.alpha.-glucosidase, and a process for producing the same

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

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435 96, 435200, 4352525, C12P 1920, C12N 926, C12N 120

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active

058277200

ABSTRACT:
The present invention relates to novel .alpha.-glucosidase being excellent in stability to heat and pH, and hydrolyzing .alpha.-glucoside linkages to form .alpha.-D-glucose, acting on maltose, maltotriose, maltotetraose, PNPG, PNPG2, isomaltose and sucrose, but hardly acting on maltooligosaccharides with a degree of polymerization of maltopentaoside or more, and completely not acting on soluble starch, as well as to a process for producing the same by use of a strain belonging to the genus Bacillus capable of producing .alpha.-glucosidase. .alpha.-Glucosidase which is useful as a coupling enzyme for quantification such as measurement of .alpha.-amylase activity, or in formation of monosaccharides such as glucose and fructose etc., from oligosaccharides, and enzymatic synthesis of heterooligosaccharides, can be produced easily and inexpensively.

REFERENCES:
Mikio Yamamoto et al., Purification and Properties of an Oligo-1,6-D-Glucosidase From an Alkalophilic Bacillus Species. Carbohydrate Research, 197, (1990) 227-235.
Yuzuru Suzuki et al., Assignment of ap-Nitrophenyl .alpha.-D-Glucopyranosidase of Bacillus Stearothermophilus ATCC 12016 to a Novel Exo-.alpha.-1,4-Glucosidase Active for Oligomaltosaccharides and .alpha.-Glucans, Biochimica et Biophysica Acta, 787, (1984)281-289.
Yuji Oda et al., Purification and Characterization of .alpha.-Glucosidase from Torulaspora pretoriensis YK-1, Biosci. Biotech. Biochem., 57(11), 1902-1905, 1993.

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