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KMID : 0380020040190060489
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Korean Journal of Biotechnology and Bioengineering
2004 Volume.19 No. 6 p.489 ~ p.493
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Investigation of Acyl Chain Specificity of Lipase-OF 360,000 on the Hydrolysis of Fish Oil
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Park Ji-Sook
Kim Han-Ok
Koh Hea-Won
Hur Byung-Ki
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Abstract
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The hydrolysis characteristics of various fatty acids composing the fish oil was investigated for function of acyl chain specificities using Lipase-OF 360,000 from Candida cylindracea. The hydrolysis of fatty acids decreased with the increase of the number of carbon and double bond in the fatty acids, in case that the number of double bond and the position of the first double bond from the methyl group of fatty acids were the same. The position of the first double bond was found to be an acyl chain specificity of Lipase-OF 360,000 for the hydrolysis of fish oil. Lipase-OF 360,000 also showed the another acyl chain specificity that the increase of double bond of fatty acids, having the same number of carbon and the position of double bond, brought about the decrease of hydrolysis.
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KEYWORD
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Hydrolysis, Acyl chain specificity, Candida cylindracea, Lipase-OF 360, 000
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