Covalent immobilization of recombinant L-asparaginase from Geobacillus kaustophilus on ReliZyme supports for mitigation of acrylamide

IF 16.4 1区化学 Q1 CHEMISTRY, MULTIDISCIPLINARY

Accounts of Chemical Research Pub Date : 2023-09-15 DOI:10.1080/10242422.2023.2257351

F. İnci Özdemir, Burcu Karaaslan, Ahmet Tülek, Deniz Yildirim

{"title":"Covalent immobilization of recombinant L-asparaginase from <i>Geobacillus kaustophilus</i> on ReliZyme supports for mitigation of acrylamide","authors":"F. İnci Özdemir, Burcu Karaaslan, Ahmet Tülek, Deniz Yildirim","doi":"10.1080/10242422.2023.2257351","DOIUrl":null,"url":null,"abstract":"AbstractIn this study, a new recombinant L-asparaginase from Geobacillus kaustophilus was covalently immobilized on ReliZyme EA403 (Relizyme/EA@GkASNase) and ReliZyme HA403 (Relizyme/HA@GkASNase) supports, and the free and immobilized L-asparaginases were used for their acrylamide mitigation performances in a food model system. The immobilization was confirmed by fourier-transform infrared spectroscopy, scanning electron microscopy, and transmission electron microscopy analysis. The optimum pH was determined as 8.5 for all the free and immobilized L-asparaginase samples. The optimum temperature was determined as 55 °C for the free enzyme and 60 °C for both the immobilized samples. The thermal stability of L-asparaginase was increased by 17.6 and 37.2 folds at 60 °C for Relizyme/EA@GkASNase and Relizyme/HA@GkASNase, respectively. Relizyme/EA@GkASNase and Relizyme/HA@GkASNase showed 16% and 43% of the catalytic efficiency of free GkASNase. The acrylamide mitigation performances of free and immobilized L-asparaginase samples were investigated using the L-asparagine–starch food model system and the formed acrylamide was completely mitigated in 1 h for all the L-asparaginase samples. Both the immobilized L-asparaginase samples retained at least 80% of their activities after five reuses. Hence, the immobilized GkASNase preparations can be potentially used in heat-treated food industries to remove acrylamide.Keywords: Geobacillus kaustophilusL-asparaginaseReliZymeacrylamide mitigation Disclosure statementAll authors declare that they have no conflict of interest.","PeriodicalId":1,"journal":{"name":"Accounts of Chemical Research","volume":null,"pages":null},"PeriodicalIF":16.4000,"publicationDate":"2023-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Accounts of Chemical Research","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/10242422.2023.2257351","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}

引用次数: 0

Abstract

AbstractIn this study, a new recombinant L-asparaginase from Geobacillus kaustophilus was covalently immobilized on ReliZyme EA403 (Relizyme/EA@GkASNase) and ReliZyme HA403 (Relizyme/HA@GkASNase) supports, and the free and immobilized L-asparaginases were used for their acrylamide mitigation performances in a food model system. The immobilization was confirmed by fourier-transform infrared spectroscopy, scanning electron microscopy, and transmission electron microscopy analysis. The optimum pH was determined as 8.5 for all the free and immobilized L-asparaginase samples. The optimum temperature was determined as 55 °C for the free enzyme and 60 °C for both the immobilized samples. The thermal stability of L-asparaginase was increased by 17.6 and 37.2 folds at 60 °C for Relizyme/EA@GkASNase and Relizyme/HA@GkASNase, respectively. Relizyme/EA@GkASNase and Relizyme/HA@GkASNase showed 16% and 43% of the catalytic efficiency of free GkASNase. The acrylamide mitigation performances of free and immobilized L-asparaginase samples were investigated using the L-asparagine–starch food model system and the formed acrylamide was completely mitigated in 1 h for all the L-asparaginase samples. Both the immobilized L-asparaginase samples retained at least 80% of their activities after five reuses. Hence, the immobilized GkASNase preparations can be potentially used in heat-treated food industries to remove acrylamide.Keywords: Geobacillus kaustophilusL-asparaginaseReliZymeacrylamide mitigation Disclosure statementAll authors declare that they have no conflict of interest.

查看原文本刊更多论文

kaustophilus地杆菌重组l -天冬酰胺酶在ReliZyme载体上的共价固定化研究

摘要本研究以kaustophilus Geobacillus重组l -天门酰胺酶为载体，将其共价固定在ReliZyme EA403 (ReliZyme /EA@GkASNase)和ReliZyme HA403 (ReliZyme /HA@GkASNase)载体上，并在食品模型体系中研究了游离和固定的l -天门酰胺酶的丙烯酰胺降解性能。通过傅里叶变换红外光谱、扫描电镜和透射电镜分析证实了固定作用。游离和固定l -天冬酰胺酶样品的最适pH均为8.5。游离酶的最佳温度为55℃，两种固定化样品的最佳温度均为60℃。Relizyme/EA@GkASNase和Relizyme/HA@GkASNase的l -天冬酰胺酶在60℃时的热稳定性分别提高了17.6倍和37.2倍。Relizyme/EA@GkASNase和Relizyme/HA@GkASNase对游离GkASNase的催化效率分别为16%和43%。采用l -天冬酰胺-淀粉食物模型体系考察了游离和固定化l -天冬酰胺酶样品的丙烯酰胺降解性能，结果表明，所有l -天冬酰胺酶样品在1 h内形成的丙烯酰胺均被完全降解。两种固定的l -天冬酰胺酶样品在重复使用五次后仍保持至少80%的活性。因此，固定化GkASNase制剂可以潜在地用于热处理食品工业中去除丙烯酰胺。关键词:考氏地obacillus kaustophilusl -天冬酰胺酶elizyymeacrylamide mitigation披露声明所有作者声明无利益冲突。

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

Accounts of Chemical Research 化学-化学综合

CiteScore

31.40

自引率

1.10%

发文量

312

审稿时长

2 months

期刊介绍： Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance. Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.