Earticle

초록

영어

Ligninolytic enzymes were produced by Pleurotus ostreatus No.42, cultivated in a new kind of bioreactor that has a rotating draft tube with a helical ribbon. Maximum laccase (Lac) production (about 8,200 U/bioreactor) was reached after 3 days of incubation, then production decreased. Production of manganese peroxidase (MnP) in this fermenter reached a maximum level of about 8,400 U/bioreactor after 6 days of incubation. Lignin peroxidase (LiP) was not detected under these growth conditions. These results indicate that the rotary draft tube bioreactor (RTB) is compatible with large scale production of ligninolytic enzymes. MnP produced under these fermentation conditions was purified via a multistep process that included chromatography on Sepharose CL-6B, prep grade Superdex 75, and Mono-Q. This major isoenzyme was confirmed to have an apparent molecular weight of 36,400 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and its isoelectric point (IEF) was determined to be 3.95. N-terminal sequencing of the major isoenzyme from this fermentation was identical to that reported for an MnP3 isoenzyme isolated under different cultivation conditions, including stationary and shaking culture.

목차

ABSTRACT
서론
재료 및 방법
공시균주 및 배양방법
리그닌 분해효소 측정
용존산소 측정
글루코오스 측정
총 단백질 함량
Manganese peroxidase(MnP)의 정제
겔 전기영동 및 등전점
N-말단 아미노산 서열분석
결과 및 고찰
회전식 통풍관 생물 반응기(RTB)를 사용한 느타리균의리그닌 분해효소 생산
Manganese peroxidase 분리 및 정제
겔 전기영동 및 등전점
적요
REFERENCES

저자

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

참고문헌