회전식 통풍관 생물반응기로부터 생산된 느타리균의 다목적 과산화효소(VP) 정제 및 특성
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....
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| Published in | Journal of mushrooms Vol. 21; no. 4; pp. 209 - 214 |
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| Main Author | |
| Format | Journal Article |
| Language | Korean |
| Published |
한국버섯학회
31.12.2023
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| Subjects | |
| Online Access | Get full text |
| ISSN | 1738-0294 2288-8853 |
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| Abstract | 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. |
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| AbstractList | 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. 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, DEAE-Sepharose 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. 본 연구에서 Pleurotus ostreatus No.42는 이전에 보고된 새로운 유형의 회전식 통풍관 생물반응기(RTB)를 사용하여 포도당-펩톤-효모-밀기울(GPYW) 배지에서 배양하였다. 이 배지에서 7일 동안 펠렛형 균사체 배양 후, 리그닌 분해효소인 다목적 과산화 효소(VP)를 분리 및 정제하였다. 다목적 과산화 효소의 정제 과정은 한외여과, DEAE-Sepharose CL-6B 컬럼, Mono Q 컬럼을 순차적으로 적용하여 정제하였다. 그 결과, SDS-PAGE상에서 분자량(MW)은 36.4 KDa, 등전점 (IEF)은 3.65로 나타났으며, 아미노산 조성은 VTCATGQTT로 확인되었다. 정제된 다목적 과산화 효소는 Mn 이온을 산화시킬 뿐만 아니라 비페놀성 화합물인 베라트릴 알코올을 분해하는 특성을 갖는 것으로 나타났다. |
| Author | 하효철 |
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| Keywords | Amino acid sequence Pellet Pleurotus ostreatus Versatile peroxidase Lignin degrading enzyme |
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| TableOfContents | 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 서 론 재료 및 방법 결과 및 고찰 적 요 REFERENCES |
| Title | 회전식 통풍관 생물반응기로부터 생산된 느타리균의 다목적 과산화효소(VP) 정제 및 특성 |
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