FOOD SCIENCE ›› 2022, Vol. 43 ›› Issue (2): 83-92.doi: 10.7506/spkx1002-6630-20201105-052

• Bioengineering • Previous Articles     Next Articles

Cloning, Expression and Characterization of α-L-Arabinofuranosidase from Aspergillus niger and Its Clarification Effect on Fruit Juice

PENG Cheng, XIAO Wenxi, NI Hui, LI Lijun, TAN Wansen, LIN Yanling, LI Qingbiao   

  1. (1. College of Food and Biological Engineering, Jimei University, Xiamen 361021, China; 2. College of Harbour and Environmental Engineering, Jimei University, Xiamen 361021, China; 3. Key Laboratory of Food Microbiology and Enzyme Engineering Technology of Fujian Province, Research Center of Food Biotechnology of Xiamen City, Xiamen 361021, China)
  • Online:2022-01-25 Published:2022-01-29

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Abstract: The sequence of the 1 887 bp long α-L-arabinofuranosidase gene in Aspergillus niger was cloned by using gene recombination, and was expressed in Pichia pastoris SMD1168. The recombinant protein had a molecular mass of 85 kDa and a specific activity of 55.73 U/mg. The optimal temperature and pH for the enzyme were 65 ℃ and 5.0, respectively. The enzymatic activity was promoted by Mn2+, while it was significantly inhibited by K+. When p-nitrophenyl-α-L-arabinofuranoside (pNPA) was used as the substrate, the Km and Vmax values of α-L-arabinofuranosidase were 2.31 mmol/L and 625 μmol/(mL·min), respectively. More interestingly, the purified α-L-arabinofuranosidase showed a significant clarification effect on citrus juice. This study not only enriches the resource library of α-L-arabinofuranosidase, but also provides a reference for juice processing with α-L-arabinofuranosidase.

Key words: Aspergillus niger; α-L-arabinofuranosidase; heterologous expression; enzymatic properties; clarification

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