Enzymological Characteristics of Lignin Peroxidase (LiP) from Coriolus versicolor

doi:10.7506/spkx1002-6630-201017050

FOOD SCIENCE ›› 2010, Vol. 31 ›› Issue (17 ): 224-227.doi: 10.7506/spkx1002-6630-201017050

• Bioengineering • Previous Articles Next Articles

Enzymological Characteristics of Lignin Peroxidase (LiP) from Coriolus versicolor

JIN Jian，KANG Wen-li，SHENG Ji-ping，CHENG Fan-sheng，WANG Quan-shuai，ZHANG Yan-xin，ZHANG Guo-peng，SHEN Lin

College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China

Received:2010-03-31 Online:2010-09-15 Published:2010-12-29
Contact: SHEN Lin E-mail:pingshen@cau.edu.cn

Abstract

Abstract:

In this paper, the enzymological characteristics of lignin peroxidase (LiP) from C. versicolor were investigated. The effects of temperature, pH, metal ions and compounds on the activity and stability of the enzyme were explored. Meanwhile, the relationship between substrate concentration and LiP activity was also studied, and the enzyme was measured for its Km. The highest enzyme activity was 72 U/mL when C. versicolor was cultured for up to 12 days. The optimal temperature and pH of the enzyme were 40 ℃ and 2.5, respectively. It exhibited a good stability in a range from 30 to 40 ℃ for temperature and from 2.0 to 3.5 for pH. Its activity could be activated by Zn2+ and inhibited by Ca2+, K+, Mg2+, Mn2+, Cu2+, EDTA, SDS and β-mercaptoethanol, while Na+ had no effect on its activity. The Km of the enzyme was 2.05 × 10-4 mol/L.

Key words: Coriolus versicolor, lignin peroxidase, temperature, pH, Km

CLC Number:

Q554.6

JIN Jian，KANG Wen-li，SHENG Ji-ping，CHENG Fan-sheng，WANG Quan-shuai，ZHANG Yan-xin，ZHANG Guo-peng，SHEN Lin. Enzymological Characteristics of Lignin Peroxidase (LiP) from Coriolus versicolor[J]. FOOD SCIENCE, 2010, 31(17 ): 224-227.

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Enzymological Characteristics of Lignin Peroxidase (LiP) from Coriolus versicolor

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