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Cloning and Characterization of Cold-Adapted α-Amylase from Antarctic Arthrobacter agilis

Cited 3 time in scopus
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Title
Cloning and Characterization of Cold-Adapted α-Amylase from Antarctic Arthrobacter agilis
Other Titles
Cold-Adapted α-Amylase 특성연구
Authors
Kim, Su-mi
Choi, Jong-il
Park, Hyun
Subject
Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology
Keywords
Arthrobacter; Cold-adapted α-amylase
Issue Date
2017
Citation
Kim, Su-mi, Choi, Jong-il, Park, Hyun. 2017. "Cloning and Characterization of Cold-Adapted α-Amylase from Antarctic Arthrobacter agilis". APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 183(3): 1048-1059.
Abstract
In this study, the gene encoding an α-amylase from a psychrophilic Arthrobacter agilis PAMC 27388 strain was cloned into a pET-28a(+) vector and heterologously expressed in Escherichia coli BL21(DE3). The recombinant α-amylase with a molecular mass of about 80 kDa was purified by using Ni2+-NTA affinity chromatography. This recombinant α- amylase exhibited optimal activity at pH 3.0 and 30 °C and was highly stable at varying temperatures (30?60 °C) and within the pH range of 4.0?8.0. Furthermore, α-amylase activity was enhanced in the presence of FeCl3 (1 mM) and β-mercaptoethanol (5 mM), while CoCl2 (1 mM), ammonium persulfate (5 mM), SDS (10 %), Triton X-100 (10 %), and urea (1 %) inhibited the enzymatic activity. Importantly, the presence of Ca2+ ions and phenylmethylsulfonyl fluoride (PMSF) did not affect enzymatic activity. Thin layer chromatography (TLC) analysis showed that recombinant A. agilis α-amylase hydrolyzed starch, maltotetraose, and maltotriose, producing maltose as the major end product. These results make recombinant A. agilis α-amylase an attractive potential candidate for industrial applications in the textile, paper, detergent, and pharmaceutical industries.
URI
http://repository.kopri.re.kr/handle/201206/5684
DOI
http://dx.doi.org/10.1007/s12010-016-2267-5
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