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Purification and Characterization of the Commercialized, Cloned Bacillus megaterium α‐Amylase. Part II: Transferase Properties
Author(s) -
Brumm P. J.,
Hebeda R. E.,
Teague W. M.
Publication year - 1991
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.19910430807
Subject(s) - transferase , bacillus megaterium , hydrolysis , chemistry , starch , maltose , acceptor , enzyme , biochemistry , chromatography , electron acceptor , amylase , bacteria , biology , physics , genetics , condensed matter physics
Using an assay procedure based on reduction of iodine binding to starch. Bacillus megaterium , α‐amylase (BMA) demonstrated transferase activity using a wide range of acceptors. The enzyme had an absolute requirement for glucose or glucosides for acceptor molecules. Maltose acted as a transferase acceptor at low concentrations and as an inhibitor of starch hydrolysis at high concentrations. Kinetic analysis indicated that, in the presence of a suitable acceptor, the mechanism of starch hydrolysis is Ping Pong Bi Bi. The products of the transferase reaction have been determined using p‐nitro‐α‐D‐glucopyranoside as acceptor combined with a novel HPLC‐based system for product detection.