Cloning, expression, and characterization of a glycoside hydrolase family 50 beta-agarase from a marine Agarivorans isolate SCIE SCOPUS

Cited 44 time in WEB OF SCIENCE Cited 46 time in Scopus
Title
Cloning, expression, and characterization of a glycoside hydrolase family 50 beta-agarase from a marine Agarivorans isolate
Author(s)
Lee, Dong-Geun; Park, Geun-Tae; Kim, Nam Young; Lee, Eo-Jin; Jang, Min Kyung; Shin, Young Gyun; Park, Gwang-Seok; Kim, Tae-Min; Lee, Jae-Hwa; Lee, Jung-Hyun; Kim, Sang-Jin; Lee, Sang-Hyeon
KIOST Author(s)
Lee, Jung Hyun(이정현)
Publication Year
2006-12
Abstract
The gene for a thermostable beta-agarase from Agarivorans sp. JA-1 was cloned and sequenced. It comprised an open reading frame of 2,988 base pairs, which encode a protein of 109,450 daltons consisting of 995 amino acid residues. A comparison of the entire sequence showed that the enzyme has 98.8% sequence similarities to beta-agarase from Vibrio sp. JT1070, indicating that it belongs to the family glycoside hydrolase (GH)-50. The gene corresponding to a mature protein of 976 amino acids was inserted and expressed in Escherichia coli. The recombinant beta-agarase was purified to homogeneity. It had maximal activity at 40 degrees C and pH 8.0 in the presence of 1 mM NaCl and 1 mM CaCl2. The enzyme hydrolyzed agarose as well as neoagarohexaose and neoagarotetraose to yield neoagarobiose as the main product. Thus, the enzyme would be useful for the industrial production of neoagarobiose.
ISSN
0141-5492
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/4819
DOI
10.1007/s10529-006-9171-y
Bibliographic Citation
BIOTECHNOLOGY LETTERS, v.28, no.23, pp.1925 - 1932, 2006
Publisher
SPRINGER
Subject
PSEUDOMONAS-ATLANTICA; PURIFICATION; BACTERIUM; GENE
Keywords
beta-agarase; Agarivorans; cloning; expression
Type
Article
Language
English
Document Type
Article
Publisher
SPRINGER
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