A putative Old Yellow Enzyme (OYE) homologue, Chr-OYE3, was identified from the genome of Chryseobacterium sp. CA49 as a new member of the "thermophilic-like" OYE subfamily. Chr-OYE3 is most closely related to YqjM from Bacillus subtilis with 51% identity. The heterologously expressed enzyme adopted two oligomeric states in solutions, dimers and tetramers.

It can reduce a spectrum of activated alkenes, and displayed increased thermal resistance with half-lives of thermal inactivation (t(1/2)) of 233.5 and 21.8 h at 35 degrees C and 55 degrees C, respectively. The enzyme also exhibited high resistance toward various organic solvents, especially water-miscible solvents with higher polarity, such as ethylene glycol and DMSO, which would facilitate its application in biocatalysis where such reaction conditions are often encountered.

This research has been published on JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, which was conducted by Prof.WU Zhongliu from Chengdu Institute of Biology.