Enzyme Catalyst Engineering toward the Integration of Biocatalysis and Chemocatalysis

Enzymatic catalysis, which has been driving biological processes in a green, mild, and efficient manner for billions of years, is increasingly being used in industrial processes to manufacture chemicals, pharmaceuticals, and materials for human society. Since enzymes were discovered, strategies to a...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Trends in biotechnology (Regular ed.) 2021-11, Vol.39 (11), p.1173-1183
Hauptverfasser: Cao, Yufei, Li, Xiaoyang, Ge, Jun
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 1183
container_issue 11
container_start_page 1173
container_title Trends in biotechnology (Regular ed.)
container_volume 39
creator Cao, Yufei
Li, Xiaoyang
Ge, Jun
description Enzymatic catalysis, which has been driving biological processes in a green, mild, and efficient manner for billions of years, is increasingly being used in industrial processes to manufacture chemicals, pharmaceuticals, and materials for human society. Since enzymes were discovered, strategies to adapt enzymes for use as catalysts for industrial processes, such as chemical modification, immobilization, site-directed mutagenesis, directed evolution of enzymes, artificial metalloenzymes, and computational design, have been continuously pursued. In contrast to these strategies, editing enzymes to easily integrate biocatalysis with chemocatalysis is a potential way to apply enzymes in industry. Enzyme catalyst editing focuses on fine-tuning the microenvironment surrounding the enzyme or achieving a new catalytic function to construct better biocatalysis under non-natural conditions for the enzyme. Nature, the best chemist of all time, utilizes powerful macromolecular protein catalysts: enzymes. By using enzymes, nature can extract chemicals and energy from the environment and convert them into the complex molecules necessary for life.Applying enzymes in industry can considerably improve the efficiency of organic synthesis, especially the synthesis of chiral compounds.Critical improvements are to expand enzyme catalysis and improve the performance of enzymes in non-native environments.Enzyme catalyst editing is proposed to design the microenvironment surrounding enzyme molecules to elegantly integrate biocatalysis and chemocatalysis for a variety of applications.
doi_str_mv 10.1016/j.tibtech.2021.01.002
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_2581759642</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0167779921000081</els_id><sourcerecordid>2581759642</sourcerecordid><originalsourceid>FETCH-LOGICAL-c440t-e53fa0cdc4ac2db2463a03b499cf445c504bb4bf5abfaffdbd648b2f100298333</originalsourceid><addsrcrecordid>eNqFkFtLAzEQhYMoWi8_QQn4vDXZJLvNk2ipFyj4os8hl0mbYrOapEr99W5p1UfhwMDwnTnMQeickiEltLlaDEswBex8WJOaDkkvUu-hAR21smJENvto0HNt1bZSHqHjnBeEENZKeoiOGBOC0rYZoJdJ_FovAY910a_rXPAkzkIESCHOcOk-dXK4zAE_xgKzpEvoIu48vg2d3TpCxjo6PJ7D8m91ig68fs1wtpsn6OVu8jx-qKZP94_jm2llOSelAsG8JtZZrm3tTM0bpgkzXErrORdWEG4MN15o47X3zriGj0ztaf-qHDHGTtDl9u5b6t5XkItadKsU-0hVixFthWx43VNiS9nU5ZzAq7cUljqtFSVqU6ZaqF2ZalOmIr3Ixnexu74yS3C_rp_2euB6C0D_40eApLINEC24kMAW5brwT8Q3uUuJng</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2581759642</pqid></control><display><type>article</type><title>Enzyme Catalyst Engineering toward the Integration of Biocatalysis and Chemocatalysis</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><source>ProQuest Central UK/Ireland</source><creator>Cao, Yufei ; Li, Xiaoyang ; Ge, Jun</creator><creatorcontrib>Cao, Yufei ; Li, Xiaoyang ; Ge, Jun</creatorcontrib><description>Enzymatic catalysis, which has been driving biological processes in a green, mild, and efficient manner for billions of years, is increasingly being used in industrial processes to manufacture chemicals, pharmaceuticals, and materials for human society. Since enzymes were discovered, strategies to adapt enzymes for use as catalysts for industrial processes, such as chemical modification, immobilization, site-directed mutagenesis, directed evolution of enzymes, artificial metalloenzymes, and computational design, have been continuously pursued. In contrast to these strategies, editing enzymes to easily integrate biocatalysis with chemocatalysis is a potential way to apply enzymes in industry. Enzyme catalyst editing focuses on fine-tuning the microenvironment surrounding the enzyme or achieving a new catalytic function to construct better biocatalysis under non-natural conditions for the enzyme. Nature, the best chemist of all time, utilizes powerful macromolecular protein catalysts: enzymes. By using enzymes, nature can extract chemicals and energy from the environment and convert them into the complex molecules necessary for life.Applying enzymes in industry can considerably improve the efficiency of organic synthesis, especially the synthesis of chiral compounds.Critical improvements are to expand enzyme catalysis and improve the performance of enzymes in non-native environments.Enzyme catalyst editing is proposed to design the microenvironment surrounding enzyme molecules to elegantly integrate biocatalysis and chemocatalysis for a variety of applications.</description><identifier>ISSN: 0167-7799</identifier><identifier>EISSN: 1879-3096</identifier><identifier>DOI: 10.1016/j.tibtech.2021.01.002</identifier><identifier>PMID: 33551176</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Biocatalysis ; Biocatalysts ; Biological activity ; Carbon ; Catalysis ; Catalysts ; Chemical modification ; Chemical reactions ; chemocatalysis ; Computer applications ; Design ; Directed evolution ; Editing ; Engineering ; Enzymes ; Enzymes - genetics ; Enzymes - metabolism ; Humans ; Immobilization ; Industry ; microenvironment ; Microenvironments ; Mutagenesis ; Mutation ; Protein Engineering ; Proteins ; Site-directed mutagenesis ; Solvents</subject><ispartof>Trends in biotechnology (Regular ed.), 2021-11, Vol.39 (11), p.1173-1183</ispartof><rights>2021 Elsevier Ltd</rights><rights>Copyright © 2021 Elsevier Ltd. All rights reserved.</rights><rights>2021. Elsevier Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-e53fa0cdc4ac2db2463a03b499cf445c504bb4bf5abfaffdbd648b2f100298333</citedby><cites>FETCH-LOGICAL-c440t-e53fa0cdc4ac2db2463a03b499cf445c504bb4bf5abfaffdbd648b2f100298333</cites><orcidid>0000-0001-5503-8899</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.proquest.com/docview/2581759642?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995,64385,64389,72469</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33551176$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cao, Yufei</creatorcontrib><creatorcontrib>Li, Xiaoyang</creatorcontrib><creatorcontrib>Ge, Jun</creatorcontrib><title>Enzyme Catalyst Engineering toward the Integration of Biocatalysis and Chemocatalysis</title><title>Trends in biotechnology (Regular ed.)</title><addtitle>Trends Biotechnol</addtitle><description>Enzymatic catalysis, which has been driving biological processes in a green, mild, and efficient manner for billions of years, is increasingly being used in industrial processes to manufacture chemicals, pharmaceuticals, and materials for human society. Since enzymes were discovered, strategies to adapt enzymes for use as catalysts for industrial processes, such as chemical modification, immobilization, site-directed mutagenesis, directed evolution of enzymes, artificial metalloenzymes, and computational design, have been continuously pursued. In contrast to these strategies, editing enzymes to easily integrate biocatalysis with chemocatalysis is a potential way to apply enzymes in industry. Enzyme catalyst editing focuses on fine-tuning the microenvironment surrounding the enzyme or achieving a new catalytic function to construct better biocatalysis under non-natural conditions for the enzyme. Nature, the best chemist of all time, utilizes powerful macromolecular protein catalysts: enzymes. By using enzymes, nature can extract chemicals and energy from the environment and convert them into the complex molecules necessary for life.Applying enzymes in industry can considerably improve the efficiency of organic synthesis, especially the synthesis of chiral compounds.Critical improvements are to expand enzyme catalysis and improve the performance of enzymes in non-native environments.Enzyme catalyst editing is proposed to design the microenvironment surrounding enzyme molecules to elegantly integrate biocatalysis and chemocatalysis for a variety of applications.</description><subject>Biocatalysis</subject><subject>Biocatalysts</subject><subject>Biological activity</subject><subject>Carbon</subject><subject>Catalysis</subject><subject>Catalysts</subject><subject>Chemical modification</subject><subject>Chemical reactions</subject><subject>chemocatalysis</subject><subject>Computer applications</subject><subject>Design</subject><subject>Directed evolution</subject><subject>Editing</subject><subject>Engineering</subject><subject>Enzymes</subject><subject>Enzymes - genetics</subject><subject>Enzymes - metabolism</subject><subject>Humans</subject><subject>Immobilization</subject><subject>Industry</subject><subject>microenvironment</subject><subject>Microenvironments</subject><subject>Mutagenesis</subject><subject>Mutation</subject><subject>Protein Engineering</subject><subject>Proteins</subject><subject>Site-directed mutagenesis</subject><subject>Solvents</subject><issn>0167-7799</issn><issn>1879-3096</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkFtLAzEQhYMoWi8_QQn4vDXZJLvNk2ipFyj4os8hl0mbYrOapEr99W5p1UfhwMDwnTnMQeickiEltLlaDEswBex8WJOaDkkvUu-hAR21smJENvto0HNt1bZSHqHjnBeEENZKeoiOGBOC0rYZoJdJ_FovAY910a_rXPAkzkIESCHOcOk-dXK4zAE_xgKzpEvoIu48vg2d3TpCxjo6PJ7D8m91ig68fs1wtpsn6OVu8jx-qKZP94_jm2llOSelAsG8JtZZrm3tTM0bpgkzXErrORdWEG4MN15o47X3zriGj0ztaf-qHDHGTtDl9u5b6t5XkItadKsU-0hVixFthWx43VNiS9nU5ZzAq7cUljqtFSVqU6ZaqF2ZalOmIr3Ixnexu74yS3C_rp_2euB6C0D_40eApLINEC24kMAW5brwT8Q3uUuJng</recordid><startdate>202111</startdate><enddate>202111</enddate><creator>Cao, Yufei</creator><creator>Li, Xiaoyang</creator><creator>Ge, Jun</creator><general>Elsevier Ltd</general><general>Elsevier Limited</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QF</scope><scope>7QO</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88C</scope><scope>88E</scope><scope>8AO</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H8D</scope><scope>H8G</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0S</scope><scope>M0T</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><orcidid>https://orcid.org/0000-0001-5503-8899</orcidid></search><sort><creationdate>202111</creationdate><title>Enzyme Catalyst Engineering toward the Integration of Biocatalysis and Chemocatalysis</title><author>Cao, Yufei ; Li, Xiaoyang ; Ge, Jun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-e53fa0cdc4ac2db2463a03b499cf445c504bb4bf5abfaffdbd648b2f100298333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Biocatalysis</topic><topic>Biocatalysts</topic><topic>Biological activity</topic><topic>Carbon</topic><topic>Catalysis</topic><topic>Catalysts</topic><topic>Chemical modification</topic><topic>Chemical reactions</topic><topic>chemocatalysis</topic><topic>Computer applications</topic><topic>Design</topic><topic>Directed evolution</topic><topic>Editing</topic><topic>Engineering</topic><topic>Enzymes</topic><topic>Enzymes - genetics</topic><topic>Enzymes - metabolism</topic><topic>Humans</topic><topic>Immobilization</topic><topic>Industry</topic><topic>microenvironment</topic><topic>Microenvironments</topic><topic>Mutagenesis</topic><topic>Mutation</topic><topic>Protein Engineering</topic><topic>Proteins</topic><topic>Site-directed mutagenesis</topic><topic>Solvents</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cao, Yufei</creatorcontrib><creatorcontrib>Li, Xiaoyang</creatorcontrib><creatorcontrib>Ge, Jun</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics &amp; Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Business File</collection><collection>Mechanical &amp; Transportation Engineering Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Healthcare Administration Database (Alumni)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>Materials Science &amp; Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies &amp; Aerospace Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ANTE: Abstracts in New Technology &amp; Engineering</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Civil Engineering Abstracts</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Computer and Information Systems Abstracts – Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Healthcare Administration Database</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies &amp; Aerospace Database</collection><collection>ProQuest Advanced Technologies &amp; Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>ProQuest Central Basic</collection><jtitle>Trends in biotechnology (Regular ed.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cao, Yufei</au><au>Li, Xiaoyang</au><au>Ge, Jun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzyme Catalyst Engineering toward the Integration of Biocatalysis and Chemocatalysis</atitle><jtitle>Trends in biotechnology (Regular ed.)</jtitle><addtitle>Trends Biotechnol</addtitle><date>2021-11</date><risdate>2021</risdate><volume>39</volume><issue>11</issue><spage>1173</spage><epage>1183</epage><pages>1173-1183</pages><issn>0167-7799</issn><eissn>1879-3096</eissn><abstract>Enzymatic catalysis, which has been driving biological processes in a green, mild, and efficient manner for billions of years, is increasingly being used in industrial processes to manufacture chemicals, pharmaceuticals, and materials for human society. Since enzymes were discovered, strategies to adapt enzymes for use as catalysts for industrial processes, such as chemical modification, immobilization, site-directed mutagenesis, directed evolution of enzymes, artificial metalloenzymes, and computational design, have been continuously pursued. In contrast to these strategies, editing enzymes to easily integrate biocatalysis with chemocatalysis is a potential way to apply enzymes in industry. Enzyme catalyst editing focuses on fine-tuning the microenvironment surrounding the enzyme or achieving a new catalytic function to construct better biocatalysis under non-natural conditions for the enzyme. Nature, the best chemist of all time, utilizes powerful macromolecular protein catalysts: enzymes. By using enzymes, nature can extract chemicals and energy from the environment and convert them into the complex molecules necessary for life.Applying enzymes in industry can considerably improve the efficiency of organic synthesis, especially the synthesis of chiral compounds.Critical improvements are to expand enzyme catalysis and improve the performance of enzymes in non-native environments.Enzyme catalyst editing is proposed to design the microenvironment surrounding enzyme molecules to elegantly integrate biocatalysis and chemocatalysis for a variety of applications.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>33551176</pmid><doi>10.1016/j.tibtech.2021.01.002</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0001-5503-8899</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0167-7799
ispartof Trends in biotechnology (Regular ed.), 2021-11, Vol.39 (11), p.1173-1183
issn 0167-7799
1879-3096
language eng
recordid cdi_proquest_journals_2581759642
source MEDLINE; Access via ScienceDirect (Elsevier); ProQuest Central UK/Ireland
subjects Biocatalysis
Biocatalysts
Biological activity
Carbon
Catalysis
Catalysts
Chemical modification
Chemical reactions
chemocatalysis
Computer applications
Design
Directed evolution
Editing
Engineering
Enzymes
Enzymes - genetics
Enzymes - metabolism
Humans
Immobilization
Industry
microenvironment
Microenvironments
Mutagenesis
Mutation
Protein Engineering
Proteins
Site-directed mutagenesis
Solvents
title Enzyme Catalyst Engineering toward the Integration of Biocatalysis and Chemocatalysis
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T20%3A30%3A44IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Enzyme%20Catalyst%20Engineering%20toward%20the%20Integration%20of%20Biocatalysis%20and%20Chemocatalysis&rft.jtitle=Trends%20in%20biotechnology%20(Regular%20ed.)&rft.au=Cao,%20Yufei&rft.date=2021-11&rft.volume=39&rft.issue=11&rft.spage=1173&rft.epage=1183&rft.pages=1173-1183&rft.issn=0167-7799&rft.eissn=1879-3096&rft_id=info:doi/10.1016/j.tibtech.2021.01.002&rft_dat=%3Cproquest_cross%3E2581759642%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2581759642&rft_id=info:pmid/33551176&rft_els_id=S0167779921000081&rfr_iscdi=true