Preparation of umami octopeptide with recombined Escherichia coli: Feasibility and challenges
The taste of umami peptide H-Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala-OH (LGAGGSLA) is controversial. One possible reason for this controversy is the use of chemically synthesized LGAGGSLA to confirm its taste. To explore other ways to further confirm the flavor of LGAGGSLA, we developed a new strategy to pr...
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| Veröffentlicht in: | Bioengineered 2018-01, Vol.9 (1), p.166-169 |
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| creator | Zhao, Liming Zhang, Yin Venkitasamy, Chandrasekar Pan, Zhongli Zhang, Longyi Guo, Siya Xiong, Wei Xia, Hu Wenlong, Liu Xinhua, Gou |
| description | The taste of umami peptide H-Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala-OH (LGAGGSLA) is controversial. One possible reason for this controversy is the use of chemically synthesized LGAGGSLA to confirm its taste. To explore other ways to further confirm the flavor of LGAGGSLA, we developed a new strategy to prepare a bio-source peptide by adopting a gene engineering method to express LGAGGSLA in recombinant Escherichia coli. In our previous work, we structured the LGAGGSLA recombinant expression system and optimized the culturing conditions for preparing a fusion protein. However, the fusion protein was not cleaved by enterokinase to obtain LGAGGSLA. Because the cleavage conditions of commercial enterokinase were not specific and recombinant engineered bacteria had the potential to be used in industrial processes, in this addendum, we calculated the mass and volume yields of key processing steps in the preparation of LGAGGSLA, and established a model of cleavage conditions with the cleavage ratio of LGAGGSLA. When the LGAGGSLA was confirmed to show umami taste, it is considered as a new umami or umami enhancer. The gene information of LGAGGSLA should have a great potential in the development of new flavor product and food product containing high umami flavor. |
| doi_str_mv | 10.1080/21655979.2017.1378839 |
| format | Article |
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One possible reason for this controversy is the use of chemically synthesized LGAGGSLA to confirm its taste. To explore other ways to further confirm the flavor of LGAGGSLA, we developed a new strategy to prepare a bio-source peptide by adopting a gene engineering method to express LGAGGSLA in recombinant Escherichia coli. In our previous work, we structured the LGAGGSLA recombinant expression system and optimized the culturing conditions for preparing a fusion protein. However, the fusion protein was not cleaved by enterokinase to obtain LGAGGSLA. Because the cleavage conditions of commercial enterokinase were not specific and recombinant engineered bacteria had the potential to be used in industrial processes, in this addendum, we calculated the mass and volume yields of key processing steps in the preparation of LGAGGSLA, and established a model of cleavage conditions with the cleavage ratio of LGAGGSLA. When the LGAGGSLA was confirmed to show umami taste, it is considered as a new umami or umami enhancer. The gene information of LGAGGSLA should have a great potential in the development of new flavor product and food product containing high umami flavor.</description><identifier>ISSN: 2165-5979</identifier><identifier>EISSN: 2165-5987</identifier><identifier>DOI: 10.1080/21655979.2017.1378839</identifier><identifier>PMID: 28902573</identifier><language>eng</language><publisher>United States: Taylor & Francis</publisher><subject>Addendum ; Amino Acid Sequence ; Cloning, Molecular ; Enteropeptidase - chemistry ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Food Technology - methods ; fusion protein ; Gene Expression ; Genetic Vectors - chemistry ; Genetic Vectors - metabolism ; Humans ; Hydrolysis ; octopeptide ; Odorants - analysis ; Oligopeptides - biosynthesis ; Oligopeptides - genetics ; Oligopeptides - isolation & purification ; Protein Engineering - methods ; recombinant bacteria ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Taste - physiology ; umami ; umami peptide</subject><ispartof>Bioengineered, 2018-01, Vol.9 (1), p.166-169</ispartof><rights>2018 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group © Liming Zhao, Yin Zhang, Chandrasekar Venkitasamy, Zhongli Pan, Longyi Zhang, Siya Guo, Wei Xiong, Hu Xia, Liu Wenlong, and Gou Xinhua 2018</rights><rights>2018 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group 2018 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c468t-8e393ccc4fbba306ee3017da502dbc17030945fec105088c98eb9a487b2635c23</citedby><cites>FETCH-LOGICAL-c468t-8e393ccc4fbba306ee3017da502dbc17030945fec105088c98eb9a487b2635c23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5972915/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5972915/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27479,27901,27902,53766,53768,59116,59117</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28902573$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhao, Liming</creatorcontrib><creatorcontrib>Zhang, Yin</creatorcontrib><creatorcontrib>Venkitasamy, Chandrasekar</creatorcontrib><creatorcontrib>Pan, Zhongli</creatorcontrib><creatorcontrib>Zhang, Longyi</creatorcontrib><creatorcontrib>Guo, Siya</creatorcontrib><creatorcontrib>Xiong, Wei</creatorcontrib><creatorcontrib>Xia, Hu</creatorcontrib><creatorcontrib>Wenlong, Liu</creatorcontrib><creatorcontrib>Xinhua, Gou</creatorcontrib><title>Preparation of umami octopeptide with recombined Escherichia coli: Feasibility and challenges</title><title>Bioengineered</title><addtitle>Bioengineered</addtitle><description>The taste of umami peptide H-Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala-OH (LGAGGSLA) is controversial. One possible reason for this controversy is the use of chemically synthesized LGAGGSLA to confirm its taste. To explore other ways to further confirm the flavor of LGAGGSLA, we developed a new strategy to prepare a bio-source peptide by adopting a gene engineering method to express LGAGGSLA in recombinant Escherichia coli. In our previous work, we structured the LGAGGSLA recombinant expression system and optimized the culturing conditions for preparing a fusion protein. However, the fusion protein was not cleaved by enterokinase to obtain LGAGGSLA. Because the cleavage conditions of commercial enterokinase were not specific and recombinant engineered bacteria had the potential to be used in industrial processes, in this addendum, we calculated the mass and volume yields of key processing steps in the preparation of LGAGGSLA, and established a model of cleavage conditions with the cleavage ratio of LGAGGSLA. When the LGAGGSLA was confirmed to show umami taste, it is considered as a new umami or umami enhancer. The gene information of LGAGGSLA should have a great potential in the development of new flavor product and food product containing high umami flavor.</description><subject>Addendum</subject><subject>Amino Acid Sequence</subject><subject>Cloning, Molecular</subject><subject>Enteropeptidase - chemistry</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Food Technology - methods</subject><subject>fusion protein</subject><subject>Gene Expression</subject><subject>Genetic Vectors - chemistry</subject><subject>Genetic Vectors - metabolism</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>octopeptide</subject><subject>Odorants - analysis</subject><subject>Oligopeptides - biosynthesis</subject><subject>Oligopeptides - genetics</subject><subject>Oligopeptides - isolation & purification</subject><subject>Protein Engineering - methods</subject><subject>recombinant bacteria</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Taste - physiology</subject><subject>umami</subject><subject>umami peptide</subject><issn>2165-5979</issn><issn>2165-5987</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>0YH</sourceid><sourceid>EIF</sourceid><recordid>eNp9kcFvFCEUxonR2Kb2T9Bw9LIrDMMCHoymaa1JEz3o0RDmzZsOhoERWJv9753Nbjf14okX-N73Pd6PkNecrTnT7F3DN1IaZdYN42rNhdJamGfkfH-_kkar56damTNyWcovxhhnopVKvyRnjTaskUqck5_fMs4uu-pTpGmg28lNniaoaca5-h7pg68jzQhp6nzEnl4XGDF7GL2jkIJ_T2_QFd_54OuOuthTGF0IGO-xvCIvBhcKXh7PC_Lj5vr71e3q7uvnL1ef7lbQbnRdaRRGAEA7dJ0TbIMoln_1TrKm74ArJphp5YDAmWRag9HYGddq1TUbIaERF-TDwXfedhP2gLFmF-yc_eTyzibn7b8v0Y_2Pv2xy34aw-Vi8PZokNPvLZZqJ18AQ3AR07ZYboTWUrF2L5UHKeRUSsbhFMOZ3dOxj3Tsno490ln63jyd8dT1yGIRfDwIfBxSntxDyqG31e1CykN2EXyx4v8ZfwHs2aDc</recordid><startdate>20180101</startdate><enddate>20180101</enddate><creator>Zhao, Liming</creator><creator>Zhang, Yin</creator><creator>Venkitasamy, Chandrasekar</creator><creator>Pan, Zhongli</creator><creator>Zhang, Longyi</creator><creator>Guo, Siya</creator><creator>Xiong, Wei</creator><creator>Xia, Hu</creator><creator>Wenlong, Liu</creator><creator>Xinhua, Gou</creator><general>Taylor & Francis</general><scope>0YH</scope><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>5PM</scope></search><sort><creationdate>20180101</creationdate><title>Preparation of umami octopeptide with recombined Escherichia coli: Feasibility and challenges</title><author>Zhao, Liming ; Zhang, Yin ; Venkitasamy, Chandrasekar ; Pan, Zhongli ; Zhang, Longyi ; Guo, Siya ; Xiong, Wei ; Xia, Hu ; Wenlong, Liu ; Xinhua, Gou</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c468t-8e393ccc4fbba306ee3017da502dbc17030945fec105088c98eb9a487b2635c23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Addendum</topic><topic>Amino Acid Sequence</topic><topic>Cloning, Molecular</topic><topic>Enteropeptidase - chemistry</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Food Technology - methods</topic><topic>fusion protein</topic><topic>Gene Expression</topic><topic>Genetic Vectors - chemistry</topic><topic>Genetic Vectors - metabolism</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>octopeptide</topic><topic>Odorants - analysis</topic><topic>Oligopeptides - biosynthesis</topic><topic>Oligopeptides - genetics</topic><topic>Oligopeptides - isolation & purification</topic><topic>Protein Engineering - methods</topic><topic>recombinant bacteria</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Taste - physiology</topic><topic>umami</topic><topic>umami peptide</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhao, Liming</creatorcontrib><creatorcontrib>Zhang, Yin</creatorcontrib><creatorcontrib>Venkitasamy, Chandrasekar</creatorcontrib><creatorcontrib>Pan, Zhongli</creatorcontrib><creatorcontrib>Zhang, Longyi</creatorcontrib><creatorcontrib>Guo, Siya</creatorcontrib><creatorcontrib>Xiong, Wei</creatorcontrib><creatorcontrib>Xia, Hu</creatorcontrib><creatorcontrib>Wenlong, Liu</creatorcontrib><creatorcontrib>Xinhua, Gou</creatorcontrib><collection>Taylor & Francis Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Bioengineered</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhao, Liming</au><au>Zhang, Yin</au><au>Venkitasamy, Chandrasekar</au><au>Pan, Zhongli</au><au>Zhang, Longyi</au><au>Guo, Siya</au><au>Xiong, Wei</au><au>Xia, Hu</au><au>Wenlong, Liu</au><au>Xinhua, Gou</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preparation of umami octopeptide with recombined Escherichia coli: Feasibility and challenges</atitle><jtitle>Bioengineered</jtitle><addtitle>Bioengineered</addtitle><date>2018-01-01</date><risdate>2018</risdate><volume>9</volume><issue>1</issue><spage>166</spage><epage>169</epage><pages>166-169</pages><issn>2165-5979</issn><eissn>2165-5987</eissn><abstract>The taste of umami peptide H-Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala-OH (LGAGGSLA) is controversial. One possible reason for this controversy is the use of chemically synthesized LGAGGSLA to confirm its taste. To explore other ways to further confirm the flavor of LGAGGSLA, we developed a new strategy to prepare a bio-source peptide by adopting a gene engineering method to express LGAGGSLA in recombinant Escherichia coli. In our previous work, we structured the LGAGGSLA recombinant expression system and optimized the culturing conditions for preparing a fusion protein. However, the fusion protein was not cleaved by enterokinase to obtain LGAGGSLA. Because the cleavage conditions of commercial enterokinase were not specific and recombinant engineered bacteria had the potential to be used in industrial processes, in this addendum, we calculated the mass and volume yields of key processing steps in the preparation of LGAGGSLA, and established a model of cleavage conditions with the cleavage ratio of LGAGGSLA. When the LGAGGSLA was confirmed to show umami taste, it is considered as a new umami or umami enhancer. The gene information of LGAGGSLA should have a great potential in the development of new flavor product and food product containing high umami flavor.</abstract><cop>United States</cop><pub>Taylor & Francis</pub><pmid>28902573</pmid><doi>10.1080/21655979.2017.1378839</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Addendum Amino Acid Sequence Cloning, Molecular Enteropeptidase - chemistry Escherichia coli - genetics Escherichia coli - metabolism Food Technology - methods fusion protein Gene Expression Genetic Vectors - chemistry Genetic Vectors - metabolism Humans Hydrolysis octopeptide Odorants - analysis Oligopeptides - biosynthesis Oligopeptides - genetics Oligopeptides - isolation & purification Protein Engineering - methods recombinant bacteria Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Taste - physiology umami umami peptide |
| title | Preparation of umami octopeptide with recombined Escherichia coli: Feasibility and challenges |
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