| 潘骊燕1,2，方慧2，邓媛元2，曾嘉锐2，赵志浩2，刘光2，周鹏飞2，张名位1,2.大孔树脂负载黑曲霉脂肪酶及其催化酶法
甘油解制备甘油二酯研究[J].中国油脂,2025,50(10):.[PAN Liyan1,2, FANG Hui2, DENG Yuanyuan2, ZENG Jiarui2,
ZHAO Zhihao2, LIU Guang2, ZHOU Pengfei2, ZHANG Mingwei1,2.Immobilization of Aspergillus niger lipase onto macroporous resin and its catalysis in diacylglycerols production by enzymatic glycerolysis[J].China Oils and Fats,2025,50(10):.] |
| 大孔树脂负载黑曲霉脂肪酶及其催化酶法
甘油解制备甘油二酯研究 |
| Immobilization of Aspergillus niger lipase onto macroporous resin and its catalysis in diacylglycerols production by enzymatic glycerolysis |
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出版日期：
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| DOI：10.19902/j.cnki.zgyz.1003-7969.240550 |
| 中文关键词: 大孔吸附树脂 固定化 国产脂肪酶 甘油二酯 甘油解反应 稻米油 |
| 英文关键词:macroporous adsorption resin immobilization domestic lipase diacylglycerols glycerolysis reaction rice bran oil |
| 基金项目:广东省重点领域研发计划项目（2022B0202010003） |
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| Author Name | Affiliation | | PAN Liyan1,2, FANG Hui2, DENG Yuanyuan2, ZENG Jiarui2,
ZHAO Zhihao2, LIU Guang2, ZHOU Pengfei2, ZHANG Mingwei1,2 | 1.College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088,
Guangdong,China
2.Guangdong Key Laboratory of Agricultural Products Processing, Key
Laboratory of Functional Foods of Ministry of Agriculture and Rural Affairs, Sericultural & Agri-Food
Research Institute, Guangdong Academy of Agricultural Sciences,Guangzhou 510610, China |
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| 中文摘要: |
| 旨在为国产固定化脂肪酶替代进口脂肪酶酶法制备功能性脂质甘油二酯（DAG）提供参考，采用3种大孔吸附树脂（SA-1、NKA-9、XAD1180）分别对国产黑曲霉脂肪酶（ANL）进行固定化，通过对比不同树脂固定化ANL的效果筛选适宜的固定化载体，在此基础上制备固定化ANL，对其进行扫描电子显微镜（SEM）和傅里叶变换红外光谱（FTIR）表征，并将其用于催化稻米油甘油解反应制备DAG中。采用单因素实验探究底物质量比、反应温度、反应时间以及加酶量对甘油解反应的影响，通过高效液相色谱（HPLC）分析了甘油解反应前后稻米油组分的变化，同时考察了固定化脂肪酶的再利用稳定性。结果表明：以XAD1180为固定化载体制备的固定化脂肪酶XAD1180-ANL比活力较高；通过SEM、FTIR表征发现ANL被成功地固定在载体上；XAD1180-ANL催化稻米油甘油解反应制备DAG的最适反应条件为反应底物(稻米油与甘油)质量比3∶ 1、加酶量5%（以稻米油质量计）、反应温度40 ℃、反应时间28 h，在此条件下产物中DAG含量为45.04%；HPLC分析表明，甘油解反应后，稻米油中DAG含量增加，甘油三酯含量减少，XAD1180-ANL具有良好的再利用稳定性，重复使用10次后催化合成DAG的活力为初始的63.09%。综上，XAD1180-ANL具有较好的催化甘油解反应制备DAG的性能及再利用稳定性，可作为酶法催化制备功能性脂质DAG反应用酶。 |
| 英文摘要: |
| To provide a reference for the substitution of imported lipases with domestic immobilized lipases in the enzymatic preparation of functional lipids diacylglycerols (DAG), three types of macroporous adsorption resins (SA-1, NKA-9, and XAD1180) were used to immobilize Aspergillus niger lipase (ANL). The effects of different resins on the immobilization of ANL were compared to select the most suitable immobilization carrier. Based on this, immobilized lipase was prepared and characterized by scanning electron microscopy (SEM) and Fourier-transform infrared spectroscopy (FTIR). The immobilized lipase was then used to catalyze the glycerolysis of rice bran oil to produce DAG. Single-factor experiments were conducted to explore the effects of substrate mass ratio, reaction temperature, reaction time, and enzyme dosage on the glycerolysis reaction. The components in rice bran oils before and after glycerolysis were determined by HPLC. In addition, the reusability of the immobilized lipase was also examined.The results showed that the immobilized lipase XAD1180-ANL, prepared with XAD1180 as the carrier, exhibited higher enzyme activity. SEM and FTIR characterizations confirmed that ANL was successfully immobilized onto the carrier. The optimal reaction conditions for the glycerolysis of rice bran oil catalyzed by XAD1180-ANL to produce DAG were as follows: substrate mass ratio (rice bran oil to glycerol) 3∶ 1, enzyme dosage 5% (based on the mass of rice bran oil),reaction temperature 40 ℃, and reaction time 28 h. Under these conditions, the DAG content in the product reached 45.04%. HPLC analysis indicated that the DAG content in rice bran oil increased, while the triacylglycerol content decreased after the glycerolysis reaction. The immobilized lipase XAD1180-ANL demonstrated good reusability. After 10 repeated uses, its catalytic activity for DAG synthesis remained at 63.09% of the initial activity. In summary, the immobilized lipase XAD1180-ANL exhibits excellent performance and reusability in catalyzing the glycerolysis reaction to produce DAG, making it a suitable enzyme for the enzymatic preparation of functional lipids of DAG. |
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