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Applied and Environmental Microbiology, October 1998, p. 4021-4027, Vol. 64, No. 10
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Purification and Substrate Specificities of Two alpha -L-Arabinofuranosidases from Aspergillus awamori IFO 4033

Satoshi Kaneko,1,dagger Mitsue Arimoto,1 Misako Ohba,1 Hideyuki Kobayashi,2 Tadashi Ishii,3 and Isao Kusakabe1,*

Institute of Applied Biochemistry, University of Tsukuba, 1-1-1 Tennoodai, Tsukuba,1 National Food Research Institute, Ministry of Agriculture, Forestry, and Fisheries,2 and Forestry and Forest Products Research Institute, Tsukuba Norin Kenkyu Danchinai,3 Ibaraki 305, Japan

Received 30 January 1998/Accepted 13 July 1998

alpha -L-Arabinofuranosidases I and II were purified from the culture filtrate of Aspergillus awamori IFO 4033 and had molecular weights of 81,000 and 62,000 and pIs of 3.3 and 3.6, respectively. Both enzymes had an optimum pH of 4.0 and an optimum temperature of 60°C and exhibited stability at pH values from 3 to 7 and at temperatures up to 60°C. The enzymes released arabinose from p-nitrophenyl-alpha -L-arabinofuranoside, O-alpha -L-arabinofuranosyl-(1right-arrow3)-O-beta -D-xylopyranosyl-(1right-arrow4)-D-xylopyranose, and arabinose-containing polysaccharides but not from O-beta -D-xylopyranosyl-(1right-arrow2)-O-alpha -L-arabinofuranosyl-(1right-arrow3)-O-beta -D-xylopyranosyl-(1right-arrow4)-O-beta -D-xylopyranosyl-(1right-arrow4)-D-xylopyranose. alpha -L-Arabinofuranosidase I also released arabinose from O-beta -D-xylopy-ranosyl-(1right-arrow4)-[O-alpha -L-arabinofuranosyl-(1right-arrow3)]-O-beta -D-xylopyranosyl-(1right-arrow4)-D-xylopyranose. However, alpha -L-arabinofuranosidase II did not readily catalyze this hydrolysis reaction. alpha -L-Arabinofuranosidase I hydrolyzed all linkages that can occur between two alpha -L-arabinofuranosyl residues in the following order: (1right-arrow5) linkage > (1right-arrow3) linkage > (1right-arrow2) linkage. alpha -L-Arabinofuranosidase II hydrolyzed the linkages in the following order: (1right-arrow5) linkage > (1right-arrow2) linkage > (1right-arrow3) linkage. alpha -L-Arabinofuranosidase I preferentially hydrolyzed the (1right-arrow5) linkage of branched arabinotrisaccharide. On the other hand, alpha -L-arabinofuranosidase II preferentially hydrolyzed the (1right-arrow3) linkage in the same substrate. alpha -L-Arabinofuranosidase I released arabinose from the nonreducing terminus of arabinan, whereas alpha -L-arabinofuranosidase II preferentially hydrolyzed the arabinosyl side chain linkage of arabinan.

* Corresponding author. Mailing address: Institute of Applied Biochemistry, University of Tsukuba, 1-1-1 Tennoodai, Tsukuba, Ibaraki 305, Japan. Phone: 81-298-53-6623. Fax: 81-298-53-4605.

dagger Present address: National Food Research Institute, Ministry of Agriculture, Forestry, and Fisheries, Ibaraki 305, Japan.

Applied and Environmental Microbiology, October 1998, p. 4021-4027, Vol. 64, No. 10
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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