Purification and Characterization of Laccase from Ganoderma weberianum

doi:10.7506/spkx1002-6300-201005045

FOOD SCIENCE ›› 2010, Vol. 31 ›› Issue (5): 201-205.doi: 10.7506/spkx1002-6300-201005045

• Bioengineering • Previous Articles Next Articles

Purification and Characterization of Laccase from Ganoderma weberianum

CHEN Qiong-hua1，ZHOU Yu-ping2，CHEN Xiao1，KE De-sen1，CHENG Hui-zhen2，TIAN Chang-en1,2,*

1. School of Life Sciences, Guangzhou University, Guangzhou 510006, China；2. Guangzhou Key Laboratory for Functional
Studies on Plant Stress-Resistant Genes, Guangzhou University, Guangzhou 510006, China

Received:2009-07-25 Revised:2009-11-11 Online:2010-03-01 Published:2010-12-29
Contact: TIAN Chang-en1 E-mail:changentian@yahoo.com.cn

Abstract

Abstract:

The laccase from Ganoderma weberianum TZC-1 was purified using fractional ammonium sulfate precipitation, dialysis, polyethylene glycol condensation and high performance liquid column chromatography. Compared to the crude extract, its purity exhibited a 37.1-fold improvement and the recovery rate of enzyme activity was 21.3%. Meanwhile, SDS-PAGE analysis revealed a single band with molecular weight of 40 kD. Moreover, the optimal reaction conditions of this laccase towards ABTS as substrate included 50－60 ℃ of reaction temperature and pH 4.6. The Km value was 13.8 μmol/L under these optimal reaction conditions. Furthermore, the activity of the enzyme exhibited excellent stability below 60 ℃ and pH 3.0－ 5.5, but could be inhibited by Fe2+, Al3+ and Mn2+ and enhanced by Hg+, Cu2+ and Mg2+. No obvious effect on laccase activity was observed due to Zn2+, Ba2+ and K+.

Key words: Ganoderma weberianum, laccase, purification, enzyme activity

CLC Number:

Q554

CHEN Qiong-hua1，ZHOU Yu-ping2，CHEN Xiao1，KE De-sen1，CHENG Hui-zhen2，TIAN Chang-en1,2,*. Purification and Characterization of Laccase from Ganoderma weberianum[J]. FOOD SCIENCE, 2010, 31(5): 201-205.

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Purification and Characterization of Laccase from Ganoderma weberianum

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