Literature DB >> 18367275

Towards new enzymes for biofuels: lessons from chitinase research.

Vincent G H Eijsink1, Gustav Vaaje-Kolstad, Kjell M Vårum, Svein J Horn.   

Abstract

Enzymatic conversion of structural polysaccharides in plant biomass is a key issue in the development of second generation ('lignocellulosic') bioethanol. The efficiency of this process depends in part on the ability of enzymes to disrupt crystalline polysaccharides, thus gaining access to single polymer chains. Recently, new insights into how enzymes accomplish this have been obtained from studies on enzymatic conversion of chitin. First, chitinolytic microorganisms were shown to produce non-hydrolytic accessory proteins that increase enzyme efficiency. Second, it was shown that a processive mechanism, which is generally considered favorable because it improves substrate accessibility, might in fact slow down enzymes. These findings suggest new focal points for the development of enzyme technology for depolymerizing recalcitrant polysaccharide biomass. Improving substrate accessibility should be a key issue because this might reduce the need for using processive enzymes, which are intrinsically slow and abundantly present in current commercial enzyme preparations for biomass conversion. Furthermore, carefully selected substrate-disrupting accessory proteins or domains might provide novel tools to improve substrate accessibility and thus contribute to more efficient enzymatic processes.

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Year:  2008        PMID: 18367275     DOI: 10.1016/j.tibtech.2008.02.004

Source DB:  PubMed          Journal:  Trends Biotechnol        ISSN: 0167-7799            Impact factor:   19.536


  33 in total

1.  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

Review 2.  Fungal chitinases: function, regulation, and potential roles in plant/pathogen interactions.

Authors:  Thorsten Langner; Vera Göhre
Journal:  Curr Genet       Date:  2015-11-02       Impact factor: 3.886

3.  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

4.  Chitin binding proteins act synergistically with chitinases in Serratia proteamaculans 568.

Authors:  Pallinti Purushotham; P V Parvati Sai Arun; Jogadhenu S S Prakash; Appa Rao Podile
Journal:  PLoS One       Date:  2012-05-09       Impact factor: 3.240

5.  Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency.

Authors:  Henrik Zakariassen; Berit Bjugan Aam; Svein J Horn; Kjell M Vårum; Morten Sørlie; Vincent G H Eijsink
Journal:  J Biol Chem       Date:  2009-02-25       Impact factor: 5.157

6.  Precise Manipulation and Patterning of Protein Crystals for Macromolecular Crystallography Using Surface Acoustic Waves.

Authors:  Feng Guo; Weijie Zhou; Peng Li; Zhangming Mao; Neela H Yennawar; Jarrod B French; Tony Jun Huang
Journal:  Small       Date:  2015-02-01       Impact factor: 13.281

7.  Cleavage of cellulose by a CBM33 protein.

Authors:  Zarah Forsberg; Gustav Vaaje-Kolstad; Bjørge Westereng; Anne C Bunæs; Yngve Stenstrøm; Alasdair MacKenzie; Morten Sørlie; Svein J Horn; Vincent G H Eijsink
Journal:  Protein Sci       Date:  2011-08-08       Impact factor: 6.725

8.  Characterization of the chitinase gene in Bacillus thuringiensis Mexican isolates.

Authors:  Ninfa M Rosas-García; Juan M Fortuna-González; J Eleazar Barboza-Corona
Journal:  Folia Microbiol (Praha)       Date:  2013-03-02       Impact factor: 2.099

Review 9.  Production of chitooligosaccharides and their potential applications in medicine.

Authors:  Berit B Aam; Ellinor B Heggset; Anne Line Norberg; Morten Sørlie; Kjell M Vårum; Vincent G H Eijsink
Journal:  Mar Drugs       Date:  2010-04-27       Impact factor: 5.118

10.  N-acetylglucosamine utilization by Saccharomyces cerevisiae based on expression of Candida albicans NAG genes.

Authors:  Jürgen Wendland; Yvonne Schaub; Andrea Walther
Journal:  Appl Environ Microbiol       Date:  2009-07-31       Impact factor: 4.792

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