Co-immobilized Lignin Peroxidase and Manganese Peroxidase From Coriolus Versicolor Capable of Decolorizing Molasses Waste Water
被引:10
作者:
Ran, Yanhong
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机构:
Jinan Univ, Coll Life Sci & Technol, Guangzhou 510632, Guangdong, Peoples R ChinaJinan Univ, Coll Life Sci & Technol, Guangzhou 510632, Guangdong, Peoples R China
Ran, Yanhong
[1
]
Che, Zhifei
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h-index: 0
机构:
Jinan Univ, Coll Life Sci & Technol, Guangzhou 510632, Guangdong, Peoples R ChinaJinan Univ, Coll Life Sci & Technol, Guangzhou 510632, Guangdong, Peoples R China
Che, Zhifei
[1
]
Chen, Wanqun
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机构:
Jinan Univ, Med Coll, Guangzhou 510632, Guangdong, Peoples R ChinaJinan Univ, Coll Life Sci & Technol, Guangzhou 510632, Guangdong, Peoples R China
Chen, Wanqun
[2
]
机构:
[1] Jinan Univ, Coll Life Sci & Technol, Guangzhou 510632, Guangdong, Peoples R China
[2] Jinan Univ, Med Coll, Guangzhou 510632, Guangdong, Peoples R China
来源:
APPLIED MECHANICS AND MECHANICAL ENGINEERING II, PTS 1 AND 2
|
2012年
/
138-139卷
This paper explains how the Lignin peroxidase and Manganese Peroxidase from Coriolus Versicolor were co-immobilized by chitosan microspheres. It studies kinetic character of the enzyme after co-immobilization. Optimum Lip and MnP activity obtained at 30-35 degrees C for 14 hours in pH 8.4 glutaraldehyde solutions during immobilized to chitosan microspheres which prepared by coagulation in NaOH: methanol=3:2. When kept at 50 degrees C for 6h, more than 80% of the immobilized enzyme activity remained, while the free enzymes were inactive under the same conditions. The co-immobilized enzyme can remain 70% activity after two weeks while both of the free enzymes inactive. Compared with the free enzymes, temperature and time stability of the co-immobilized enzyme was considerably improved.