Abstract：
:The kinetic and thermodynamic parameters of wheat β-amylase (WBA) were characterized and various additives were evaluated for enhancing its activity and thermostability. WBA activity was examined by neocuproine method using soluble starch as substrate. The Michaelis constant (K(m)) and molecular activity (k(cat)) were determined to be 1.0±0.1% (w/v) and 94±3s(-1), respectively, at pH 5.4 and at 25°C. The optimum reaction temperature (T(opt)) for WBA activity was 55°C and the temperature (T(50)) at which it loses half of the activity after 30-min incubation was 50±1°C. Modifications of the solvent with 182mM glycine and 0.18% (w/v) gelatin have increased the T(50) by 5°C. Glycerol, ethylene glycol, dimethylformamide (DMF) and dimethyl sulfoxide have also slightly enhanced the thermostability plausibly through weakening the water structure and decreasing the water shell around the WBA protein. Ethanol and DMF activated WBA by up to 24% at 25°C probably by inducing favorable conformation for the active site or changing the substrate structure by weakening the hydrogen bonding. Its half-life in the inactivation at 55°C was improved from 23 to 48min by 182mM glycine. The thermodynamic parameters indicate that WBA is thermo-labile and sufficient stabilization was achieved through solvent modification with additives and that the heat inactivation of WBA is entropic-driven. It is suggested that WBA could be applied more widely in starch-saccharification industries with employing suitable additives.
journal_name
Enzyme Microb Technoljournal_title
Enzyme and microbial technologyauthors
Daba T,Kojima K,Inouye Kdoi
10.1016/j.enzmictec.2012.07.004subject
Has Abstractpub_date
2012-10-10 00:00:00pages
245-51issue
5eissn
0141-0229issn
1879-0909pii
S0141-0229(12)00117-2journal_volume
51pub_type
杂志文章abstract：:Various recombinant proteins can be produced by the yeast Saccharomyces cerevisiae cell factories; therefore, efficient recombinant protein production techniques are desirable. In this study, to establish an efficient recombinant protein production technique in S. cerevisiae, the secretory production of recombinant pr...
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journal_title：Enzyme and microbial technology
pub_type： 评论,杂志文章
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journal_title：Enzyme and microbial technology
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journal_title：Enzyme and microbial technology
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abstract：:Glutaric acid is one of the promising C5 platform compounds in the biochemical industry. It can be produced chemically, through the ring-opening of butyrolactone followed by hydrolysis. Alternatively, glutaric acid can be produced via lysine degradation pathways by microorganisms. In microorganisms, the overexpression...
journal_title：Enzyme and microbial technology
pub_type： 杂志文章
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更新日期：2018-11-01 00:00:00
