刘壮1,刘萱1,罗日明2,陈东升3,杨博4,王卫飞1,蓝东明1.单、双甘油酯脂肪酶催化酯化合成高纯度山茶籽油丙二醇单酯[J].中国油脂,2022,47(11):.[IU Zhuang1, LIU Xuan1, LUO Riming2, CHEN Dongsheng3, YANG Bo4, WANG Weifei1,LAN Dongming1.Synthesis of high purity propylene glycol monoesters from oil-tea camellia seed oil catalyzed by mono- and diacylglycerol lipases[J].China Oils and Fats,2022,47(11):.]
单、双甘油酯脂肪酶催化酯化合成高纯度山茶籽油丙二醇单酯
Synthesis of high purity propylene glycol monoesters from oil-tea camellia seed oil catalyzed by mono- and diacylglycerol lipases
  
DOI:
中文关键词:  丙二醇单酯  山茶籽油  单、双甘油酯脂肪酶  酶催化
英文关键词:propylene glycol monoester  oil-tea camellia seed oil  mono- and diacylglycerol lipase  enzymatic catalysis
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作者单位
刘壮1,刘萱1,罗日明2,陈东升3,杨博4,王卫飞1,蓝东明1 1.华南理工大学 食品科学与工程学院广州 510640 2.广东粤膳特医营养科技有限公司广东 佛山 528226 3.中粮工科(西安)国际工程有限公司西安 710082 4.华南理工大学 生物科学与工程学院广州 510640 
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中文摘要:
      为了提高丙二醇酯合成中的单酯比例,以山茶籽油脂肪酸为原料,以单、双甘油酯脂肪酶Lipase AOL、Lipase G Amano 50为催化剂酯化合成丙二醇单酯,考察了加酶量、反应温度、底物物质的量比以及摇床转速对酯化反应合成丙二醇单酯的影响,并对产物进行了鉴定,与Lipase SMG1-F278N催化酯化效果进行了比较。结果表明,Lipase AOL、Lipase G Amano 50催化酯化合成丙二醇单酯的最佳反应条件为Lipase AOL加酶量80 U/g、底物(山茶籽油脂肪酸与丙二醇)物质的量比1∶4,Lipase G Amano 50加酶量100 U/g、底物物质的量比1∶2,反应温度35℃,摇床转速180 r/min,反应时间18 h,在此条件下Lipase AOL、Lipase G Amano 50催化酯化合成的丙二醇单酯含量分别达到85.55%和72.98%。经GC-MS鉴定合成的丙二醇单酯主要由丙二醇单油酸酯、丙二醇单棕榈酸酯和丙二醇单亚油酸酯组成。与Lipase G Amano 50、Lipase SMG1-F278N相比,Lipase AOL催化酯化合成的丙二醇单酯含量和纯度更高,更适合作为丙二醇单酯的催化合成用酶。
英文摘要:
      To improve the proportion of monoesters in the synthesis of propylene glycol esters, the synthesis of propylene glycol monoesters was catalyzed by the esterification of mono- and diacylglycerol lipases Lipase AOL and Lipase G Amano 50 with oil-tea camellia seed oil fatty acids as raw materials. The effects of enzyme addition, reaction temperature, substrate molar ratio and rotational speed on the synthesis of propylene glycol monoesters by esterification reaction were investigated, and the products were identified and compared with Lipase SMG1-F278N catalyzed esterification. The results showed that the optimal reaction conditions for the synthesis of propylene glycol monoesters by Lipase AOL and Lipase G Amano 50 were as follows: Lipase AOL with 80 U/g of addition and 1∶4 molar ratio of oil-tea camellia seed oil fatty acids to 1,3- propylene glycol, Lipase G Amano 50 with 100 U/g of addition and 1∶2 molar ratio of oil-tea camellia seed oil fatty acids to 1,3- propylene glycol, reaction temperature 35℃, reaction time 18 h, and rotational speed 180 r/min. Under these conditions, the contents of propylene glycol monoesters reached 85.55% and 72.98% by Lipase AOL and Lipase G Amano 50 catalyzed esterification. The synthesized propylene glycol monoesters were identified by GC-MS as consisting of propylene glycol monopalmitate, propylene glycol monolinoleate and propylene glycol monooleate. Compared with Lipase G Amano 50 and Lipase SMG1-F278N, Lipase AOL catalyzed the synthesis of propylene glycol monoesters with higher content and purity, and it was more suitable as an enzyme for the catalytic synthesis of propylene glycol monoesters.
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