Recombinant Production of Arginyl Dipeptides by l-Amino Acid Ligase RizA Coupled with ATP Regeneration
Arginyl dipeptides like Arg-Ser, Arg-Ala, and Arg-Gly are salt-taste enhancers and can potentially be used to reduce the salt content of food. The l-amino acid ligase RizA from B. subtilis selectively synthesizes arginyl dipeptides. However, industrial application is prevented by the high cost of th...
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| Published in | Catalysts Vol. 11; no. 11; p. 1290 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
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01.11.2021
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| Abstract | Arginyl dipeptides like Arg-Ser, Arg-Ala, and Arg-Gly are salt-taste enhancers and can potentially be used to reduce the salt content of food. The l-amino acid ligase RizA from B. subtilis selectively synthesizes arginyl dipeptides. However, industrial application is prevented by the high cost of the cofactor adenosine triphosphate (ATP). Thus, a coupled reaction system was created consisting of RizA and acetate kinase (AckA) from E. coli providing ATP regeneration from acetyl phosphate. Both enzymes were recombinantly produced in E. coli and purified by affinity chromatography. Biocatalytic reactions were varied and analyzed by RP-HPLC with fluorescence detection. Under optimal conditions the system produced up to 5.9 g/L Arg-Ser corresponding to an ATP efficiency of 23 g Arg-Ser per gram ATP. Using similar conditions with alanine or glycine as second amino acid, 2.6 g/L Arg-Ala or 2.4 g/L Arg Gly were produced. The RizA/AckA system selectively produced substantial amounts of arginyl dipeptides while minimizing the usage of the expensive ATP. |
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| AbstractList | Arginyl dipeptides like Arg-Ser, Arg-Ala, and Arg-Gly are salt-taste enhancers and can potentially be used to reduce the salt content of food. The l-amino acid ligase RizA from B. subtilis selectively synthesizes arginyl dipeptides. However, industrial application is prevented by the high cost of the cofactor adenosine triphosphate (ATP). Thus, a coupled reaction system was created consisting of RizA and acetate kinase (AckA) from E. coli providing ATP regeneration from acetyl phosphate. Both enzymes were recombinantly produced in E. coli and purified by affinity chromatography. Biocatalytic reactions were varied and analyzed by RP-HPLC with fluorescence detection. Under optimal conditions the system produced up to 5.9 g/L Arg-Ser corresponding to an ATP efficiency of 23 g Arg-Ser per gram ATP. Using similar conditions with alanine or glycine as second amino acid, 2.6 g/L Arg-Ala or 2.4 g/L Arg Gly were produced. The RizA/AckA system selectively produced substantial amounts of arginyl dipeptides while minimizing the usage of the expensive ATP. |
| Author | Berger, Ralf G. Mast, Tim A. Bordewick, Sven Ersoy, Franziska |
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| Cites_doi | 10.1021/acs.jafc.9b04385 10.1002/cbic.201402550 10.1002/mnfr.201200168 10.1038/sj.jhh.1001459 10.1271/bbb.80842 10.1016/j.jbiosc.2016.01.014 10.1007/s00253-008-1590-3 10.1263/jbb.106.313 10.1038/s41929-020-0429-x 10.1016/j.btre.2016.10.001 10.1016/j.enzmictec.2020.109537 10.1038/jhh.2008.144 10.1080/09168451.2015.1056511 10.1002/(SICI)1097-0290(1999)66:3<180::AID-BIT6>3.0.CO;2-S 10.1136/bmj.b4567 10.1093/oxfordjournals.jbchem.a132108 10.1021/acschembio.6b00838 10.1371/journal.pone.0130247 10.3390/catal10010033 10.1021/jo00166a048 10.1016/j.bbrc.2008.04.105 10.1007/s11274-013-1534-7 10.1016/j.meatsci.2006.04.014 10.1016/j.foodcont.2020.107739 10.1021/acs.jafc.0c04055 10.1021/bi500292b 10.1021/acs.jafc.6b02716 10.1080/07388551.2020.1826403 10.1126/science.aay8484 10.1002/bmb.2002.494030060138 10.1038/42388 |
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| References | Kino (ref_23) 2008; 371 Andexer (ref_14) 2015; 16 Yushkova (ref_30) 2019; 67 Kagebayashi (ref_29) 2012; 56 ref_12 Kim (ref_19) 1999; 66 Nakajima (ref_25) 1978; 84 Harth (ref_9) 2018; 66 Wang (ref_10) 2020; 136 Suo (ref_31) 2016; 12 Strazzullo (ref_3) 2009; 339 Li (ref_15) 2020; 68 Kino (ref_11) 2009; 73 Rottmann (ref_32) 2021; 123 He (ref_1) 2009; 23 Crans (ref_18) 1983; 48 Kino (ref_21) 2015; 79 Dean (ref_26) 2002; 30 Huffman (ref_20) 2019; 366 Kino (ref_24) 2008; 106 Chen (ref_17) 2021; 41 Kino (ref_27) 2016; 122 Alissandratos (ref_13) 2016; 11 He (ref_5) 2002; 16 Desmond (ref_6) 2006; 74 Burgener (ref_28) 2020; 3 ref_2 Yan (ref_16) 2014; 30 Breslin (ref_7) 1997; 387 Yagasaki (ref_8) 2008; 81 ref_4 Tsuda (ref_22) 2014; 53 |
| References_xml | – volume: 67 start-page: 11553 year: 2019 ident: ref_30 article-title: Application of Immobilized Enzymes in Food Industry publication-title: J. Agric. Food Chem. doi: 10.1021/acs.jafc.9b04385 contributor: fullname: Yushkova – volume: 16 start-page: 380 year: 2015 ident: ref_14 article-title: Emerging Enzymes for ATP Regeneration in Biocatalytic Processes publication-title: ChemBioChem doi: 10.1002/cbic.201402550 contributor: fullname: Andexer – volume: 56 start-page: 1456 year: 2012 ident: ref_29 article-title: Novel CCK-dependent vasorelaxing dipeptide, Arg-Phe, decreases blood pressure and food intake in rodents publication-title: Mol. Nutr. Food Res. doi: 10.1002/mnfr.201200168 contributor: fullname: Kagebayashi – volume: 16 start-page: 761 year: 2002 ident: ref_5 article-title: Effect of modest salt reduction on blood pressure: A meta-analysis of randomized trials. Implications for public health publication-title: J. Hum. Hypertens. doi: 10.1038/sj.jhh.1001459 contributor: fullname: He – volume: 73 start-page: 901 year: 2009 ident: ref_11 article-title: A Novel L-Amino Acid Ligase from Bacillus subtilis NBRC3134, a Microorganism Producing Peptide-Antibiotic Rhizocticin publication-title: Biosci. Biotechnol. Biochem. doi: 10.1271/bbb.80842 contributor: fullname: Kino – volume: 122 start-page: 155 year: 2016 ident: ref_27 article-title: Effective production of Pro–Gly by mutagenesis of l-amino acid ligase publication-title: J. Biosci. Bioeng. doi: 10.1016/j.jbiosc.2016.01.014 contributor: fullname: Kino – volume: 81 start-page: 13 year: 2008 ident: ref_8 article-title: Synthesis and application of dipeptides; current status and perspectives publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-008-1590-3 contributor: fullname: Yagasaki – volume: 106 start-page: 313 year: 2008 ident: ref_24 article-title: A novel L-amino acid ligase from Bacillus Licheniformis publication-title: J. Biosci. Bioeng. doi: 10.1263/jbb.106.313 contributor: fullname: Kino – volume: 3 start-page: 186 year: 2020 ident: ref_28 article-title: A roadmap towards integrated catalytic systems of the future publication-title: Nat. Cat. doi: 10.1038/s41929-020-0429-x contributor: fullname: Burgener – volume: 12 start-page: 33 year: 2016 ident: ref_31 article-title: Nucleic acid protocols: Extraction and optimization publication-title: Biotechnol. Rep. doi: 10.1016/j.btre.2016.10.001 contributor: fullname: Suo – volume: 136 start-page: 109537 year: 2020 ident: ref_10 article-title: L-amino acid ligase: A promising alternative for the biosynthesis of L-dipeptides publication-title: Enzyme Microb. Technol. doi: 10.1016/j.enzmictec.2020.109537 contributor: fullname: Wang – volume: 23 start-page: 363 year: 2009 ident: ref_1 article-title: A comprehensive review on salt and health and current experience of worldwide salt reduction programmes publication-title: J. Hum. Hypertens. doi: 10.1038/jhh.2008.144 contributor: fullname: He – volume: 79 start-page: 1827 year: 2015 ident: ref_21 article-title: Alteration of the substrate specificity of L-amino acid ligase and selective synthesis of Met-Gly as a salt taste enhancer publication-title: Biosci. Biotechnol. Biochem. doi: 10.1080/09168451.2015.1056511 contributor: fullname: Kino – volume: 66 start-page: 180 year: 1999 ident: ref_19 article-title: Prolonging cell-free protein synthesis with a novel ATP regeneration system publication-title: Biotechnol. Bioeng. doi: 10.1002/(SICI)1097-0290(1999)66:3<180::AID-BIT6>3.0.CO;2-S contributor: fullname: Kim – volume: 339 start-page: b4567 year: 2009 ident: ref_3 article-title: Salt intake, stroke, and cardiovascular disease: Meta-analysis of prospective studies publication-title: BMJ doi: 10.1136/bmj.b4567 contributor: fullname: Strazzullo – volume: 84 start-page: 193 year: 1978 ident: ref_25 article-title: Purification and Properties of Acetate Kinase from Bacillus stearothermophilus publication-title: J. Biochem. doi: 10.1093/oxfordjournals.jbchem.a132108 contributor: fullname: Nakajima – volume: 11 start-page: 3289 year: 2016 ident: ref_13 article-title: ATP Recycling with Cell Lysate for Enzyme-Catalyzed Chemical Synthesis, Protein Expression and PCR publication-title: ACS Chem. Biol. doi: 10.1021/acschembio.6b00838 contributor: fullname: Alissandratos – ident: ref_2 doi: 10.1371/journal.pone.0130247 – ident: ref_4 – ident: ref_12 doi: 10.3390/catal10010033 – volume: 48 start-page: 3130 year: 1983 ident: ref_18 article-title: A convenient synthesis of disodium acetyl phosphate for use in in situ ATP cofactor regeneration publication-title: J. Org. Chem. doi: 10.1021/jo00166a048 contributor: fullname: Crans – volume: 371 start-page: 536 year: 2008 ident: ref_23 article-title: Dipeptide synthesis by L-amino acid ligase from Ralstonia solanacearum publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2008.04.105 contributor: fullname: Kino – volume: 30 start-page: 1123 year: 2014 ident: ref_16 article-title: Production of glucose-6-phosphate by glucokinase coupled with an ATP regeneration system publication-title: World J. Microbiol. Biotechnol. doi: 10.1007/s11274-013-1534-7 contributor: fullname: Yan – volume: 74 start-page: 188 year: 2006 ident: ref_6 article-title: Reducing salt: A challenge for the meat industry publication-title: Meat Sci. doi: 10.1016/j.meatsci.2006.04.014 contributor: fullname: Desmond – volume: 123 start-page: 107739 year: 2021 ident: ref_32 article-title: Enzymatic acrylamide mitigation in French fries–An industrial-scale case study publication-title: Food Control doi: 10.1016/j.foodcont.2020.107739 contributor: fullname: Rottmann – volume: 68 start-page: 9188 year: 2020 ident: ref_15 article-title: Efficient One-Pot Synthesis of Cytidine 5′-Monophosphate Using an Extremophilic Enzyme Cascade System publication-title: J. Agric. Food Chem. doi: 10.1021/acs.jafc.0c04055 contributor: fullname: Li – volume: 53 start-page: 2650 year: 2014 ident: ref_22 article-title: Single Mutation Alters the Substrate Specificity of L-Amino Acid Ligase publication-title: Biochemistry doi: 10.1021/bi500292b contributor: fullname: Tsuda – volume: 66 start-page: 2344 year: 2018 ident: ref_9 article-title: Salt Taste Enhancing L-Arginyl Dipeptides from Casein and Lysozyme Released by Peptidases of Basidiomycota publication-title: J. Agric. Food Chem. doi: 10.1021/acs.jafc.6b02716 contributor: fullname: Harth – volume: 41 start-page: 16 year: 2021 ident: ref_17 article-title: Enzymatic regeneration and conservation of ATP: Challenges and opportunities publication-title: Crit. Rev. Biotechnol. doi: 10.1080/07388551.2020.1826403 contributor: fullname: Chen – volume: 366 start-page: 1255 year: 2019 ident: ref_20 article-title: Design of an in vitro biocatalytic cascade for the manufacture of islatravir publication-title: Science doi: 10.1126/science.aay8484 contributor: fullname: Huffman – volume: 30 start-page: 401 year: 2002 ident: ref_26 article-title: Kinetic studies with alkaline phosphatase in the presence and absence of inhibitors and divalent cations publication-title: Biochem. Mol. Biol. Educ. doi: 10.1002/bmb.2002.494030060138 contributor: fullname: Dean – volume: 387 start-page: 563 year: 1997 ident: ref_7 article-title: Salt enhances flavour by suppressing bitterness publication-title: Nature doi: 10.1038/42388 contributor: fullname: Breslin |
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| SubjectTerms | acetate kinase Adenosine triphosphate Alanine Amino acids arginyl dipeptides ATP regeneration Blood pressure Catalysts Chemical reactions coupled catalysis E coli Enzymes Experiments Fluorescence Glycine High performance liquid chromatography Industrial applications Kinases l -amino acid ligase Regeneration salt taste Taste |
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| Title | Recombinant Production of Arginyl Dipeptides by l-Amino Acid Ligase RizA Coupled with ATP Regeneration |
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