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Comparative NMR analysis of cellooligosaccharide hydrolysis by GH9 bacterial and plant endo-1,4-ss-glucanases
KTH, School of Biotechnology (BIO), Centres, Swedish Center for Biomimetic Fiber Engineering, BioMime.
KTH, School of Biotechnology (BIO), Centres, Swedish Center for Biomimetic Fiber Engineering, BioMime.
KTH, School of Biotechnology (BIO), Centres, Swedish Center for Biomimetic Fiber Engineering, BioMime.
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2008 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 47, no 18, 5235-5241 p.Article in journal (Refereed) Published
Abstract [en]

H-1 NMR spectroscopy has been used to analyze the product profiles arising from the hydrolysis of cellooligosaccharides by family GH9 cellulases. The product profiles obtained with the wild type and several active site mutants of a bacterial processive endoglucanase, Tf Cel9A, were compared with those obtained by a randomly acting plant endoglucanase, PttCe19A. PttCe19A is an orthologue of the Arabidopsis endocellulase, Korrigan, which is required for efficient cellulose biosynthesis. As expected, poplar PttCe19A was shown to catalyze the degradation of cellooligosaccharides by inversion of the configuration of the anomeric carbon. The product analyses showed that the number of interactions between the glucose units of the substrate and the aromatic residues in the enzyme active sites determines the point of cleavage in both enzymes.

Place, publisher, year, edition, pages
2008. Vol. 47, no 18, 5235-5241 p.
Keyword [en]
THERMOMONOSPORA-FUSCA, TRICHODERMA-REESEI, SUBSTRATE-BINDING, PICHIA-PASTORIS, ENDO-1, 4-BETA-GLUCANASE, PURIFICATION, MECHANISM, ENDO-BETA-1, 4-GLUCANASE, OLIGOSACCHARIDES, STRAWBERRY
National Category
Industrial Biotechnology
Identifiers
URN: urn:nbn:se:kth:diva-34106DOI: 10.1021/bi702193eISI: 000255429200017Scopus ID: 2-s2.0-42949151881OAI: oai:DiVA.org:kth-34106DiVA: diva2:419196
Note
QC 20110526Available from: 2011-05-26 Created: 2011-05-25 Last updated: 2017-12-11Bibliographically approved

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Jonsson Rudsander, UllaPiens, KathleenMaster, EmmaBrumer, HarryTeeri, Tuula T.
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