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Title 

Catalytic properties of the cloned amylase from Bacillus licheniformis

Authors 

In-Cheol KimJae-Ho ChaJung-Ryul KimSo-Young JangByung-Cheol SeoTae-Kyou CheongDae Sil LeeYang Do ChoiKwan-Hwa Park

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

1992

Citation 

Journal of Biological Chemistry, vol. 267, no. 31, pp. 22108-22114

Keywords 

amylasebacillus licheniformisamylasesbacillus

Abstract 

A gene encoding a new amylolytic enzyme of Bacillus licheniformis (BLMA) has been cloned, and we characterized the enzyme expressed in Escherichia coli. The genomic DNA of B. licheniformis was double-digested with EcoRI and BamHI and ligated the pBR322. The transformed E. coli was selected by its amylolytic activity, which carries the recombinant plasmid pIJ322 containing a 3.5-kilobase fragment of B. licheniformis DNA. The purified enzyme encoded by pIJ322 was capable of hydrolyzing pullulan and cyclodextrin as well as starch. It was active over a pH range of 6-8 and its optimum temperature was 50 °C. The molecular weight of the enzyme was 64,000, and the isoelectric point was 5.4. It degraded soluble starch by cleaving maltose units preferentially but did not attack α-1,6-linkage. The enzyme also hydrolyzed pullulan to panose units exclusively. In the presence of glucose, however, it transferred the panosyl moiety to glucose with the formation of α-1,6- linkage. The specificity of transferring activity is evident from the result of the maltosyl-transferring reaction which produces isopanose from maltotriose and glucose. The molecular structure of the enzyme deduced from the nucleotide sequence of the clone maintains limited similarity in the conserved regions to the other amylolytic enzymes.

ISSN 

0021-9258

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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