Purification and characterization of pectin lyase secreted by Aspergillus flavus MTCC 10938

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• 作者：S. Yadav (16512)
  A. K. Dubey (16512)
  G. Anand (16512)
  D. Yadav (16512)
  
• 刊名：Applied Biochemistry and Microbiology
• 出版年：2013
• 出版时间：July 2013
• 年：2013
• 卷：49
• 期：4
• 页码：400-405
• 全文大小：246KB
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• 作者单位：S. Yadav (16512)
  A. K. Dubey (16512)
  G. Anand (16512)
  D. Yadav (16512)
  
  16512. Department of Biotechnology, D.D.U. Gorakhpur University, Gorakhpur, 273009, India
  

文摘

An indigenously isolated fungal strain Aspergillus flavus MTCC 10938 was subjected to pectin lyase (PNL) production under submerged fermentation conditions. The enzyme was purified to homogeneity from the culture filtrate of the fungus involving concentration by ultrafiltration, anion exchange chromatography on DEAE cellulose and gel filtration chromatography on Sephadex G-100. The purified PNL gave a single protein band in SDS-PAGE analysis with a relative molecular mass corresponding to 50 kDa. Using citrus pectin as the substrate the K m and k cat values of the enzyme were obtained as 1.7 mg/ml and 66 s?, respectively. The optimum pH of the purified PNL from A. flavus MTCC 10938 was 8.0 and up to 90% of its activity retained in the pH range from 3.0 to 11.0 after 24 h incubation. The optimum temperature of the purified enzyme was revealed at 55°C and it was completely stable up to 40°C when exposed for 30 min. The purified A. flavus MTCC 10938 PNL showed efficient retting of Crotalaria juncea fibres.