从蓖麻（Ricinus communis L.）中鉴定一种新型 sn1,3 脂肪酶，适合生产油酸-棕榈酸-甘油油酸酯。
Characterization of a novel sn1,3 lipase from Ricinus communis L. suitable for production of oleic acid-palmitic acid-glycerol oleate.
机构信息
Department of Food Science, Shenyang Agricultural University, Shenyang, 110866, People's Republic of China.
College of Life Sciences and Food Engineering, Inner Mongolia University for Nationalities, Tongliao, 028000, People's Republic of China.
出版信息
Sci Rep. 2021 Mar 25;11(1):6913. doi: 10.1038/s41598-021-86305-z.
The hydrolysis properties of lipase in castor was evaluated using two different substrate forms (tripalmitic glycerides and trioleic glycerides) to catalyze the reaction under different operational conditions. RcLipase was obtained from castor seeds and results show that RcLipase is a conservative serine lipase with a conserved catalytic center (SDH) and a conserved pentapeptide (GXSXG). This enzyme exhibited the greatest activity and tolerance to chloroform and toluene when it was expressed in Pichia pastoris GS115 at 40 ℃ and pH 8.0. Zn and Cu ions exerted obvious inhibitory effects on the enzyme, and displayed good hydrolytic activity for long-chain natural and synthetic lipids. HPLC analysis showed that this enzyme has 1,3 regioselectivity when glycerol tripalmitate and oleic acid are used as substrates. The fatty acid composition in the reaction product was 21.3% oleic acid and 79.1% sn-2 palmitic acid.
采用两种不同的底物形式（三棕榈酸甘油酯和三油酸甘油酯）来评估蓖麻油脂肪酶的水解特性，以在不同的操作条件下催化反应。RcLipase 是从蓖麻种子中获得的，结果表明 RcLipase 是一种保守的丝氨酸脂肪酶，具有保守的催化中心（SDH）和保守的五肽（GXSXG）。当在 40℃和 pH8.0 下在毕赤酵母 GS115 中表达时，该酶表现出最大的活性和对氯仿和甲苯的耐受性。Zn 和 Cu 离子对该酶表现出明显的抑制作用，并且对长链天然和合成脂质表现出良好的水解活性。HPLC 分析表明，当使用三棕榈酸甘油酯和油酸作为底物时，该酶具有 1,3 区域选择性。反应产物中的脂肪酸组成是 21.3%油酸和 79.1% sn-2 棕榈酸。
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