Literature DB >> 19577626

Modeling cellulase kinetics on lignocellulosic substrates.

Prabuddha Bansal1, Mélanie Hall1, Matthew J Realff1, Jay H Lee1, Andreas S Bommarius2.   

Abstract

The enzymatic hydrolysis of cellulose to glucose by cellulases is one of the major steps involved in the conversion of lignocellulosic biomass to yield biofuel. This hydrolysis by cellulases, a heterogeneous reaction, currently suffers from some major limitations, most importantly a dramatic rate slowdown at high degrees of conversion. To render the process economically viable, increases in hydrolysis rates and yields are necessary and require improvement both in enzymes (via protein engineering) and processing, i.e. optimization of reaction conditions, reactor design, enzyme and substrate cocktail compositions, enzyme recycling and recovery strategies. Advances in both areas in turn strongly depend on the progress in the accurate quantification of substrate-enzyme interactions and causes for the rate slowdown. The past five years have seen a significant increase in the number of studies on the kinetics of the enzymatic hydrolysis of cellulose. This review provides an overview of the models published thus far, classifies and tabulates these models, and presents an analysis of their basic assumptions. While the exact mechanism of cellulases on lignocellulosic biomass is not completely understood yet, models in the literature have elucidated various factors affecting the enzymatic rates and activities. Different assumptions regarding rate-limiting factors and basic substrate-enzyme interactions were employed to develop and validate these models. However, the models need to be further tested against additional experimental data to validate or disprove any underlying hypothesis. It should also provide better insight on additional parameters required in the case that more substrate and enzyme properties are to be included in a model.

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Year:  2009        PMID: 19577626     DOI: 10.1016/j.biotechadv.2009.06.005

Source DB:  PubMed          Journal:  Biotechnol Adv        ISSN: 0734-9750            Impact factor:   14.227


  63 in total

1.  Computational investigation of glycosylation effects on a family 1 carbohydrate-binding module.

Authors:  Courtney B Taylor; M Faiz Talib; Clare McCabe; Lintao Bu; William S Adney; Michael E Himmel; Michael F Crowley; Gregg T Beckham
Journal:  J Biol Chem       Date:  2011-12-06       Impact factor: 5.157

2.  Kinetic modeling of rapid enzymatic hydrolysis of crystalline cellulose after pretreatment by NMMO.

Authors:  Mahdi Khodaverdi; Azam Jeihanipour; Keikhosro Karimi; Mohammad J Taherzadeh
Journal:  J Ind Microbiol Biotechnol       Date:  2011-11-04       Impact factor: 3.346

3.  Pre-steady-state kinetics for hydrolysis of insoluble cellulose by cellobiohydrolase Cel7A.

Authors:  Nicolaj Cruys-Bagger; Jens Elmerdahl; Eigil Praestgaard; Hirosuke Tatsumi; Nikolaj Spodsberg; Kim Borch; Peter Westh
Journal:  J Biol Chem       Date:  2012-04-09       Impact factor: 5.157

4.  Product binding varies dramatically between processive and nonprocessive cellulase enzymes.

Authors:  Lintao Bu; Mark R Nimlos; Michael R Shirts; Jerry Ståhlberg; Michael E Himmel; Michael F Crowley; Gregg T Beckham
Journal:  J Biol Chem       Date:  2012-05-30       Impact factor: 5.157

5.  Processivity of cellobiohydrolases is limited by the substrate.

Authors:  Mihhail Kurasin; Priit Väljamäe
Journal:  J Biol Chem       Date:  2010-11-04       Impact factor: 5.157

6.  Slow Off-rates and Strong Product Binding Are Required for Processivity and Efficient Degradation of Recalcitrant Chitin by Family 18 Chitinases.

Authors:  Mihhail Kurašin; Silja Kuusk; Piret Kuusk; Morten Sørlie; Priit Väljamäe
Journal:  J Biol Chem       Date:  2015-10-14       Impact factor: 5.157

7.  Systems-level modeling with molecular resolution elucidates the rate-limiting mechanisms of cellulose decomposition by cellobiohydrolases.

Authors:  Barry Z Shang; Rakwoo Chang; Jhih-Wei Chu
Journal:  J Biol Chem       Date:  2013-08-15       Impact factor: 5.157

8.  The predominant molecular state of bound enzyme determines the strength and type of product inhibition in the hydrolysis of recalcitrant polysaccharides by processive enzymes.

Authors:  Silja Kuusk; Morten Sørlie; Priit Väljamäe
Journal:  J Biol Chem       Date:  2015-03-12       Impact factor: 5.157

Review 9.  Biology and biotechnology of Trichoderma.

Authors:  André Schuster; Monika Schmoll
Journal:  Appl Microbiol Biotechnol       Date:  2010-05-12       Impact factor: 4.813

10.  Comparative kinetic analysis of two fungal beta-glucosidases.

Authors:  Marie Chauve; Hugues Mathis; Delphine Huc; Dominique Casanave; Frédéric Monot; Nicolas Lopes Ferreira
Journal:  Biotechnol Biofuels       Date:  2010-02-11       Impact factor: 6.040

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