Abstract：
:Amylosucrase (ASase) has great industrial potential owing to its multifunctional activities, including transglucosylation, polymerization, and isomerization. In the present study, the properties of Deinococcus geothermalis ASase (DGAS) expressed in Corynebacterium glutamicum (cDGAS) and purified via Ni-NTA affinity chromatography were compared to those of DGAS expressed in Escherichia coli (eDGAS). The pH profile of cDGAS was similar to that of eDGAS, whereas the temperature profile of cDGAS was lower than that of eDGAS. The melting temperature of both enzymes did not differ significantly. Interestingly, polymerization activity was slightly lower in cDGAS than in eDGAS, whereas luteolin (an acceptor molecule) transglucosylation activity in cDGAS was 10 % higher than that in eDGAS. Analysis of protein secondary structure via circular dichroism spectroscopy revealed that cDGAS had a lower strand/helix ratio than eDGAS. The present results indicate that cDGAS is of greater industrial significance than eDGAS.
journal_name
Enzyme Microb Technoljournal_title
Enzyme and microbial technologyauthors
Chin YW,Jang SW,Shin HS,Kim TW,Kim SK,Park CS,Seo DHdoi
10.1016/j.enzmictec.2019.109505subject
Has Abstractpub_date
2020-04-01 00:00:00pages
109505eissn
0141-0229issn
1879-0909pii
S0141-0229(19)30243-1journal_volume
135pub_type
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journal_title：Enzyme and microbial technology
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journal_title：Enzyme and microbial technology
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journal_title：Enzyme and microbial technology
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journal_title：Enzyme and microbial technology
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