Selective synthesis of triacylglycerols by the ADS-17-supported Candida antarctica lipase B through esterification of oleic acid and glycerol

IF 3.5 2区 农林科学 Q1 AGRICULTURE, MULTIDISCIPLINARY Journal of the Science of Food and Agriculture Pub Date : 2025-01-21 DOI:10.1002/jsfa.14137
Jiawei Zheng, Qiangyue Zhang, Nanjing Zhong
{"title":"Selective synthesis of triacylglycerols by the ADS-17-supported Candida antarctica lipase B through esterification of oleic acid and glycerol","authors":"Jiawei Zheng,&nbsp;Qiangyue Zhang,&nbsp;Nanjing Zhong","doi":"10.1002/jsfa.14137","DOIUrl":null,"url":null,"abstract":"<div>\n \n \n <section>\n \n <h3> BACKGROUND</h3>\n \n <p>Immobilized enzyme possessing both high activity and good selectivity is important in practice. In this study, <i>Candida antarctica</i> lipase B (CALB) was immobilized onto the macroporous resin ADS-17 for triacylglycerol (TAG) synthesis through esterification of oleic acid and glycerol. The reaction conditions were optimized by single-factor study and orthogonal test, and the reusability of the immobilized CALB (CALB@ADS-17) was evaluated. In addition, the mechanism of lipase immobilization was studied and the catalytic mechanism of CALB@ADS-17 was investigated.</p>\n </section>\n \n <section>\n \n <h3> RESULTS</h3>\n \n <p>Oleic acid conversion up to 99.20% and TAG content at 91.58 wt% could be obtained under optimal conditions. In addition, the CALB@ADS-17 retained 84.28% of its initial activity after 11 cycles of reuse. The mechanism of lipase immobilization was through hydrophobic adsorption. The relationship between temperature and oleic acid conversion was ln<i>V</i><sub>0</sub> = 6.3316 − 4.3321/<i>T</i>, and the activation energy (<i>E</i><sub>a</sub>) was 36.02 kJ mol<sup>−1</sup>. CALB@ADS-17 did not exhibit an obvious interfacial activation phenomenon. Its kinetic behavior can be described by the Michaelis–Menten model, whose kinetic parameters of <i>v</i><sub>max</sub>, <i>k</i><sub>cat</sub>, <i>K</i><sub>m</sub>, <i>K</i><sub><i>i</i></sub>, and <i>k</i><sub>ca<i>t</i></sub><i>/K</i><sub>m</sub> were 0.01265 μmol L<sup>−1</sup> s<sup>−1</sup>, 9310.72 s<sup>−1</sup>, 0.4907 mmol L<sup>−1</sup>, 3.997 mmol L<sup>−1</sup>, and 1.90 × 10<sup>4</sup> L mmol<sup>−1</sup> s<sup>−1</sup>, respectively.</p>\n </section>\n \n <section>\n \n <h3> CONCLUSION</h3>\n \n <p>CALB@ADS-17 showed good esterification performance and exhibited good selectivity towards TAG generation. In addition, CALB@ADS-17 exhibited good reusability in esterification reactions and has potential in practical applications. © 2025 Society of Chemical Industry.</p>\n </section>\n </div>","PeriodicalId":17725,"journal":{"name":"Journal of the Science of Food and Agriculture","volume":"105 7","pages":"3931-3941"},"PeriodicalIF":3.5000,"publicationDate":"2025-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of the Science of Food and Agriculture","FirstCategoryId":"97","ListUrlMain":"https://scijournals.onlinelibrary.wiley.com/doi/10.1002/jsfa.14137","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0

Abstract

BACKGROUND

Immobilized enzyme possessing both high activity and good selectivity is important in practice. In this study, Candida antarctica lipase B (CALB) was immobilized onto the macroporous resin ADS-17 for triacylglycerol (TAG) synthesis through esterification of oleic acid and glycerol. The reaction conditions were optimized by single-factor study and orthogonal test, and the reusability of the immobilized CALB (CALB@ADS-17) was evaluated. In addition, the mechanism of lipase immobilization was studied and the catalytic mechanism of CALB@ADS-17 was investigated.

RESULTS

Oleic acid conversion up to 99.20% and TAG content at 91.58 wt% could be obtained under optimal conditions. In addition, the CALB@ADS-17 retained 84.28% of its initial activity after 11 cycles of reuse. The mechanism of lipase immobilization was through hydrophobic adsorption. The relationship between temperature and oleic acid conversion was lnV0 = 6.3316 − 4.3321/T, and the activation energy (Ea) was 36.02 kJ mol−1. CALB@ADS-17 did not exhibit an obvious interfacial activation phenomenon. Its kinetic behavior can be described by the Michaelis–Menten model, whose kinetic parameters of vmax, kcat, Km, Ki, and kcat/Km were 0.01265 μmol L−1 s−1, 9310.72 s−1, 0.4907 mmol L−1, 3.997 mmol L−1, and 1.90 × 104 L mmol−1 s−1, respectively.

CONCLUSION

CALB@ADS-17 showed good esterification performance and exhibited good selectivity towards TAG generation. In addition, CALB@ADS-17 exhibited good reusability in esterification reactions and has potential in practical applications. © 2025 Society of Chemical Industry.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
ads -17负载的南极念珠菌脂肪酶B通过油酸和甘油酯化选择性合成三酰基甘油。
背景:具有高活性和高选择性的固定化酶在实际应用中具有重要意义。本研究将南极念珠菌脂肪酶B (CALB)固定在大孔树脂ADS-17上,通过油酸和甘油的酯化反应合成三酰基甘油(TAG)。通过单因素试验和正交试验对反应条件进行优化,并对固定化CALB (CALB@ADS-17)的可重复使用性进行评价。此外,还研究了脂肪酶固定化的机理,探讨了CALB@ADS-17的催化机理。结果:在最佳工艺条件下,油酸转化率达99.20%,TAG含量为91.58 wt%。此外,CALB@ADS-17在重复使用11个周期后,保留了其初始活性的84.28%。脂肪酶固定化的机理是疏水吸附。温度与油酸转化率的关系为lnV0 = 6.3316 ~ 4.3321/T,活化能(Ea)为36.02 kJ mol-1。CALB@ADS-17未表现出明显的界面活化现象。其动力学参数vmax、kcat、Km、Ki和kcat/Km分别为0.01265 μmol L-1 s-1、9310.72 s-1、0.4907 mmol L-1、3.997 mmol L-1和1.90 × 104 L mmol-1 s-1,符合Michaelis-Menten模型。结论:CALB@ADS-17具有良好的酯化性能,对TAG的生成具有良好的选择性。此外,CALB@ADS-17在酯化反应中表现出良好的可重复使用性,具有实际应用潜力。©2025化学工业协会。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
CiteScore
8.10
自引率
4.90%
发文量
634
审稿时长
3.1 months
期刊介绍: The Journal of the Science of Food and Agriculture publishes peer-reviewed original research, reviews, mini-reviews, perspectives and spotlights in these areas, with particular emphasis on interdisciplinary studies at the agriculture/ food interface. Published for SCI by John Wiley & Sons Ltd. SCI (Society of Chemical Industry) is a unique international forum where science meets business on independent, impartial ground. Anyone can join and current Members include consumers, business people, environmentalists, industrialists, farmers, and researchers. The Society offers a chance to share information between sectors as diverse as food and agriculture, pharmaceuticals, biotechnology, materials, chemicals, environmental science and safety. As well as organising educational events, SCI awards a number of prestigious honours and scholarships each year, publishes peer-reviewed journals, and provides Members with news from their sectors in the respected magazine, Chemistry & Industry . Originally established in London in 1881 and in New York in 1894, SCI is a registered charity with Members in over 70 countries.
期刊最新文献
Circular economy opportunities in the yerba mate industry: a review. Advanced millet protein processing for designing plant-based whole foods: a review. Probiotics: mechanism of action and gastrointestinal health: gut guardians: unlocking the power of probiotics. From plant to potential therapy: antioxidant and anticancer potential of Medicago lupulina and Trifolium arvense. Identification of the major QTL related to stipe length based on QTL mapping and BSA-Seq in oyster mushroom.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1