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Spectrophotometry on the Change in Conformation of Bacterial Alpha‐amylase, Characterized with 6m Urea
Author(s) -
Iwata Ken,
Hiromi Keitaro,
Ohnishi Masatake
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.19910430706
Subject(s) - urea , bacillus subtilis , chemistry , absorption (acoustics) , enzyme , amylase , phase (matter) , molecule , stereochemistry , crystallography , biochemistry , bacteria , organic chemistry , physics , biology , optics , genetics
Change in conformation of bacterial alpha‐amylase ( Bacillus subtilis , liquefying, BLA), induced with 6m urea, was observed on difference absorption‐ and optical rotation spectrophotometries as probes. Time courses of the latter were coincident with those of the former for the whole time range examined (‐110min). BLA‐catalyzed activity in 6m urea, the third probe, was found to show a biphasic time‐course. Phase I and Phase II, and to be lost at Phase II: Phase I is tolerant against the urea‐induced change in conformation. Hence, the active site may be conservative in an enzyme engineering on the BLA molecule.