Purification and Characterization of the Commercialized, Cloned  Bacillus megaterium  α‐Amylase. Part II: Transferase Properties | Zendy

Brumm P. J. | Zendy; Hebeda R. E. | Zendy; Teague W. M. | Zendy

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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.

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