Increased Thermostability of an Engineered Flavin-Containing Monooxygenase to Remediate Trimethylamine in Fish Protein Hydrolysates-Reference-Cited by-同舟云学术

Increased Thermostability of an Engineered Flavin-Containing Monooxygenase to Remediate Trimethylamine in Fish Protein Hydrolysates

Published:2023-06-28 Issue:6 Volume:89 Page:
ISSN:0099-2240
Container-title:Applied and Environmental Microbiology
language:en
Short-container-title:Appl Environ Microbiol

Author:

Goris Marianne¹^ORCID,Cea-Rama Isabel²,Puntervoll Pål¹^ORCID,Ree Rasmus¹,Almendral David³,Sanz-Aparicio Julia²,Ferrer Manuel³^ORCID,Bjerga Gro Elin Kjæreng¹^ORCID

Affiliation:

1. NORCE Climate & Environment - NORCE Norwegian Research Centre, Bergen, Norway

2. Instituto de Quimica Fisica Rocasolano (IQFR), CSIC, Madrid, Spain

3. Instituto de Catalisis y Petroleoquimica (ICP), CSIC, Madrid, Spain

Abstract

Marine by-products are a high-quality source for peptide ingredients, but the unpleasant fishy odor caused by TMA limits their access to the food market. This problem can be mitigated by enzymatic conversion of TMA into the odorless TMAO.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Link

https://journals.asm.org/doi/pdf/10.1128/aem.00390-23

Reference33 articles.

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4. Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase

5. A novel flavin-containing monooxygenase from Methylophaga sp. strain SK1 and its indigo synthesis in Escherichia coli

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