Characteristics of fungal cellulases

Goyal, Anil K.; Ghosh, B. K.; Eveleigh, D. E.

doi:10.1016/0960-8524(91)90098-5

Cited by 181 publications

(89 citation statements)

References 71 publications

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“…The rate constant for EG1, k EG1 , was set at fivefold that used for CBH1 in light of the relative specific activity of these two enzymes, mechanistic considerations, and experimental data fitting (Tomme et al, 1988;Zhang and Lynd, 2004). The typical composition of unfractionated T. reesei cellulase mixtures was taken to be as reported elsewhere (Goyal et al, 1991) such that 100 mg cellulase contains 60 mg CBH1, 20 mg CBH2, and 12 mg EG1.…”

Section: Parameter Valuesmentioning

confidence: 99%

A functionally based model for hydrolysis of cellulose by fungal cellulase

Zhang

Lynd

2006

Biotechnol. Bioeng.

203

158

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A new functionally based kinetic model for enzymatic hydrolysis of pure cellulose by the Trichoderma cellulase system is presented. The model represents the actions of cellobiohydrolases I, cellobiohydrolase II, and endoglucanase I; and incorporates two measurable and physically interpretable substrate parameters: the degree of polymerization (DP) and the fraction of b-glucosidic bonds accessible to cellulase, F a (Zhang and Lynd, 2004). Initial enzyme-limited reaction rates simulated by the model are consistent with several important behaviors reported in the literature, including the effects of substrate characteristics on exoglucanase and endoglucanase activities; the degree of endo/exoglucanase synergy; the endoglucanase partition coefficient on hydrolysis rates; and enzyme loading on relative reaction rates for different substrates. This is the first cellulase kinetic model involving a single set of kinetic parameters that is successfully applied to a variety of cellulosic substrates, and the first that describes more than one behavior associated with enzymatic hydrolysis. The model has potential utility for data accommodation and design of industrial processes, structuring, testing, and extending understanding of cellulase enzyme systems when experimental date are available, and providing guidance for functional design of cellulase systems at a molecular scale. Opportunities to further refine cellulase kinetic models are discussed, including parameters that would benefit from further study.

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Section: Parameter Valuesmentioning

confidence: 99%

A functionally based model for hydrolysis of cellulose by fungal cellulase

Zhang

Lynd

2006

Biotechnol. Bioeng.

203

158

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“…At least two cellobiohydrolases (CBH1-2), five endoglucanases (EG1-5), h-glucosidases, and hemicellulases have been identified by 2D electrophoresis (Vinzant et al, 2001). CBH1, CBH2, and EG2 are the three main components of the T. reesei cellu- lase system, representing 60 F 5%, 20 F 6%, and 12 F 3% of total cellulase protein, respectively (Goyal et al, 1991;Gritzali and Brown, 1978;Knowles et al, 1987;Kyriacou et al, 1987;Nidetzky and Claeyssens, 1994). Reconstituted cellulase preparations based on purified components in these proportions exhibit specific activity equivalent to unfractionated preparations (Baker et al, 1998).…”

Section: Trichoderma Reesei Cellulase Systemmentioning

confidence: 99%

Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems

Zhang

Lynd

2004

Biotech & Bioengineering

1,640

1,284

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Information pertaining to enzymatic hydrolysis of cellulose by noncomplexed cellulase enzyme systems is reviewed with a particular emphasis on development of aggregated understanding incorporating substrate features in addition to concentration and multiple cellulase components. Topics considered include properties of cellulose, adsorption, cellulose hydrolysis, and quantitative models. A classification scheme is proposed for quantitative models for enzymatic hydrolysis of cellulose based on the number of solubilizing activities and substrate state variables included. We suggest that it is timely to revisit and reinvigorate functional modeling of cellulose hydrolysis, and that this would be highly beneficial if not necessary in order to bring to bear the large volume of information available on cellulase components on the primary applications that motivate interest in the subject. B

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“…П³ñëÿ äîñÿгíåííÿ ìàêñèìàëüíèх зíà÷åíü åíäîгëюêàíàзíà àêòèâí³ñòü пî â³äíîшåííю äî Na-ÊÌÖ òàêîж зìåíшóâàëàñü, íàé³ìîâ³ðí³шå âíàñë³äîê ³íàêòèâàö³ї åíзèìó пðîäóêòàìè ðåàêö³ї. Яê âèäíî з ðèñóíêó 3, äèíàì³êà åíäîгëюêàíàзíîї àêòèâíîñò³ êóëü-òóðàëüíèх ф³ëüòðàò³â пî â³äíîшåííю äî г³äðîêñèåòèëöåëюëîзè (ГÅÖ) â³äð³зíÿєòüñÿ â³ä äèíàì³êè àêòèâíîñò³ пî â³äíîшåííю äî Na-ÊÌÖ, щî ìîжíà пîÿñíèòè òèì, щî ГÅÖ ëåгшå г³äðîë³зóєòüñÿ åíзèìàìè [12,14,15], âêëàäîì äî г³äðîë³зó öèх ñпîëóê íå ³ñòèííî öåëюëîзîë³òè÷íèх фåðìåíò³â Ìікробіоëоãія і біотеõноëоãія ¹ 4/2011 Ê.Ã. Äреваль, Ê.В.…”

Section: ðис 1 äинамIка синтезу целюлаз штамами Irpex Lacteus ê-1 unclassified

“…Юдiна, Ì.I. Áойко [9], à òàêîж âпëèâîì ñòðóêòóðè зàì³ñíèê³â ó ìîëåêóë³ öåëюëîзè [14,15]. Íà â³äì³íó â³ä öåëюëîзîë³òè÷íîї àêòèâíîñò³ пî â³äíîшåííю äî ³íшèх ñóбñòðàò³â, íàéâèщó ГÅÖ-àêòèâí³ñòü âñòàíîâëåíî äëÿ шòàìó S. hirsutum Sh-1, щî ìîжíà пîÿñíèòè â³äì³ííîñòÿìè ó ñпåöèф³÷íîñò³ ä³ї åíäîгëюêàíàз ð³зíèх бàзèä³îì³öåò³â.…”

Section: ðис 1 äинамIка синтезу целюлаз штамами Irpex Lacteus ê-1 unclassified