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J. Biochem, 1987, Vol. 101, No. 4 847-854
© 1987 Japanese Biochemical Society

other

Purification and Properties of ß-D-Glucosidase (Linamarase) from the Butter Bean, Phaseolus lunatus1

Tomoko ITOH-NASHIDA, Masao HIRAIWA and Yutaka UDA

Laboratory of Health Chemistry, Niigata College of Pharmacy Niigata, Niigata 950–21

A ß-D-glucosidase (linamarase) was purified 11,700-fold from the butter bean, Phaseolus lunatus L., by means of successive procedures including extraction, ammonium sulfate fractionation, acetone treatment, and chromatographies on CM-Sephadex, DEAE-Sephadex, and Sephadex G-200. The final preparation gave a single protein band on both disc polyacrylamide gel electrophoresis and SDS-polyacrylamide gel electrophoresis. In spite of its electrophoretic purity, the final enzyme preparation showed four glycosidase activities; ß-D-glucosidase, ß-D-galactosidase, ß-D-fucosidase, and ß-D-xylosidase. The molecular weight of the enzyme was determined to be 124,000 ±9,000 by Sephadex G-200 gel filtration, and 59,000±2,400 by SDS-disc gel electrophoresis. The enzyme showed a pH optimum in the range of 5.1 to 6.0 with p-nitrophenyl ß-D-glucoside, 4-methylumbelliferyl ß-D-glucoside, and linamarin. Among natural substrates containing a ß-glucosyl terminal, linamarin, prunasin, and salicin were hydrolyzed by the enzyme from butter beans, but amygdalin, cellobiose, gentiobiose, and laminarin were hardly hydrolyzed.

1This study was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Health and Welfare of Japan.


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