Introduction of Raw Starch-Binding Domains into Bacillus subtilis α-Amylase by Fusion with the Starch-Binding Domain of Bacillus Cyclomaltodextrin Glucanotransferase
In: Applied and Environmental Microbiology, Jg. 66 (2000-07-01), S. 3058-3064
Online
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Zugriff:
We constructed two types of chimeric enzymes, Ch1 Amy and Ch2 Amy. Ch1 Amy consisted of a catalytic domain of Bacillus subtilis X-23 α-amylase (Ba-S) and the raw starch-binding domain (domain E) of Bacillus A2-5a cyclomaltodextrin glucanotransferase (A2-5a CGT). Ch2 Amy consisted of Ba-S and D (function unknown) plus E domains of A2-5a CGT. Ch1 Amy acquired raw starch-binding and -digesting abilities which were not present in the catalytic part (Ba-S). Furthermore, the specific activity of Ch1 Amy was almost identical when enzyme activity was evaluated on a molar basis. Although Ch2 Amy exhibited even higher raw starch-binding and -digesting abilities than Ch1 Amy, the specific activity was lower than that of Ba-S. We did not detect any differences in other enzymatic characteristics (amylolytic pattern, transglycosylation ability, effects of pH, and temperature on stability and activity) among Ba-S, Ch1 Amy, and Ch2 Amy.
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Introduction of Raw Starch-Binding Domains into Bacillus subtilis α-Amylase by Fusion with the Starch-Binding Domain of Bacillus Cyclomaltodextrin Glucanotransferase
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Autor/in / Beteiligte Person: | Okada, Shigetaka ; Kuriki, Takashi ; Ohdan, Kohji ; Takata, Hiroki ; Kaneko, Hiroki |
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Zeitschrift: | Applied and Environmental Microbiology, Jg. 66 (2000-07-01), S. 3058-3064 |
Veröffentlichung: | American Society for Microbiology, 2000 |
Medientyp: | unknown |
ISSN: | 1098-5336 (print) ; 0099-2240 (print) |
DOI: | 10.1128/aem.66.7.3058-3064.2000 |
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