In the present study we found that the fruiting body of the medicinal and edible mushroom Sparassis crispa produces lignin peroxidase. Lignin peroxidase was measured with two assays: quantitation of the veratraldehyde produced on oxidation of veratryl alcohol. The assay was also used to monitor oxidation of the dye azure B involving absorbance measurements in the visible range. The S. crispa lignin peroxidase was purified using ammonium sulphate precipitation, anion exchange and gel filtration chromatography. The molecular weight of the purified enzyme was approximately 45 kDa, as determined by SDS-PAGE. A zymogram analysis using a pyrogallol substrate revealed that this enzyme is peroxidase. The substrate specificity, optimum pH and temperature of this enzyme were determined. The effect of nutrient nitrogen was also assessed because nitrogen sources are frequently affecting the enzyme production. We summarize the potential application of this fungal lignin peroxidase in chemical industry, coal chemistry and environmental protection, etc. References:1.Horie K, Rakwal R, Hirano M, Shibato J, Nam HW, Kim YS, Kouzuma Y, Agarwal GK, Masuo Y and Yonekura M. Proteomics of Two Cultivated Mushrooms Sparassis crispa and Hericium erinaceum Provides Insight into their Numerous Functional Protein Components and Diversity. Journal of Proteome Research. 2008;7:1819-35.
키워드
Lignin peroxidaseEnzymeSparassis crispa
저자
Gayathri CHANDRASEKARAN [ Dept. of Biochemical and chemical Engineering, Chosun University. ]
Hyun-Jae SHIN [ Dept. of Biochemical and chemical Engineering, Chosun University. ]
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
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간행물
간행물명
한국생물공학회 학술대회
간기
반년간
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1985~2013
십진분류
KDC 476DDC 576
이 권호 내 다른 논문 / 한국생물공학회 학술대회 2011년도 한국생물공학회 춘계학술발표대회