Rationale behind the near-ideal catalysis of Candida antarctica lipase A (CAL-A) for highly concentrating ω-3 polyunsaturated fatty acids into monoacylglycerols

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Rationale behind the near-ideal catalysis of Candida antarctica lipase A (CAL-A) for highly concentrating ω-3 polyunsaturated fatty acids into monoacylglycerols

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作者：Yongjin He^a ; ^b ; ^c ; Jingbo Li^a ; Sitharam Kodali^a ; Bilian Chen^b ; ^c ; ^{chenbil@fjnu.edu.cn" class="auth_mail" title="E-mail the corresponding author} ; Zheng Guo^a ; ^{guo@eng.au.dk" class="auth_mail" title="E-mail the corresponding author}
关键词：Docosahexaenoic acid (PubChem CID ; 445580) ; Ethanol (PubChem CID ; 702) ; Eicosapentaenoic acid (PubChem CID ; 446284) ; Palmitic acid (PubChem CID ; 985) ; Oleic acid (PubChem CID ; 445639) ; α-Linolenic acid (PubChem CID ; 5280934) ; Stearidonic acid (PubChem CID ; 5312508)
刊名：Food Chemistry
出版年：2017
出版时间：15 March 2017
年：2017
卷：219
期：Complete
页码：230-239
全文大小：689 K

文摘

•: Rationale for enzymatic concentration of n-3 PUFAs into glycerides is defined.
•: Non-regiospecificity & high non-n-3 PUFAs preference are ideal catalytic feature.
•: CAL-A identified as a near-ideal enzyme for concentrating n-3 PUFAs via ethanolysis.
•: CAL-A affords concentration efficacy of n-3 PUFAs from 25% in oil to 90% in MAGs.
•: ¹³CNMR analysis verifies the conceptual hypothesis and reveals catalytic mechanism.