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 Hea ; b ; c ; Jingbo Lia ; Sitharam Kodalia ; Bilian Chenb ; c ; chenbil@fjnu.edu.cn" class="auth_mail" title="E-mail the corresponding author ; Zheng Guoa ; 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
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Rationale for enzymatic concentration of n-3 PUFAs into glycerides is defined.
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Non-regiospecificity & high non-n-3 PUFAs preference are ideal catalytic feature.
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CAL-A identified as a near-ideal enzyme for concentrating n-3 PUFAs via ethanolysis.
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CAL-A affords concentration efficacy of n-3 PUFAs from 25% in oil to 90% in MAGs.
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13CNMR analysis verifies the conceptual hypothesis and reveals catalytic mechanism.