Purification and Characterization of a Glucose-tolerant β-Glucosidase from Aspergillus niger CCRC 31494

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概要

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• An extracellular glucose-tolerant β-glucosidase was purified to homogeneity by alcohol fractionation and preparative isoelectric focusing from Aspergillus niger CCRC 31494. The enzyme was a dimeric protein with a subunit of 49,000, and had its optimum activity at pH 5.0 and 55℃. The enzyme was completely inhibited by 5 mM Ag^+. Thiol groups and serine residues were not essential for its activity. Low concentrations of alcohols (10%) except for methanol could activate the enzyme. It was very specific for para-nitrophenyl-β-D-glucoside (pNPG) and cellobiose. However, the enzyme also had some β-xylosidase activity, but showed no activity towards x-linked glycosidic substrates. The V_<max> of 124.4 U/mg and 21.6 U/mg were found for pNPG (K_m = 21.7 mM) and para-nitrophenyl-β-D-xyloside (pNPX) (K_m = 14.2 mM), respectively. The enzyme was tolerant to glucose inhibition with a K_i of 543 mM, while fructose, galactose, mannose, and xylose were not inhibitory.

• 社団法人日本農芸化学会の論文
• 1997-06-23

著者

• Yan T‐r

  Laboratory Of Biochemistry Department Of Bioengineering Tatung Institute Of Technology

• YAN Tsong-Rong

  Laboratory of Biochemistry, Department of Bioengineering, Tatung Institute of Technology

• LIN Chun-Lieh

  Laboratory of Biochemistry, Department of Bioengineering, Tatung Institute of Technology

• Lin Chun-lieh

  Laboratory Of Biochemistry Department Of Bioengineering Tatung Institute Of Technology

関連論文

• Purification and Characterization of a Glucose-tolerant β-Glucosidase from Aspergillus niger CCRC 31494

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