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KMID : 1160619960010020244
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Preventive Nutrition and Food Science
1996 Volume.1 No. 2 p.244 ~ p.251
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Purification and Amino Acid Sequence of the Linoleate Isomerase Produced from Butyrivibrio fibrisolvens A-38
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Park Sook-Jahr
Park Kyung-Ah
Park Cherl-Woo
Park Won-Seck
Kim Jeong-Ok
Ha Yeong-Lae
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Abstract
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Molecular weight and partial amino acid sequence of the cis, 9-cis, 12-octadecadienoate isomerase(linoleate isomerase) of Butyrivibrio fibrisovens A-38 were determined. Linoleate isomerase was isolated from the bac-teria cultured anaerobically and purified by ultracentrifugation in conjunction with Sepharose 6B column chro-matography, Phenyl sepharose 4B column chromatography and fast performance liquid chromatography (EPLC). The isomerase was single polypeptide with 19KD of molecular weight, when determined by SDS-PAGE. Fourteen amino acids sequence of N-terminal of the linoleate isomerase was N-GEIDKYPRIIKQQ determined by Edman method.
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KEYWORD
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conjugated linoleic acid(CLA), linoleate isomerase, Butyrivibrio fibrisolvens
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