Earticle

초록

영어

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.

목차

ABSTRACT
서론
재료 및 방법
공시균주 및 배양방법
다목적 과산화 효소 측정
총 단백질 함량
Vesatile peroxidase(VP)의 분리 및 정제
겔 전기영동 및 등전점
N-말단 아미노산 서열분석
결과 및 고찰
회전식 통풍관 생물 반응기(RTB)를 사용한 느타리균의 다목적 과산화 효소(VP) 분리 정제
겔 전기영동 및 등전점
느타리 속 균주가 생산하는 다목적 과산화 효소(VP)의기질 산화비교
적요
REFERENCES

저자

• 하효철 [ Hyo-Cheol Ha | 대구한의대학교 바이오산업융합학부 ] Corresponding Author

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