Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 498308
Title Different action patterns of glucoamylases on branched gluco-oligosaccharides from amylopectin
Author(s) Jonathan, M.C.; Brussel, M. Van; Scheffers, M.S.; Kabel, M.A.
Source Carbohydrate Polymers 143 (2016). - ISSN 0144-8617 - p. 198 - 203.
DOI http://dx.doi.org/10.1016/j.carbpol.2016.02.005
Department(s) Food Chemistry Group
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2016
Keyword(s) Amyloglucosidase - Amylopectin - Panose - Pullulan - Saccharification
Abstract

A bottleneck in enzymatic starch hydrolysis, like in biofuel industry, is relatively slow degradation of branched structures compared to linear ones. This research aimed to evaluate glucoamylases for their activity towards branched gluco-oligosaccharides. The activity of seven modified glucoamylases and two homologs was compared to that of a reference glucoamylase obtained from a commercial enzyme cocktail 'Distillase® SSF'. All enzymes were evaluated for their activity towards panose (glc(α1-6)glc(α1-4)glc), pullulan and a purified branched gluco-oligosaccharide with a degree of polymerisation of 5 (bDP5) identified as glc(α1-4)[glc(α1-4)glc(α1-6)]glc(α1-4)glc. The enzymes degraded bDP5 differently, which was mainly due to variation in their capability to cleave α-(1→6)-linked or the α-(1→4)-linked glucosyl residue at the non-reducing end of the branched glucosyl residue. By comparing the enzyme activity towards bDP5 with those towards panose and pullulan, it was suggested that the activity towards bDP5 could be estimated only when the activity towards both commercial substrates was evaluated.

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