Environmental Microbiology 81, no. 2 (2014): 597–603. http://dx.doi.org/10.1128/aem.02885-14.

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Abstract (sommario):

ABSTRACTWe report engineeringNeurospora crassato improve the yield of cellobiose and cellobionate from cellulose. A previously engineered strain ofN. crassa(F5) with six of seven β-glucosidase (bgl) genes knocked out was shown to produce cellobiose and cellobionate directly from cellulose without the addition of exogenous cellulases. In this study, the F5 strain was further modified to improve the yield of cellobiose and cellobionate from cellulose by increasing cellulase production and decreasing product consumption. The effects of two catabolite repression genes,cre-1andace-1, on cellulase p

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47

Lucia, Arianna, Markus Bacher, Hendrikus W. G. van Herwijnen, and Thomas Rosenau. "A Direct Silanization Protocol for Dialdehyde Cellulose." Molecules 25, no. 10 (2020): 2458. http://dx.doi.org/10.3390/molecules25102458.

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Abstract (sommario):

Cellulose derivatives have many potential applications in the field of biomaterials and composites, in addition to several ways of modification leading to them. Silanization in aqueous media is one of the most promising routes to create multipurpose and organic–inorganic hybrid materials. Silanization has been widely used for cellulosic and nano-structured celluloses, but was a problem so far if to be applied to the common cellulose derivative “dialdehyde cellulose” (DAC), i.e., highly periodate-oxidized celluloses. In this work, a straightforward silanization protocol for dialdehyde cellulose

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48

Wang, Lunji, Yishen Zhao, Siqiao Chen, et al. "Growth, Enzymatic, and Transcriptomic Analysis of xyr1 Deletion Reveals a Major Regulator of Plant Biomass-Degrading Enzymes in Trichoderma harzianum." Biomolecules 14, no. 2 (2024): 148. http://dx.doi.org/10.3390/biom14020148.

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Abstract (sommario):

The regulation of plant biomass degradation by fungi is critical to the carbon cycle, and applications in bioproducts and biocontrol. Trichoderma harzianum is an important plant biomass degrader, enzyme producer, and biocontrol agent, but few putative major transcriptional regulators have been deleted in this species. The T. harzianum ortholog of the transcriptional activator XYR1/XlnR/XLR-1 was deleted, and the mutant strains were analyzed through growth profiling, enzymatic activities, and transcriptomics on cellulose. From plate cultures, the Δxyr1 mutant had reduced growth on D-xylose, xyl

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49

Krauss, Jan, Vladimir V. Zverlov, and Wolfgang H. Schwarz. "In VitroReconstitution of the Complete Clostridium thermocellum Cellulosome and Synergistic Activity on Crystalline Cellulose." Applied and Environmental Microbiology 78, no. 12 (2012): 4301–7. http://dx.doi.org/10.1128/aem.07959-11.

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Abstract (sommario):

ABSTRACTArtificial cellulase complexes active on crystalline cellulose were reconstitutedin vitrofrom a native mix of cellulosomal enzymes and CipA scaffoldin. Enzymes containing dockerin modules for binding to the corresponding cohesin modules were prepared from culture supernatants of aC. thermocellum cipAmutant. They were reassociated to cellulosomes via dockerin-cohesin interaction. Recombinantly produced mini-CipA proteins with one to three cohesins either with or without the carbohydrate-binding module (CBM) and the complete CipA protein were used as the cellulosomal backbone. The bindin

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50

Ramalingam, Subramanian, and Dhanashekar Revathi. "De-Escalation of Saccharification Costs through Enforcement of Immobilization of Cellulase Synthesized by Wild Trichoderma viride." Catalysts 12, no. 6 (2022): 659. http://dx.doi.org/10.3390/catal12060659.

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Abstract (sommario):

The economic uncertainty associated with cellulosic bioethanol can be overcome through the inclusion of cheap substrates and methodologies that can extend the shelf life of cellulolytic enzymes. In this study, wild Trichoderma viride was used to produce cellulases, media formulation studies were conducted to enhance the cellulase production further and immobilization strategies were tested for stable cellulase–iron oxide magnetic nanoparticle coupling. Out of the seven different production media designed, media containing glucose, wheat bran, cellulose and corn steep liquor supported the highe

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