Characterization of cellulase and xylanase from Lentinus polychrous Lev. LP-PT-1

Biotechnology, a knowledge of science and technology is interesting for the scientists around the world. Biotechnological processing uses enzymes and microorganisms to make products in a wide range of industrial sectors. The culture conditions of cellulose and xylanase production by Lentinus polychrous Lev. LP-PT-1, under solid state fermentation (SSF) economical using rice straw as substrate, were investigated. The optimum temperature and pH of enzyme activities and stabilities were examined. Partial purification of enzyme and molecular mass determination were investigated. The xylanase and cellulose production from Lentinus polychrous Lev. LP-PT-1 under solid state fermentation indicated that the optimal temperature of xylanase and cellulose production were found to be at 35 C. The 75% and 80% moisture levels showed significantly higher cellulose production than other treatments (p<0.05). The 75% and 80% moisture levels showed significantly higher xylanase production than 50% and 55% moisture levels (p<0.05). The inoculum level at 0.5 cm per disk for four disks in 4 grams substrate culture was found to be optimum for xylanase and cellulose production. The stability of xylanase and cellulose from L.polychrous Lev. LP-PT-1 was determined. Crude enzymes were extracted by McIIvaine buffer pH 5.0 at 150 rpm for 30 minutes. The relatively good thermostability of xylanase and cellulose was maintained at high temperature at 60 C with 89% and 81% of the remaining activity. The cellulose was stable at pH 4.0-5.0 with 94% remaining activity. The xylanase appeared to be stable over a broad pH range of 4.0-7.0. high cellulose activity was achieved at temperatures between 30 and 60 C. The xylanase activity increased with high temperature to 60C. The optimum pHs for cellulase and xylanase activity were found in the range of pH 4.0-6.0. The partial purification was achieved using 20-40% ammonium sulfate precipitation. The results from SDS polyacrylamide electrophoresis (SDS-PAGE) showed that the partial purified enzyme had 3 subunits with their molecular weight as following 45 kDa, 40 kDa and 35 kDa, respectively. The present findings revealed that the high thermostability of cellulose and xylanase from Lentinus polychrous Lev. LP-PT-1 would be potentially more beneficial in the industrial biotechnological applications.