상세 정보

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

Title 

Properties of laccase purified from nitrogen limited culture of white-rot fungus Coriolus Hirsutus

Authors 

Kwang-soo ShinChang Jin Kim

Publisher 

Springer

Issue Date 

1998

Citation 

Biotechnology Techniques, vol. 12, no. 2, pp. 101-104

Keywords 

CoriolusFungi

Abstract 

Laccase produced by nitrogen-limited culture of Coriolus hirsutus was purified to electrophoretic homogeneity (133-fold) with an overall yield of 40%. The molecular mass of the enzyme was determined as 82 kDa by SDS-PAGE and 80 kDa using gel filtration. It had a pl of 3.50. With ferulic acid and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate) (ABTS) as the substrate, the enzyme had optimal activity at pH 4.0 and 2.5, respectively. The enzyme was stable in the range pH 5.5 to 7.0 at 30 °C for 1 h. The enzyme was optimally active at 70 °C and it lost all activity within 15 min at 80 °C. The apparent K(m) value of enzyme toward ABTS was 67 °M and had highest affinity toward sinapinic acid. The enzyme was totally inhibited by 0.01 mM cysteine.

ISSN 

0951-208X

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)