Some like it hot, some like it cold: Temperature dependent biotechnological applications and improvements in extremophilic enzymes
The full biotechnological exploitation of enzymes is still hampered by their low activity, low stability and high cost. Temperature-dependent catalytic properties of enzymes are a key to efficient and cost-effective translation to commercial applications. Organisms adapted to temperature extremes ar...
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Veröffentlicht in: | Biotechnology advances 2015-12, Vol.33 (8), p.1912-1922 |
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creator | Siddiqui, Khawar Sohail |
description | The full biotechnological exploitation of enzymes is still hampered by their low activity, low stability and high cost. Temperature-dependent catalytic properties of enzymes are a key to efficient and cost-effective translation to commercial applications. Organisms adapted to temperature extremes are a rich source of enzymes with broad ranging thermal properties which, if isolated, characterized and their structure–function–stability relationship elucidated, could underpin a variety of technologies. Enzymes from thermally-adapted organisms such as psychrophiles (low-temperature) and thermophiles (high-temperature) are a vast natural resource that is already under scrutiny for their biotechnological potential. However, psychrophilic and thermophilic enzymes show an activity–stability trade-off that necessitates the use of various genetic and chemical modifications to further improve their properties to suit various industrial applications. This review describes in detail the properties and biotechnological applications of both cold-adapted and thermophilic enzymes. Furthermore, the review critically examines ways to improve their value for biotechnology, concluding by proposing an integrated approach involving thermally-adapted, genetically and magnetically modified enzymes to make biocatalysis more efficient and cost-effective.
•Enzyme applications are hindered by low activity, low stability and high cost.•Thermally-adapted organisms are a good source of efficient enzymes.•Psychrophilic and thermophilic enzymes show activity–stability tradeoff.•Activity–stability tradeoff can be avoided by genetic and chemical modifications.•Immobilization on magnetic nanoparticles allow enzyme recycling reducing cost. |
doi_str_mv | 10.1016/j.biotechadv.2015.11.001 |
format | Article |
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•Enzyme applications are hindered by low activity, low stability and high cost.•Thermally-adapted organisms are a good source of efficient enzymes.•Psychrophilic and thermophilic enzymes show activity–stability tradeoff.•Activity–stability tradeoff can be avoided by genetic and chemical modifications.•Immobilization on magnetic nanoparticles allow enzyme recycling reducing cost.</description><identifier>ISSN: 0734-9750</identifier><identifier>EISSN: 1873-1899</identifier><identifier>DOI: 10.1016/j.biotechadv.2015.11.001</identifier><identifier>PMID: 26585268</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Bacteria - enzymology ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Biotechnology ; Catalysis ; Cold Temperature ; Cold-adapted ; Computational, genetic and chemical modification ; Enzymes ; Enzymes - chemistry ; Enzymes - genetics ; Genetic Engineering ; Genetics ; Hot Temperature ; Magnetic nanoparticles ; Natural resources ; Organisms ; Protein structure, function, stability ; Psychrophiles ; Psychrophilic ; Thermophilic ; Tradeoffs ; Translations</subject><ispartof>Biotechnology advances, 2015-12, Vol.33 (8), p.1912-1922</ispartof><rights>2015 Elsevier Inc.</rights><rights>Copyright © 2015 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-eea8cba49e6710eab94c975f0cd1b7840295c3448fd2a391a78d0bd171296b5a3</citedby><cites>FETCH-LOGICAL-c440t-eea8cba49e6710eab94c975f0cd1b7840295c3448fd2a391a78d0bd171296b5a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.biotechadv.2015.11.001$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26585268$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Siddiqui, Khawar Sohail</creatorcontrib><title>Some like it hot, some like it cold: Temperature dependent biotechnological applications and improvements in extremophilic enzymes</title><title>Biotechnology advances</title><addtitle>Biotechnol Adv</addtitle><description>The full biotechnological exploitation of enzymes is still hampered by their low activity, low stability and high cost. Temperature-dependent catalytic properties of enzymes are a key to efficient and cost-effective translation to commercial applications. Organisms adapted to temperature extremes are a rich source of enzymes with broad ranging thermal properties which, if isolated, characterized and their structure–function–stability relationship elucidated, could underpin a variety of technologies. Enzymes from thermally-adapted organisms such as psychrophiles (low-temperature) and thermophiles (high-temperature) are a vast natural resource that is already under scrutiny for their biotechnological potential. However, psychrophilic and thermophilic enzymes show an activity–stability trade-off that necessitates the use of various genetic and chemical modifications to further improve their properties to suit various industrial applications. This review describes in detail the properties and biotechnological applications of both cold-adapted and thermophilic enzymes. Furthermore, the review critically examines ways to improve their value for biotechnology, concluding by proposing an integrated approach involving thermally-adapted, genetically and magnetically modified enzymes to make biocatalysis more efficient and cost-effective.
•Enzyme applications are hindered by low activity, low stability and high cost.•Thermally-adapted organisms are a good source of efficient enzymes.•Psychrophilic and thermophilic enzymes show activity–stability tradeoff.•Activity–stability tradeoff can be avoided by genetic and chemical modifications.•Immobilization on magnetic nanoparticles allow enzyme recycling reducing cost.</description><subject>Bacteria - enzymology</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Biotechnology</subject><subject>Catalysis</subject><subject>Cold Temperature</subject><subject>Cold-adapted</subject><subject>Computational, genetic and chemical modification</subject><subject>Enzymes</subject><subject>Enzymes - chemistry</subject><subject>Enzymes - genetics</subject><subject>Genetic Engineering</subject><subject>Genetics</subject><subject>Hot Temperature</subject><subject>Magnetic nanoparticles</subject><subject>Natural resources</subject><subject>Organisms</subject><subject>Protein structure, function, stability</subject><subject>Psychrophiles</subject><subject>Psychrophilic</subject><subject>Thermophilic</subject><subject>Tradeoffs</subject><subject>Translations</subject><issn>0734-9750</issn><issn>1873-1899</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQQC0EotvCX0A-ciDBk9iJzQ0qKEiVOLQ9W449y3pJ4mB7V5RjfzmudqHc6Mkj683nI4QCq4FB93ZbDz5ktBvj9nXDQNQANWPwhKxA9m0FUqmnZMX6lleqF-yEnKa0LYBgon1OTppOSNF0ckXursKEdPTfkfpMNyG_oenfHxtG945e47RgNHkXkTpccHY4Z3qcYQ5j-OatGalZlrEE2Yc5UTM76qclhj1OhU7UzxR_5ohTWDa-cBTnX7cTphfk2dqMCV8e3zNy8-nj9fnn6vLrxZfz95eV5ZzlCtFIOxiusOuBoRkUt2W3NbMOhl5y1ihhW87l2jWmVWB66djgoIdGdYMw7Rl5fahbZvqxw5T15JPFcTQzhl3S0MsOlJRCPAYVTaOkko9AueqAc8UKKg-ojSGliGu9RD-ZeKuB6XuveqsfvOp7rxpAF20l9dWxy26Y0P1N_COyAB8OAJYL7j1GnazH2aLzEW3WLvj_d_kNzj67TA</recordid><startdate>20151201</startdate><enddate>20151201</enddate><creator>Siddiqui, Khawar Sohail</creator><general>Elsevier Inc</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>7X8</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7U5</scope><scope>L7M</scope></search><sort><creationdate>20151201</creationdate><title>Some like it hot, some like it cold: Temperature dependent biotechnological applications and improvements in extremophilic enzymes</title><author>Siddiqui, Khawar Sohail</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-eea8cba49e6710eab94c975f0cd1b7840295c3448fd2a391a78d0bd171296b5a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Bacteria - enzymology</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Biotechnology</topic><topic>Catalysis</topic><topic>Cold Temperature</topic><topic>Cold-adapted</topic><topic>Computational, genetic and chemical modification</topic><topic>Enzymes</topic><topic>Enzymes - chemistry</topic><topic>Enzymes - genetics</topic><topic>Genetic Engineering</topic><topic>Genetics</topic><topic>Hot Temperature</topic><topic>Magnetic nanoparticles</topic><topic>Natural resources</topic><topic>Organisms</topic><topic>Protein structure, function, stability</topic><topic>Psychrophiles</topic><topic>Psychrophilic</topic><topic>Thermophilic</topic><topic>Tradeoffs</topic><topic>Translations</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Siddiqui, Khawar Sohail</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - 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Temperature-dependent catalytic properties of enzymes are a key to efficient and cost-effective translation to commercial applications. Organisms adapted to temperature extremes are a rich source of enzymes with broad ranging thermal properties which, if isolated, characterized and their structure–function–stability relationship elucidated, could underpin a variety of technologies. Enzymes from thermally-adapted organisms such as psychrophiles (low-temperature) and thermophiles (high-temperature) are a vast natural resource that is already under scrutiny for their biotechnological potential. However, psychrophilic and thermophilic enzymes show an activity–stability trade-off that necessitates the use of various genetic and chemical modifications to further improve their properties to suit various industrial applications. This review describes in detail the properties and biotechnological applications of both cold-adapted and thermophilic enzymes. Furthermore, the review critically examines ways to improve their value for biotechnology, concluding by proposing an integrated approach involving thermally-adapted, genetically and magnetically modified enzymes to make biocatalysis more efficient and cost-effective.
•Enzyme applications are hindered by low activity, low stability and high cost.•Thermally-adapted organisms are a good source of efficient enzymes.•Psychrophilic and thermophilic enzymes show activity–stability tradeoff.•Activity–stability tradeoff can be avoided by genetic and chemical modifications.•Immobilization on magnetic nanoparticles allow enzyme recycling reducing cost.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>26585268</pmid><doi>10.1016/j.biotechadv.2015.11.001</doi><tpages>11</tpages></addata></record> |
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subjects | Bacteria - enzymology Bacterial Proteins - chemistry Bacterial Proteins - genetics Biotechnology Catalysis Cold Temperature Cold-adapted Computational, genetic and chemical modification Enzymes Enzymes - chemistry Enzymes - genetics Genetic Engineering Genetics Hot Temperature Magnetic nanoparticles Natural resources Organisms Protein structure, function, stability Psychrophiles Psychrophilic Thermophilic Tradeoffs Translations |
title | Some like it hot, some like it cold: Temperature dependent biotechnological applications and improvements in extremophilic enzymes |
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