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Effects of phospholipids on substrate specificity of beta-galactosidase purified from Aspergillus oryzae


Effects of phospholipids on substrate specificity of beta-galactosidase purified from Aspergillus oryzae



Archives of Biochemistry and Biophysics 215(1): 157-162



ISSN/ISBN: 0003-9861

PMID: 6807206

DOI: 10.1016/0003-9861(82)90290-9

When entrapped into liposomes composed of phosphatidylcholine and other lipids, .beta.-galactosidase (.beta.-D-galactoside galactohydrolase, EC 3.2.1.23) purified from A. oryzae could cleave the .beta.-galactosidic bond of the terminal galactose of galactocerebroside and GM1-ganglioside (II3NeuAc-GgOse4Cer, galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminosyl)-galactosylglucosylceramide), while the free enzyme could not. The products of the hydrolysis of galactocerebroside were .beta.-galactose and ceramide, which was confirmed by using a fluorescent analog of galactocerebroside, 1-O-galactosyl-2-N-(1-dimethylaminonaphthalene-5-sulfonyl)-sphingosine, as substrate. The formation of GM2-ganglioside (II3NeuAc-GgOse3Cer, N-acetylgalactosaminyl-(N-acetylneuraminosyl)-galactosylglucosylceramide) by the hydrolysis of GM1-ganglioside was demonstrated. The lipid composition of the liposomes influenced the amount of the enzyme entrapped and the activity of the trapped enzyme. A large amount of the enzyme was entrapped into the liposomes composed of phosphatidylcholine-cholesterol-stearoylamine (molar ratio, 7:2:1). The enzyme trapped in the liposomes and that in those of phosphatidylcholine-cholesterol-sulfatide (molar ratio, 7:2:1) had higher activity on galactocerebroside and GM1-ganglioside than that in other liposomes. The activity of .beta.-galactosidase trapped in liposomes was increased in the presence of detergent, while that of the free enzyme was not changed. By a similar procedure to introduce enzymes into hydrophobic environments, enzymes other than .beta.-galactosidase might come to possess different substrate specificities.

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Accession: 068643957

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