ウシ乳清中のβ-Acetylglucosaminidase

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概要

• 論文の詳細を見る

• Some properties of β-acetylglucosaminidase in bovine milk whey have been studied. The optimum at pH 4.4 and the Km value 1.13±0.062 (S.D.) mM were obtained for the crude enzyme in whey, using p-nitrophenyl N-acetylglucosaminide as a substrate. By carboxy methyl cellulose column chromatography of the whey protein, most of the enzyme activities appeared as a peak (a) at pH 5.0 and two peaks (b_1 and b_2) at pH 5.5. The Km values for a, b_1,and b_2 were respectively 1.19±0.077,1.17±0.018,and 0.90±0.047 mM. Both the majority of the enzyme activities and the highest specific activity were found in "globulin and proteose-peptone fraction" obtained by the fractionation of whey protein with sodium sulfate. Heat stability of the enzyme in whey (at pH 4.4) and raw skimmed milk (at pH 6.9) was examined. The commercial milk sterilized by the ultrahigh temperature method did not show any β-acetylglucoaminidase activity.

• 社団法人日本薬学会の論文
• 1971-12-31

著者

• 田中 光也

  東邦大学薬学部

• 伊藤 之子

  Faculty of Pharmaceutical Sciences, Toho University

• 伊藤 之子

  東邦大学薬学部

• 内山 紀子

  東邦大学薬学部

• 伊藤 之子

  Faculty Of Pharmaceutical Sciences Toho University

関連論文

• The Rates of Hydrolysis of Some Substituted Phenyl 2-Acetamido-2-deoxy-α-and-β-D-glucopyranosides
• ウシ乳清中のβ-Acetylglucosaminidase

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