Invertase Immobilization on Magnetite Nanoparticles for Efficient Fructooligosaccharide Generation: A Comprehensive Kinetic Analysis and Reactor Design Strategy

IF 2.8 Q2 ENGINEERING, CHEMICAL
David Polanía Melo, Andrés Hernández Bravo, Juan C. Cruz, L. H. Reyes
{"title":"Invertase Immobilization on Magnetite Nanoparticles for Efficient Fructooligosaccharide Generation: A Comprehensive Kinetic Analysis and Reactor Design Strategy","authors":"David Polanía Melo, Andrés Hernández Bravo, Juan C. Cruz, L. H. Reyes","doi":"10.3390/chemengineering7030055","DOIUrl":null,"url":null,"abstract":"This study investigated the effectiveness of immobilizing Saccharomyces cerevisiae invertase (SInv) on magnetite nanoparticles to produce fructooligosaccharides (FOSs). Based on the existing literature and accompanied by parameter estimation, a modified kinetic model was employed to represent the kinetics of sucrose hydrolysis and transfructosylation using SInv immobilized on magnetite nanoparticle surfaces. This model was utilized to simulate the performance of batch reactors for both free and immobilized enzymes. The maximum FOS concentration for the free enzyme was determined to be 123.1 mM, while the immobilized case achieved a slightly higher concentration of 125.4 mM. Furthermore, a continuous stirred-tank reactor (CSTR) model was developed for the immobilized enzyme, resulting in a maximum FOS concentration of 73.96 mM at the reactor’s outlet and a dilution rate of 14.2 h−1. To examine the impact of glucose inhibition on FOS production, a glucose oxidase reaction mechanism was integrated into the fitted immobilized theoretical model. In a batch reactor, the reduction or elimination of glucose in the reactive media led to a 2.1% increase in FOS production. Immobilizing the biocatalyst enhanced the overall performance of SInv. This enzyme immobilization approach also holds the potential for coupling glucose oxidase onto functionalized nanoparticles to minimize glucose inhibition, thereby improving FOS synthesis and facilitating optimal enzyme recovery and reuse.","PeriodicalId":9755,"journal":{"name":"ChemEngineering","volume":" ","pages":""},"PeriodicalIF":2.8000,"publicationDate":"2023-06-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"ChemEngineering","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3390/chemengineering7030055","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"ENGINEERING, CHEMICAL","Score":null,"Total":0}
引用次数: 0

Abstract

This study investigated the effectiveness of immobilizing Saccharomyces cerevisiae invertase (SInv) on magnetite nanoparticles to produce fructooligosaccharides (FOSs). Based on the existing literature and accompanied by parameter estimation, a modified kinetic model was employed to represent the kinetics of sucrose hydrolysis and transfructosylation using SInv immobilized on magnetite nanoparticle surfaces. This model was utilized to simulate the performance of batch reactors for both free and immobilized enzymes. The maximum FOS concentration for the free enzyme was determined to be 123.1 mM, while the immobilized case achieved a slightly higher concentration of 125.4 mM. Furthermore, a continuous stirred-tank reactor (CSTR) model was developed for the immobilized enzyme, resulting in a maximum FOS concentration of 73.96 mM at the reactor’s outlet and a dilution rate of 14.2 h−1. To examine the impact of glucose inhibition on FOS production, a glucose oxidase reaction mechanism was integrated into the fitted immobilized theoretical model. In a batch reactor, the reduction or elimination of glucose in the reactive media led to a 2.1% increase in FOS production. Immobilizing the biocatalyst enhanced the overall performance of SInv. This enzyme immobilization approach also holds the potential for coupling glucose oxidase onto functionalized nanoparticles to minimize glucose inhibition, thereby improving FOS synthesis and facilitating optimal enzyme recovery and reuse.
磁性纳米粒子固定化转化酶高效生产低聚果糖的综合动力学分析和反应器设计策略
本研究考察了将酿酒酵母转化酶(SInv)固定在磁铁矿纳米颗粒上生产低聚果糖(FOSs)的有效性。在现有文献的基础上,结合参数估计,采用改进的动力学模型来表示使用固定在磁铁矿纳米颗粒表面的SInv进行蔗糖水解和转结构糖基化的动力学。该模型用于模拟间歇反应器对游离酶和固定化酶的性能。游离酶的最大FOS浓度确定为123.1 mM,而固定化酶的浓度略高,为125.4 mM。此外,为固定化酶开发了连续搅拌槽反应器(CSTR)模型,导致反应器出口的最大FOS浓度为73.96 mM,稀释率为14.2 h−1。为了检验葡萄糖抑制对FOS产生的影响,将葡萄糖氧化酶反应机制整合到拟合的固定化理论模型中。在间歇式反应器中,反应介质中葡萄糖的减少或消除导致FOS产量增加2.1%。固定化生物催化剂提高了SInv的整体性能。这种酶固定化方法还具有将葡萄糖氧化酶偶联到功能化纳米颗粒上的潜力,以最大限度地减少葡萄糖抑制,从而改善FOS的合成并促进最佳的酶回收和再利用。
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 求助全文
来源期刊
ChemEngineering
ChemEngineering Engineering-Engineering (all)
CiteScore
4.00
自引率
4.00%
发文量
88
审稿时长
11 weeks
×
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
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
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 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信