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Biochemical approaches of increasing thermostability of β‐amylase from Bacillus megaterium B 6
Author(s) -
Ray Rina Rani,
Jana Subhas Chandra,
Nanda Geeta
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01227-x
Subject(s) - thermostability , bacillus megaterium , amylase , chemistry , biochemistry , enzyme , biology , bacteria , genetics
Studies on the irreversible thermoinactivation of β‐amylase from Bacillus megaterium B 6 exposed to 60°C revealed that the deactivation mechanism probably results from the oxidation of thiols present at the active site of the enzyme. Several attempts were made to increase its thermostability, which indicated that Mn 2+ played a key role in determining thermostability and partially reactivating the inactivated enzyme. Immobilization of β‐amylase through gel‐entrapment and covalent crosslinking brought about a remarkable increase in thermotolerance with about a 14‐fold increase in catalytic half‐life.