Biodegradation of feather wastes and the purification and characterization of a concomitant keratinase from Paecilomyces lilacinus

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• 作者：Q. Y. Wang (1)
  M. D. Liao (1)
  
• 刊名：Applied Biochemistry and Microbiology
• 出版年：2014
• 出版时间：May 2014
• 年：2014
• 卷：50
• 期：3
• 页码：279-285
• 全文大小：
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• 作者单位：Q. Y. Wang (1)
  M. D. Liao (1)
  
  1. Key Lab of Natural Pesticide and Chemical Biology of Ministry of Education, College of Resources and Environment, South China Agricultural University, Guangzhou, Guangdong, 510642, China
  
• ISSN：1608-3024

文摘

Paecilomyces lilacinus strain PL-HN-16 was found to have the ability to degrade feathers. During the degradation process, the broth initially turned as sticky as gelatin and then turned into fluid that means the feathers can be hydrolyzed completely. Keratinolytic protein (Ker) of aforementioned strain was purified using ammonium sulphate precipitation, HiTrap?Butyl FF chromatography and Sephacryl S-200 gel filtration. The Ker of P. lilacinus PL-HN-16 had molecular mass of 33 kDa, the optimum pH 8.0 and temperature optimum at 40°C. It used the soluble keratin as substrate. The enzyme showed high activity and stability over a wide range of pH (6.0 to 10.0) and temperature (30°C to 60°C) values but was completely inhibited by PMSF. Ker of P. lilacinus PL-HN-16 exhibited stability toward SDS. These promising properties make the enzyme a potential candidate for future applications in biotechnological processes as keratin hydrolysis and dehairing during leather processing.