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자료유형
학술저널
저자정보
Jarosz-Wilkolazka, Anna (Department of Biochemistry, Maria Curie-Sklodowska University) Luterek, Jolanta (Department of Biochemistry, Maria Curie-Sklodowska University) Malarczyk, Elzbieta (Department of Biochemistry, Maria Curie-Sklodowska University) Leonowicz, Andrzej (Department of Biochemistry, Maria Curie-Sklodowska University) Cho, Hee-Yeon (Dental Research Institute, School of Dentistry, UCLA) Shin, Soo-Jeong (Wood and Paper Science, Chungbuk National University) Cho, Nam-Seok (Wood and Paper Science, Chungbuk National University)
저널정보
한국목재공학회 목재공학(Journal of the Korean Wood Science and Technology) 목재공학 제35권 제2호
발행연도
2007.1
수록면
85 - 95 (11page)

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Manganese dependent peroxidase (MnP) is the most ubiquitous enzyme produced by white-rot fungi, MnP is known to be involved in lignin degradation, biobleaching and oxidation of hazardous organopollutants. Bjerkandera fumosa is a nitrogen-unregulated white-rot fungus, which produces high amounts of MnP in the excess of N-nutrients due to increased biomass yield. The objective of this study was to optimize the MnP production in N-sufficient cultures by varying different physiological factors such as Mn concentration, culture pH, and incubation temperature. The growth of fungus was optimal in pH 4.5 at $30^{\circ}C$, $N_2$-unregulated white-rot fungus produces high amounts of MnP in the excess N-nutrients. The fungus produced the highest level of MnP (up to $1000U/{\ell}$) with $0.25g/{\ell}$ asparagine and $1g/{\ell}$ $NH_4Cl$ as N source at 1.5 mM $MnCl_2$ concentration, pH value of 4.5 at $30^{\circ}C$. Purification of MnP revealed the existence of two isoforms: MnPl and MnP2. The molecular masses of the purified MnPl and MnP2 were in the same range of 42~45 kDa. These isoforms of B. fumosa strictly require Mn to oxidize phenolic substrates. Concerned to kinetic constants of B. fumosa MnPs, B. fumosa has similar Km value and Vmax compared to the other white-rot fungi.

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