Metal-organic framework hybrid materials of ZIF-8/RGO for immobilization of D-amino acid dehydrogenase

IF 9 2区 材料科学 Q1 CHEMISTRY, PHYSICAL Nano Research Pub Date : 2023-07-15 DOI:10.1007/s12274-023-5811-y
Hangbin Lei, Qian Zhang, Xiaoyan Xiang, Liang Jiang, Shiyan Wang, Lingxuan Duan, Shizhen Wang
{"title":"Metal-organic framework hybrid materials of ZIF-8/RGO for immobilization of D-amino acid dehydrogenase","authors":"Hangbin Lei,&nbsp;Qian Zhang,&nbsp;Xiaoyan Xiang,&nbsp;Liang Jiang,&nbsp;Shiyan Wang,&nbsp;Lingxuan Duan,&nbsp;Shizhen Wang","doi":"10.1007/s12274-023-5811-y","DOIUrl":null,"url":null,"abstract":"<div><p>Immobilization of D-amino acid dehydrogenase (DAADH) by the assembly of peptide linker was studied for the biosynthesis of D-phenylalanine. Hybrid material of zeolitic imidazolate framework-8 (ZIF-8) combined with reduced graphene oxide (RGO) was applied for the immobilization of DAADH from <i>Ureibacillus thermosphaericus</i>. The recovery rate of DAADH/ZIF-8/RGO was 165.6%. DAADH/ZIF-8/RGO remained 53.4% of its initial activity at 50 °C for 10 h while the free enzyme was inactivated. DAADH/ZIF-8/RGO maintained 70.5% activity in hyperalkaline solution with pH 12. Kinetic parameters indicated that DAADH/ZIF-8/RGO had greater affinity of phenylpyruvate as <i>V</i><sub>max</sub>/<i>K</i><sub>m</sub> of DAADH/ZIF-8/RGO was 1.27-fold than free enzyme. After seven recycles, the activity of DAADH/ZIF-8/RGO remained 64.3%. Furthermore, one-step separation and <i>in situ</i> immobilization of DAADH by ZIF-8/RGO/Ni was carried out with 1.5-fold activity enhancement. Combining peptide linker and metal-organic framework (MOF) immobilization, thermostability and activity of the immobilized DAADH were significantly improved.\n</p><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":713,"journal":{"name":"Nano Research","volume":"17 :","pages":"290 - 296"},"PeriodicalIF":9.0000,"publicationDate":"2023-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nano Research","FirstCategoryId":"88","ListUrlMain":"https://link.springer.com/article/10.1007/s12274-023-5811-y","RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
引用次数: 0

Abstract

Immobilization of D-amino acid dehydrogenase (DAADH) by the assembly of peptide linker was studied for the biosynthesis of D-phenylalanine. Hybrid material of zeolitic imidazolate framework-8 (ZIF-8) combined with reduced graphene oxide (RGO) was applied for the immobilization of DAADH from Ureibacillus thermosphaericus. The recovery rate of DAADH/ZIF-8/RGO was 165.6%. DAADH/ZIF-8/RGO remained 53.4% of its initial activity at 50 °C for 10 h while the free enzyme was inactivated. DAADH/ZIF-8/RGO maintained 70.5% activity in hyperalkaline solution with pH 12. Kinetic parameters indicated that DAADH/ZIF-8/RGO had greater affinity of phenylpyruvate as Vmax/Km of DAADH/ZIF-8/RGO was 1.27-fold than free enzyme. After seven recycles, the activity of DAADH/ZIF-8/RGO remained 64.3%. Furthermore, one-step separation and in situ immobilization of DAADH by ZIF-8/RGO/Ni was carried out with 1.5-fold activity enhancement. Combining peptide linker and metal-organic framework (MOF) immobilization, thermostability and activity of the immobilized DAADH were significantly improved.

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
ZIF-8/RGO金属-有机骨架杂化材料固定化d -氨基酸脱氢酶
以d -苯丙氨酸为合成原料,研究了肽连接体组装固定d -氨基酸脱氢酶(DAADH)的方法。采用沸石咪唑酸骨架-8 (ZIF-8)与还原氧化石墨烯(RGO)复合的杂化材料,固定化热球脲杆菌DAADH。DAADH/ZIF-8/RGO的回收率为165.6%。当游离酶失活时,DAADH/ZIF-8/RGO在50℃作用10 h仍保持53.4%的初始活性。DAADH/ZIF-8/RGO在pH为12的高碱性溶液中保持70.5%的活性。动力学参数表明,DAADH/ZIF-8/RGO对苯基丙酮酸具有更强的亲和力,其Vmax/Km为游离酶的1.27倍。经过7次循环后,DAADH/ZIF-8/RGO的活性仍为64.3%。ZIF-8/RGO/Ni一步分离原位固定化DAADH,活性提高1.5倍。结合肽连接剂和金属有机骨架(MOF)固定,固定化的DAADH的热稳定性和活性显著提高。
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
Nano Research
Nano Research 化学-材料科学:综合
CiteScore
14.30
自引率
11.10%
发文量
2574
审稿时长
1.7 months
期刊介绍: Nano Research is a peer-reviewed, international and interdisciplinary research journal that focuses on all aspects of nanoscience and nanotechnology. It solicits submissions in various topical areas, from basic aspects of nanoscale materials to practical applications. The journal publishes articles on synthesis, characterization, and manipulation of nanomaterials; nanoscale physics, electrical transport, and quantum physics; scanning probe microscopy and spectroscopy; nanofluidics; nanosensors; nanoelectronics and molecular electronics; nano-optics, nano-optoelectronics, and nano-photonics; nanomagnetics; nanobiotechnology and nanomedicine; and nanoscale modeling and simulations. Nano Research offers readers a combination of authoritative and comprehensive Reviews, original cutting-edge research in Communication and Full Paper formats. The journal also prioritizes rapid review to ensure prompt publication.
期刊最新文献
Immunoengineering strategies using nanoparticles for obesity treatment. Incidental vs. Engineered Nanoparticles in Alzheimer's and Parkinson's Disease: Pathological Pathways and Therapeutic Interventions. Single-dose cathepsin L CRISPR nanotherapy mitigates PASC-like lung damage in hamsters. Advances in nanotechnology-enabled adjuvants for peptide-based cancer vaccines. CdS quantum dot aerogels for photocatalytic hydrogen evolution
×
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