دورية أكاديمية
Use of Flavin-Containing Monooxygenases for Conversion of Trimethylamine in Salmon Protein Hydrolysates.
| العنوان: | Use of Flavin-Containing Monooxygenases for Conversion of Trimethylamine in Salmon Protein Hydrolysates. |
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| المؤلفون: | Goris M; NORCE Norwegian Research Centre, Bergen, Norway., Puntervoll P; NORCE Norwegian Research Centre, Bergen, Norway., Rojo D; Centre for Metabolomics and Bioanalysis (CEMBIO), Department of Chemistry and Biochemistry, Facultad de Farmacia, Universidad San Pablo-CEU, CEU Universities, Urbanización Montepríncipe, Madrid, Spain., Claussen J; NORCE Norwegian Research Centre, Bergen, Norway., Larsen Ø; NORCE Norwegian Research Centre, Bergen, Norway., Garcia-Moyano A; NORCE Norwegian Research Centre, Bergen, Norway., Almendral D; Institute of Catalysis, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain., Barbas C; Centre for Metabolomics and Bioanalysis (CEMBIO), Department of Chemistry and Biochemistry, Facultad de Farmacia, Universidad San Pablo-CEU, CEU Universities, Urbanización Montepríncipe, Madrid, Spain., Ferrer M; Institute of Catalysis, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain., Bjerga GEK; NORCE Norwegian Research Centre, Bergen, Norway gro.bjerga@norceresearch.no. |
| المصدر: | Applied and environmental microbiology [Appl Environ Microbiol] 2020 Nov 24; Vol. 86 (24). Date of Electronic Publication: 2020 Nov 24 (Print Publication: 2020). |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 7605801 Publication Model: Electronic-Print Cited Medium: Internet ISSN: 1098-5336 (Electronic) Linking ISSN: 00992240 NLM ISO Abbreviation: Appl Environ Microbiol Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, American Society for Microbiology. |
| مواضيع طبية MeSH: | Bacterial Proteins/*metabolism , Escherichia coli/*metabolism , Methylamines/*metabolism , Oxygenases/*metabolism, Amino Acid Sequence ; Bacterial Proteins/chemistry ; Oxygenases/chemistry ; Phylogeny ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Sequence Alignment |
| مستخلص: | Enzymatic processing of fish by-products for recovery of peptides (hydrolysates) is a promising technology to reach food grade ingredients of high nutritional quality. Despite this, their bitter taste and "fish" odor block implementation in food products and limit their economic potential. Trimethylamine (TMA) is a known contributor to malodor in fish. Current strategies to mask or remove the odor either are not effective or give rise to undesirable side effects. As an alternative approach to remediate TMA, we propose a novel enzymatic strategy to convert TMA into the odorless trimethylamine N -oxide (TMAO) using TMA monooxygenases (Tmms). We identified a diverse set of bacterial Tmms using a sequence similarity network. Purified, recombinant enzymes were assessed for their biocatalytic capacity by monitoring NADPH consumption and TMAO generation. Selected Tmms were subjected to biochemical characterization and investigated for their ability to oxidize TMA in an industry-relevant substrate. From the 45 bacterial Tmm candidates investigated, eight enzymes from four different taxa were selected for their high activity toward TMA. The three most active enzymes were shown to vary in temperature optimum, with the highest being 45°C. Enzymatic activity dropped at high temperatures, likely due to structural unfolding. The enzymes were all active from pH 6.0 to 8.5, with functional stability being lowest around the optimal pH. All three Tmms, given sufficient NADPH cofactor, were found to generate TMAO in the TMA-rich salmon protein hydrolysate. The Tmms serve as unique starting points for engineering and should be useful for guiding process development for marine biorefineries. IMPORTANCE Enzyme-based conversion of marine biomass to high-quality peptide ingredients leaves a distinct smell of "fish" caused by the presence of trimethylamine, which limits their economic potential. We suggest an enzymatic solution for converting trimethylamine to the odorless trimethylamine N -oxide as a novel strategy to improve the smell quality of marine protein hydrolysates. Following a systematic investigation of 45 putative bacterial trimethylamine monooxygenases from several phyla, we expand the repertoire of known active trimethylamine monooxygenases. As a proof-of-concept, we demonstrate that three of these enzymes oxidized trimethylamine in an industry-relevant salmon protein hydrolysate. Our results add new oxidoreductases to the industrial biocatalytic toolbox and provide a new point of departure for enzyme process developments in marine biorefineries. (Copyright © 2020 Goris et al.) |
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| فهرسة مساهمة: | Keywords: enzyme discovery; fish protein hydrolysate; flavin-containing monooxygenases; malodor; oxidoreductases; trimethylamine; trimethylamine N-oxide; trimethylamine monooxygenases |
| المشرفين على المادة: | 0 (Bacterial Proteins) 0 (Methylamines) 0 (Recombinant Proteins) EC 1.13.- (Oxygenases) EC 1.14.13.8 (dimethylaniline monooxygenase (N-oxide forming)) FLD0K1SJ1A (trimethyloxamine) LHH7G8O305 (trimethylamine) |
| تواريخ الأحداث: | Date Created: 20200926 Date Completed: 20201221 Latest Revision: 20201221 |
| رمز التحديث: | 20221213 |
| مُعرف محوري في PubMed: | PMC7688232 |
| DOI: | 10.1128/AEM.02105-20 |
| PMID: | 32978141 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1098-5336 |
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| DOI: | 10.1128/AEM.02105-20 |