Purification and Characterization of Triacylglycerol Lipase from Aspergillus oryzae
スポンサーリンク
概要
- 論文の詳細を見る
Triacylglycerol lipase (L3) was purified from Aspergillus oryzae RIB128 by ammonium sulfate fractionation, acetone precipitation, anion-exchange chromatography, and gel filtration. The purified enzyme was formed from a glycoprotein and a monomeric protein with molecular masses of 25 and 29 kDa, by SDS-PAGE and gel filtration, respectively. The optimum pH at 40℃ was 5.5 and the optimum temperature at pH 5.5 was 40℃. The enzyme was stable between a pH range of 4.0-7.5 at 30℃ for 24 h, and at up to 30℃ at pH 5.5 for 1 h. Heavy metal ions, detergents, DFP, and DEP strongly inhibited the enzyme activity. The lipase hydrolyzed not only triacylglycerols but also monoacylglycerols and diacylglycerols. The enzyme had higher specificity toward triacylglycerols of middle-chain saturated fatty acids than short-chain or long-chain fatty acids. The enzyme had 1,3-positional specificity. The N-terminal amino acid sequence of the enzyme was not significantly similar to that of other lipases with published sequences.
- 社団法人日本農芸化学会の論文
- 1998-04-23
著者
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ARIKAWA YUKIHIKO
Food Technology Research Institute of Nagano Prefecture
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Amano Yoshihiko
Department Of Chemistry And Material Engineering Faculty Of Engineering Shinshu University
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FUKUZAWA MIKIO
Food Technology Research Institute of Nagano Prefecture
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Fukuzawa M
Food Technol. Res. Inst. Nagano Prefecture Nagano City Jpn
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Sekiguchi Junichi
Department Of Applied Biology Faculty Of Textile Science And Technology Shinshu University
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Arikawa Y
Department Of Chemistry And Material Engineering Faculty Of Engineering Shinshu University
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TOIDA Jinichi
Food Technology Research Institute of Nagano Prefecture
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KONDOU Kimio
Food Technology Research Institute of Nagano Prefecture
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Toida J
Food Technol. Res. Inst. Nagano Prefecture Nagano Jpn
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