Insight into the Modification of Phosphatidylcholine with n-3 Polyunsaturated Fatty Acids-Rich Ethyl Esters by Immobilized MAS1 Lipase

Insight into the Modification of Phosphatidylcholine with n-3 Polyunsaturated Fatty Acids-Rich Ethyl Esters by Immobilized MAS1 Lipase
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深入探讨固定化 MAS1 脂肪酶用富含 n-3 多不饱和脂肪酸的乙酯修饰磷脂酰胆碱

DOI:
10.3390/molecules24193528
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发表时间:
2019-09
期刊:
影响因子:
4.6
通讯作者:
Wang Yonghua
Wang Yonghua
中科院分区:
化学2区
文献类型:
--
作者:
Wang Xiumei;Qin Xiaoli;Li Xiuting;Zhao Zexin;Yang Bo;Wang Yonghua

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本研究报告了在无溶剂体系中通过固定化 MAS1 脂肪酶催化的酯交换反应,用富含 n-3 多不饱和脂肪酸 (PUFA) 的乙酯 (EE) 修饰磷脂酰胆碱 (PC)。分别研究了富含n-3 PUFA的EE/PC质量比、酶负载量、反应温度和水用量对n-3 PUFA掺入PC的影响。结果表明,在富含n-3 PUFA的EE/PC质量比为6:1、加酶量为20%、反应温度为55 ℃、水用量为1.0%的条件下,n-3 PUFA在PC中的最大掺入量达到33.5%(24 h)。反应72小时后,n-3 PUFA与PC的结合率为43.55%,并通过31P核磁共振(NMR)分析反应混合物的组成。结果表明,反应产物由32.68% PC、28.76% 1-二酰基-sn-甘油-3-溶血磷脂酰胆碱(sn-1 LPC)、4.90% 2-二酰基-sn-甘油-3-溶血磷脂酰胆碱(sn-2 LPC)和33.60%组成。 sn-甘油-3-磷脂酰胆碱 (GPC)。这项研究深入了解了固定化 MAS1 脂肪酶的磷脂酶活性,并提出了固定化 MAS1 脂肪酶在工业用途磷脂修饰中的扩展应用。
This study reported the modification of phosphatidylcholine (PC) with n-3 polyunsaturated fatty acids (PUFA)-rich ethyl esters (EE) by immobilized MAS1 lipase-catalyzed transesterification in the solvent-free system. Effects of n-3 PUFA-rich EE/PC mass ratio, enzyme loading, reaction temperature, and water dosage on the incorporation of n-3 PUFA into PC were investigated, respectively. The results indicate that the maximum incorporation of n-3 PUFA into PC reached 33.5% (24 h) under the following conditions: n-3 PUFA-rich EE/PC mass ratio of 6:1, enzyme loading of 20%, reaction temperature of 55 °C, and water dosage of 1.0%. After 72 h of reaction, the incorporation of n-3 PUFA into PC was 43.55% and the composition of the reaction mixture was analyzed by 31P nuclear magnetic resonance (NMR). The results show that the reaction product consisted of 32.68% PC, 28.76% 1-diacyl-sn-glycero-3-lysophosphatidylcholine (sn-1 LPC), 4.90% 2-diacyl-sn-glycero-3-lysophosphatidylcholine (sn-2 LPC), and 33.60% sn-glycero-3-phosphatidylcholine (GPC). This study offers insight into the phospholipase activity of immobilized MAS1 lipase and suggests the extended applications of immobilized MAS1 lipase in the modification of phospholipids for industrial purpose.
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