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Purification and Characterization of α‐Galactosidase from Feijão bean Phaseolus vulgaris
Author(s) -
BALDINI V. L. S.,
DRAETTA I. S.,
PARK YONG K.
Publication year - 1985
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1985.tb10591.x
Subject(s) - phaseolus , enzyme , chemistry , biochemistry , galactose , molecular mass , biology , botany
α‐Galactosidase is an important enzyme which degrades galactooligosaccharide in legumes. α‐Galactosidase from feijão beans was purified and its characteristics established. The purified enzyme exhibits multiple forms –enzymes I and II with molecular weights of 140,000 and 49,000 daltons, respectively. Optimum pH was 5.5 for enzyme I and 6.0 for enzyme II. Optimum temperature for both was 55°C. Kinetically, enzyme I is more reactive. Heavy metal ions completely inhibited both enzymes I and II. Galactose is a potential inhibitor for both enzymes.