상세 정보

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

Title 

Purification and characterization of the Bacillus sp. KK-1 β-xylosidase from a recombinant Escherichia coli

Authors 

Kyung Hwa JungYong Chin ChunJae Chan LeeSeung Hwan ParkKi Hong Yoon

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

1998

Citation 

Journal of Microbiology and Biotechnology, vol. 8, no. 3, pp. 258-263

Keywords 

Bacillusβ-xylosidasepurification4 nitrophenyl beta dextro glucopyranoside4 nitrophenyl beta dextro xylopyranosidebacterial enzymecarbohydratecarboxymethylcellulosedodecyl sulfate sodiumunclassified drug

Abstract 

β-Xylosidase was purified from the recombinant Escherichia coli carrying the Bacillus sp. KK-1 β-xylosidase gene (xylB). The molecular mass of the purified enzyme was estimated to be 62 kDa by sodium dodecyl sulfate- polyacrylamide gel electrophoresis. However, the apparent molecular mass of the β-xylosidase was 140 kDa, indicating that the native β-xylosidase has an oligomeric structure composed of two identical subunits. The isoelectric point was determined to be pH 5.5. The enzyme was highly active on p- nitrophenyl-β-D-xylopyranoside but it barely hydrolyzed xylan substrates, and did not exhibit activity towards carboxymethylcellulose and p- nitrophenyl-β-D-glucopyranoside. The enzyme had a pH optimum for its activity at pH 6.5 and a temperature optimum at 40°C. The enzyme activity was completely inhibited by the presence of Hg++, and also markedly inhibited by D-xylose and D-glucose.

ISSN 

1017-7825

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)