Related Experiment Video
Updated: Mar 21, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Biochemical characterization of thermostable ω-transaminase from Sphaerobacter thermophilus and its application for
Sam Mathew1, Saravanan Prabhu Nadarajan2, Taeowan Chung1
1School of Biotechnology, Yeungnam University, Gyeongsan, Gyeongbuk 712-749, South Korea.
Abstract:
An (S)-ω-transaminase from the thermophilic eubacterium Sphaerobacter thermophilus was expressed and functionally characterized. The enzyme showed good stability at high temperature and in the presence of various substrates. Substrate specificity analysis showed that the enzyme had activity towards a broad range of substrates including amines, β- and γ-amino acids. The purified enzyme showed a specific activity of 3.3U/mg towards rac-β-phenylalanine at 37°C. The applicability of this enzyme as an attractive biocatalyst was demonstrated by synthesizing optically pure β- and γ-amino acids. Among the various beta and gamma amino acids produced via asymmetric synthesis, (S)-4-amino-4-(4-methoxyphenyl)-butanoic acid showed highest analytical yield (82%) with excellent enantiomeric excess (>99%).
More Related Videos
11:51Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
Published on: April 27, 2018
13:30A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Related Concept Videos
Hyperthermophilic Bacteria
Diversity of Archaea IV
Production of Pharmaceuticals
Diversity of Archaea III
Amino Acid Catabolism
Diversity of Archaea I