In this study, Pleurotus ostreatus No.42 was cultured in glucose-peptone-yeast-wheat bran medium using a previously reported novel rotary draft tube bioreactor. Versatile peroxidase (VP), a lignin-degrading enzyme, was isolated from a pellet-type mycelium culture grown in the medium for seven days. The VP was purified by sequentially applying ultra-filtration, DEAESepharose CL-6B column, and Mono Q column. SDS-PAGE analysis revealed the molecular weight of VP to be 36.4 KDa with an isoelectric point of 3.65. The amino acid sequence was confirmed as VTCATGQTT. The purified VP was observed to possess the property of not only oxidizing Mn ions but also decomposing veratryl alcohol, a non-phenolic compound. The catalytic ability of VP is a subject for future research.

• 하효철(대구한의대학교 바이오산업융합학부) | Hyo-Cheol Ha (Department of bio-technology and convergence, Daegu Haany University, 1, Hanui-daero, Gyeongsan 712-715, Korea ABSTRACT:) Corresponding author