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Title 

β-agarase from Pseudomonas sp. W7 : purification of the recombinant enzyme from Escherichia coli and the effects of salt on its activity

Authors 

Jeong-Chul HaGu-Taek KimSung-Koo KimTae Kwang OhJu-Hyun YuIn-Soo Kong

Publisher 

Portland Press

Issue Date 

1997

Citation 

Biotechnology and Applied Biochemistry, vol. 26, no. 1, pp. 1-6

Keywords 

beta agaraserecombinant enzymeenzyme activityenzyme purificationEscherichia coliPseudomonasrecombinant proteins

Abstract 

The recombinant plasmid (pJAI), harbouring the agarase gene (pjaA) of Pseudomonas sp. W7, was introduced and expressed in Escherichia coli JM83. The agarase was purified using a combination of acetone precipitation and anion-exchange, gel-filtration and affinity chromatographies, with overall yield of 10% from the culture supernatant of E. coli JM83 (pJAI). The purified agarase migrated as a single band (molecular mass 59 kDa) on SDS/PAGE and was found to be β-agarase, which could hydrolyse the β-1,4 linkage of agarose to yield neoagarotetraose as the main product. Optimal enzyme activity was at pH 7.8 and the temperature optimum spanned the broad range 20-40 °C. The recombinant agarase was halophilic, maximum activity being exhibited at 0.9 M NaCl. This halophilic property could improve the production of neoagaro-oligosaccharides available in a marine environment.

ISSN 

0885-4513

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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