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Action pattern of alpha‐amylase from Aspergillus oryzae in concentrated media
Author(s) -
Graber Marianne,
Combes Didier
Publication year - 1990
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260360103
Subject(s) - chemistry , substrate (aquarium) , aspergillus oryzae , hydrolysis , degree of polymerization , amylase , polymerization , enzyme , alpha amylase , stereochemistry , biochemistry , food science , organic chemistry , biology , polymer , ecology
The influence of concentrated maltotetraose solutions on fungal alpha‐amylase activity and specificity has been determined. It has been found that the enzyme is not inhibited by 500 g/L substrate concentration and that transglycosylation reactions are increased with rising substrate concentration. The amount of oligosaccharides of polymerization degree higher than maltotetraose reaches 20% (w/w). Moreover, the effect of polyhydric alcohols, known as water activity depressors has been analyzed: the presence of polyols does not modify the amount of transglycosylation products, but changes the hydrolysis pattern by favoring the formation of low polymerization degree oligosaccharides.

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