Open AccessIsolation and some properties of extracellular amylases from Fusarium martii var. minus f.2
Author(s) -
Joanna Boguszewska
Publication year - 2014
Publication title -
acta mycologica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.38
H-Index - 5
eISSN - 2353-074X
pISSN - 0001-625X
DOI - 10.5586/am.1980.017
Subject(s) - amylase , extracellular , fusarium , enzyme , chemistry , biochemistry , stereochemistry , biology , botany
α-amylase and glucoamylase were isolated from the liquid culture medium of Fusarium martii. At 10-3 M concentrations PCMB inhibited the activity of both enzymes, which indicated that they require SH groups for enzymatic activity, α-amylase was also inhibited by DFP at 10-3 M. One may thus assume that serine is present in the active center of the examined amylase
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