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Changes in hydrolysis specificities of lipase from Rhizomucor miehei to polyunsaturated fatty acyl ethyl esters in different aggregation states
Alternative TitleJ. Am. Oil Chem. Soc.
Kosugi, Y; Chang, QL; Kanazawa, K; Nakanishi, H
1997-11-01
Source PublicationJOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY
ISSN0003-021X
Volume74Issue:11Pages:1395-1399
AbstractHydrolysis specificities of lipase from Rhizomucor miehei were compared for various fatty acyl ethyl esters. Activity yields of immobilized lipases, measured with 1 mM substrate, were more than 100%. Differences in hydrolysis rate and affinity for the substrates between lipase preparations were also typically higher during hydrolysis of substrates at 100 mM than at 1 mM, indicating better mass transfer effects for 1-mM substrates. The native lipase showed higher affinity for polyunsaturated fatty acid substrates at 1 mM than at 100 mM. Hydrolysis rates for 1-mM substrates were observed with immobilized lipases, fixed on anion exchange resin with glutaraldehyde and on cation exchange carrier with carbodiimide, and suggested some modification of the basic amino acid related to the lid of R. miehei lipase. Activation with these bifunctional reagents was not observed for 100-mM substrates, indicating that interfacial activation always occurred because of aggregation of 100-mM substrates. These results show that lipase from R. miehei recognizes molecular aggregation of lipids, and that various changes occur in the hydrolysis specificities for fatty acids.; Hydrolysis specificities of lipase from Rhizomucor miehei were compared for various fatty acyl ethyl esters. Activity yields of immobilized lipases, measured with 1 mM substrate, were more than 100%. Differences in hydrolysis rate and affinity for the substrates between lipase preparations were also typically higher during hydrolysis of substrates at 100 mM than at 1 mM, indicating better mass transfer effects for 1-mM substrates. The native lipase showed higher affinity for polyunsaturated fatty acid substrates at 1 mM than at 100 mM. Hydrolysis rates for 1-mM substrates were observed with immobilized lipases, fixed on anion exchange resin with glutaraldehyde and on cation exchange carrier with carbodiimide, and suggested some modification of the basic amino acid related to the lid of R. miehei lipase. Activation with these bifunctional reagents was not observed for 100-mM substrates, indicating that interfacial activation always occurred because of aggregation of 100-mM substrates. These results show that lipase from R. miehei recognizes molecular aggregation of lipids, and that various changes occur in the hydrolysis specificities for fatty acids.
KeywordAggregation Fatty Acid Immobilized Lipase Interfacial Activation Lipase Polyunsaturated Fatty Acid Specificity
SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences ; Life Sciences & Biomedicine
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Indexed ByISTP ; SCI
Language英语
WOS KeywordORGANIC MEDIA ; INTERFACIAL ACTIVATION ; ACIDS ; OIL ; IMMOBILIZATION
WOS Research AreaChemistry ; Food Science & Technology
WOS SubjectChemistry, Applied ; Food Science & Technology
WOS IDWOS:A1997YG66100008
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Cited Times:6[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/5872
Collection研究所(批量导入)
AffiliationCHINESE ACAD SCI,INST CHEM MET,BEIJING 100864,PEOPLES R CHINA
Recommended Citation
GB/T 7714
Kosugi, Y,Chang, QL,Kanazawa, K,et al. Changes in hydrolysis specificities of lipase from Rhizomucor miehei to polyunsaturated fatty acyl ethyl esters in different aggregation states[J]. JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY,1997,74(11):1395-1399.
APA Kosugi, Y,Chang, QL,Kanazawa, K,&Nakanishi, H.(1997).Changes in hydrolysis specificities of lipase from Rhizomucor miehei to polyunsaturated fatty acyl ethyl esters in different aggregation states.JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY,74(11),1395-1399.
MLA Kosugi, Y,et al."Changes in hydrolysis specificities of lipase from Rhizomucor miehei to polyunsaturated fatty acyl ethyl esters in different aggregation states".JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY 74.11(1997):1395-1399.
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