Covalent Immobilization of L-Asparaginase and Optimization of Its Enzyme Reactor for Reducing Acrylamide Formation in a Heated Food Model System

Acrylamide is a potent carcinogen and neurotoxin that is mainly formed by the Maillard reaction of asparagine with starch at high temperatures. In this work, a food safety immobilization system for L-asparaginase (L-ASNase) consisting of food-grade agarose (Aga) spheres and N-hydroxysuccinimide este...

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Main Authors:	Ran Li, Zehua Zhang, Xiaomei Pei, Xiaole Xia
Format:	Article
Language:	English
Published:	Frontiers Media S.A. 2020-10-01
Series:	Frontiers in Bioengineering and Biotechnology
Subjects:	acrylamide asparaginase immobilization packed bed reactor kinetic model
Online Access:	https://www.frontiersin.org/article/10.3389/fbioe.2020.584758/full

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spelling	doaj-f02aacbcdb8f40e6b48ed193ebe4e5c32020-11-25T03:54:16ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852020-10-01810.3389/fbioe.2020.584758584758Covalent Immobilization of L-Asparaginase and Optimization of Its Enzyme Reactor for Reducing Acrylamide Formation in a Heated Food Model SystemRan LiZehua ZhangXiaomei PeiXiaole XiaAcrylamide is a potent carcinogen and neurotoxin that is mainly formed by the Maillard reaction of asparagine with starch at high temperatures. In this work, a food safety immobilization system for L-asparaginase (L-ASNase) consisting of food-grade agarose (Aga) spheres and N-hydroxysuccinimide esters was developed to decrease the formation of acrylamide in a fluid food model system. L-asparaginase was successfully immobilized with a maximum immobilization efficiency of 68.43%. The immobilized enzymes exhibited superior storage stability and reusability with 93.21 and 72.25% of the initial activity retained after six consecutive cycles and storage for 28 days, indicating its high industrial application potential. Meanwhile, a simplified mathematical model of the enzyme reactor was developed and verified with experiments, which demonstrated its auxiliary role in the design and optimization of reactors. In addition, simulated fluidized food components were continuously catalyzed in the designed packed bed reactor, achieving a reduction rate of nearly 89%.https://www.frontiersin.org/article/10.3389/fbioe.2020.584758/fullacrylamideasparaginaseimmobilizationpacked bed reactorkinetic model
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Ran Li Zehua Zhang Xiaomei Pei Xiaole Xia
spellingShingle	Ran Li Zehua Zhang Xiaomei Pei Xiaole Xia Covalent Immobilization of L-Asparaginase and Optimization of Its Enzyme Reactor for Reducing Acrylamide Formation in a Heated Food Model System Frontiers in Bioengineering and Biotechnology acrylamide asparaginase immobilization packed bed reactor kinetic model
author_facet	Ran Li Zehua Zhang Xiaomei Pei Xiaole Xia
author_sort	Ran Li
title	Covalent Immobilization of L-Asparaginase and Optimization of Its Enzyme Reactor for Reducing Acrylamide Formation in a Heated Food Model System
title_short	Covalent Immobilization of L-Asparaginase and Optimization of Its Enzyme Reactor for Reducing Acrylamide Formation in a Heated Food Model System
title_full	Covalent Immobilization of L-Asparaginase and Optimization of Its Enzyme Reactor for Reducing Acrylamide Formation in a Heated Food Model System
title_fullStr	Covalent Immobilization of L-Asparaginase and Optimization of Its Enzyme Reactor for Reducing Acrylamide Formation in a Heated Food Model System
title_full_unstemmed	Covalent Immobilization of L-Asparaginase and Optimization of Its Enzyme Reactor for Reducing Acrylamide Formation in a Heated Food Model System
title_sort	covalent immobilization of l-asparaginase and optimization of its enzyme reactor for reducing acrylamide formation in a heated food model system
publisher	Frontiers Media S.A.
series	Frontiers in Bioengineering and Biotechnology
issn	2296-4185
publishDate	2020-10-01
description	Acrylamide is a potent carcinogen and neurotoxin that is mainly formed by the Maillard reaction of asparagine with starch at high temperatures. In this work, a food safety immobilization system for L-asparaginase (L-ASNase) consisting of food-grade agarose (Aga) spheres and N-hydroxysuccinimide esters was developed to decrease the formation of acrylamide in a fluid food model system. L-asparaginase was successfully immobilized with a maximum immobilization efficiency of 68.43%. The immobilized enzymes exhibited superior storage stability and reusability with 93.21 and 72.25% of the initial activity retained after six consecutive cycles and storage for 28 days, indicating its high industrial application potential. Meanwhile, a simplified mathematical model of the enzyme reactor was developed and verified with experiments, which demonstrated its auxiliary role in the design and optimization of reactors. In addition, simulated fluidized food components were continuously catalyzed in the designed packed bed reactor, achieving a reduction rate of nearly 89%.
topic	acrylamide asparaginase immobilization packed bed reactor kinetic model
url	https://www.frontiersin.org/article/10.3389/fbioe.2020.584758/full
work_keys_str_mv	AT ranli covalentimmobilizationoflasparaginaseandoptimizationofitsenzymereactorforreducingacrylamideformationinaheatedfoodmodelsystem AT zehuazhang covalentimmobilizationoflasparaginaseandoptimizationofitsenzymereactorforreducingacrylamideformationinaheatedfoodmodelsystem AT xiaomeipei covalentimmobilizationoflasparaginaseandoptimizationofitsenzymereactorforreducingacrylamideformationinaheatedfoodmodelsystem AT xiaolexia covalentimmobilizationoflasparaginaseandoptimizationofitsenzymereactorforreducingacrylamideformationinaheatedfoodmodelsystem
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Covalent Immobilization of L-Asparaginase and Optimization of Its Enzyme Reactor for Reducing Acrylamide Formation in a Heated Food Model System

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