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 52 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)
-
Alternative Author(s)
- 이정현; 김상진
-
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
- Files in This Item:
-
There are no files associated with this item.
Items in ScienceWatch@KIOST are protected by copyright, with all rights reserved, unless otherwise indicated.