Site-directed mutagenesis of coenzyme-independent carotenoid oxygenase CSO2 to enhance the enzymatic synthesis of vanillin
Vanillin is a popular flavoring compound and an important food additive. Owing to the consumer preference for inexpensive natural aroma flavors, vanillin production through a biotechnological pathway has become of great interest and commercial value in recent years. In this study, an enzymatic synth...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2020-05, Vol.104 (9), p.3897-3907 |
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| creator | Yao, Xueyan Lv, Yuemeng Yu, Huilei Cao, Hao Wang, Luyao Wen, Boting Gu, Tianyi Wang, Fengzhong Sun, Lichao Xin, Fengjiao |
| description | Vanillin is a popular flavoring compound and an important food additive. Owing to the consumer preference for inexpensive natural aroma flavors, vanillin production through a biotechnological pathway has become of great interest and commercial value in recent years. In this study, an enzymatic synthetic system for vanillin using a coenzyme-independent decarboxylase (FDC) and oxygenase (CSO2) cascade was reconstituted and optimized. This system produces a slightly higher production yield (40.20%) than the largest yield reported for immobilized FDC and CSO2 (35.00%) with ferulic acid as a substrate. It was previously reported that the low catalytic activity and thermal instability of CSO2 restrict the overall productivity of vanillin. In present study, site-directed mutagenesis was applied to rate-limiting oxygenase CSO2 to generate positive mutants. The production yields of mutants A49P (58.44%) and Q390A (65.29%) were 1.45- and 1.62-fold that of CSO2 wild type, respectively. The potential mechanism for enhanced vanillin production using A49P involved increased thermostability and catalytic efficiency, while that using Q390A was probably associated with a better thermostable performance and increased catalytic efficiency resulting from a larger entrance channel. |
| doi_str_mv | 10.1007/s00253-020-10433-1 |
| format | Article |
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Owing to the consumer preference for inexpensive natural aroma flavors, vanillin production through a biotechnological pathway has become of great interest and commercial value in recent years. In this study, an enzymatic synthetic system for vanillin using a coenzyme-independent decarboxylase (FDC) and oxygenase (CSO2) cascade was reconstituted and optimized. This system produces a slightly higher production yield (40.20%) than the largest yield reported for immobilized FDC and CSO2 (35.00%) with ferulic acid as a substrate. It was previously reported that the low catalytic activity and thermal instability of CSO2 restrict the overall productivity of vanillin. In present study, site-directed mutagenesis was applied to rate-limiting oxygenase CSO2 to generate positive mutants. The production yields of mutants A49P (58.44%) and Q390A (65.29%) were 1.45- and 1.62-fold that of CSO2 wild type, respectively. The potential mechanism for enhanced vanillin production using A49P involved increased thermostability and catalytic efficiency, while that using Q390A was probably associated with a better thermostable performance and increased catalytic efficiency resulting from a larger entrance channel.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-020-10433-1</identifier><identifier>PMID: 32130469</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Aroma ; Bacillus pumilus - enzymology ; Bacillus pumilus - genetics ; Benzaldehydes - metabolism ; Biomedical and Life Sciences ; Biosynthesis ; Biotechnologically Relevant Enzymes and Proteins ; Biotechnology ; Carotenoids ; Catalysis ; Catalytic activity ; Caulobacter - enzymology ; Caulobacter - genetics ; Coenzymes ; Enzymatic synthesis ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Ferulic acid ; Food additives ; Hydrogen-Ion Concentration ; Life Sciences ; Metabolic Engineering ; Methods ; Microbial Genetics and Genomics ; Microbiological research ; Microbiology ; Mutagenesis ; Mutagenesis, Site-Directed ; Mutants ; Oxidases ; Oxygenase ; Oxygenases - genetics ; Oxygenases - metabolism ; Physiological aspects ; Protein Biosynthesis ; Site-directed mutagenesis ; Substrates ; Thermal instability ; Thermal stability ; Vanillin</subject><ispartof>Applied microbiology and biotechnology, 2020-05, Vol.104 (9), p.3897-3907</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2020</rights><rights>COPYRIGHT 2020 Springer</rights><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2020.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c513t-987f701f884c1b1f4a4d281899eaf56f7773d131c21071aeb29458410414e8853</citedby><cites>FETCH-LOGICAL-c513t-987f701f884c1b1f4a4d281899eaf56f7773d131c21071aeb29458410414e8853</cites><orcidid>0000-0002-8494-1419</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-020-10433-1$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-020-10433-1$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32130469$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yao, Xueyan</creatorcontrib><creatorcontrib>Lv, Yuemeng</creatorcontrib><creatorcontrib>Yu, Huilei</creatorcontrib><creatorcontrib>Cao, Hao</creatorcontrib><creatorcontrib>Wang, Luyao</creatorcontrib><creatorcontrib>Wen, Boting</creatorcontrib><creatorcontrib>Gu, Tianyi</creatorcontrib><creatorcontrib>Wang, Fengzhong</creatorcontrib><creatorcontrib>Sun, Lichao</creatorcontrib><creatorcontrib>Xin, Fengjiao</creatorcontrib><title>Site-directed mutagenesis of coenzyme-independent carotenoid oxygenase CSO2 to enhance the enzymatic synthesis of vanillin</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>Vanillin is a popular flavoring compound and an important food additive. Owing to the consumer preference for inexpensive natural aroma flavors, vanillin production through a biotechnological pathway has become of great interest and commercial value in recent years. In this study, an enzymatic synthetic system for vanillin using a coenzyme-independent decarboxylase (FDC) and oxygenase (CSO2) cascade was reconstituted and optimized. This system produces a slightly higher production yield (40.20%) than the largest yield reported for immobilized FDC and CSO2 (35.00%) with ferulic acid as a substrate. It was previously reported that the low catalytic activity and thermal instability of CSO2 restrict the overall productivity of vanillin. In present study, site-directed mutagenesis was applied to rate-limiting oxygenase CSO2 to generate positive mutants. The production yields of mutants A49P (58.44%) and Q390A (65.29%) were 1.45- and 1.62-fold that of CSO2 wild type, respectively. The potential mechanism for enhanced vanillin production using A49P involved increased thermostability and catalytic efficiency, while that using Q390A was probably associated with a better thermostable performance and increased catalytic efficiency resulting from a larger entrance channel.</description><subject>Aroma</subject><subject>Bacillus pumilus - enzymology</subject><subject>Bacillus pumilus - genetics</subject><subject>Benzaldehydes - metabolism</subject><subject>Biomedical and Life Sciences</subject><subject>Biosynthesis</subject><subject>Biotechnologically Relevant Enzymes and Proteins</subject><subject>Biotechnology</subject><subject>Carotenoids</subject><subject>Catalysis</subject><subject>Catalytic activity</subject><subject>Caulobacter - enzymology</subject><subject>Caulobacter - genetics</subject><subject>Coenzymes</subject><subject>Enzymatic synthesis</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Ferulic 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mutagenesis of coenzyme-independent carotenoid oxygenase CSO2 to enhance the enzymatic synthesis of vanillin</title><author>Yao, Xueyan ; Lv, Yuemeng ; Yu, Huilei ; Cao, Hao ; Wang, Luyao ; Wen, Boting ; Gu, Tianyi ; Wang, Fengzhong ; Sun, Lichao ; Xin, Fengjiao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c513t-987f701f884c1b1f4a4d281899eaf56f7773d131c21071aeb29458410414e8853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Aroma</topic><topic>Bacillus pumilus - enzymology</topic><topic>Bacillus pumilus - genetics</topic><topic>Benzaldehydes - metabolism</topic><topic>Biomedical and Life Sciences</topic><topic>Biosynthesis</topic><topic>Biotechnologically Relevant Enzymes and Proteins</topic><topic>Biotechnology</topic><topic>Carotenoids</topic><topic>Catalysis</topic><topic>Catalytic activity</topic><topic>Caulobacter - enzymology</topic><topic>Caulobacter - 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Owing to the consumer preference for inexpensive natural aroma flavors, vanillin production through a biotechnological pathway has become of great interest and commercial value in recent years. In this study, an enzymatic synthetic system for vanillin using a coenzyme-independent decarboxylase (FDC) and oxygenase (CSO2) cascade was reconstituted and optimized. This system produces a slightly higher production yield (40.20%) than the largest yield reported for immobilized FDC and CSO2 (35.00%) with ferulic acid as a substrate. It was previously reported that the low catalytic activity and thermal instability of CSO2 restrict the overall productivity of vanillin. In present study, site-directed mutagenesis was applied to rate-limiting oxygenase CSO2 to generate positive mutants. The production yields of mutants A49P (58.44%) and Q390A (65.29%) were 1.45- and 1.62-fold that of CSO2 wild type, respectively. 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| subjects | Aroma Bacillus pumilus - enzymology Bacillus pumilus - genetics Benzaldehydes - metabolism Biomedical and Life Sciences Biosynthesis Biotechnologically Relevant Enzymes and Proteins Biotechnology Carotenoids Catalysis Catalytic activity Caulobacter - enzymology Caulobacter - genetics Coenzymes Enzymatic synthesis Escherichia coli - genetics Escherichia coli - metabolism Ferulic acid Food additives Hydrogen-Ion Concentration Life Sciences Metabolic Engineering Methods Microbial Genetics and Genomics Microbiological research Microbiology Mutagenesis Mutagenesis, Site-Directed Mutants Oxidases Oxygenase Oxygenases - genetics Oxygenases - metabolism Physiological aspects Protein Biosynthesis Site-directed mutagenesis Substrates Thermal instability Thermal stability Vanillin |
| title | Site-directed mutagenesis of coenzyme-independent carotenoid oxygenase CSO2 to enhance the enzymatic synthesis of vanillin |
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