상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

Characterization and cloning of a phytase from Escherichia coli WC7

 

Escherichia coli WC7가 생산하는 phytase의 효소특성과 그 유전자의 클로닝

Authors 

Won Chan ChoiByung Chul OhHyung Kwoun KimSun Chul KangTae Kwang Oh

Publisher 

The Korean Society for Applied Microbiology and Biotechnology

Issue Date 

2002

Citation 

Korean Journal of Microbiology & Biotechnology, vol. 30, no. 1, pp. 1-7

Keywords 

escherichia colihistidine acid phosphatasephytasephytate4 nitrophenyl phosphateacid phosphataseamino acidsignal peptideamino acid sequencecloning

Abstract 

Phytase from Escherichia coli WC7 was purified from cell extracts and its molecular mass was estimated to be 45 kDa by SDS-PAGE. Its optimum temperature and pH for phytate hydrolysis was 60°C and pH 5.0, respectively. The enzyme was stable up to 60°C and over broad pH range (pH 2-12). The enzyme had higher affinity for sodium phytate than p-nitrophenylphosphate (pNPP). That is, the apparent Km value for sodium phytate and pNPP were 0.15 ± 0.02 mM and 2.82 ± 0.05 mM, respectively. The gene encoding the phytase was cloned in E. coli XL1-Blue. Sequence analysis showed an open reading frame of 1241 bp encoding a signal peptide (22 aa) and a mature enzyme (410 aa). WC7 phytase was expressed up to 17.5 U/ml in the transformed E. coli XL1-Blue/pUEP, which was 23-fold higher than the activity from wild strain.

ISSN 

0257-2389

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)