| Title | Purification and characterization of a xylanase from alkalophilic cephalosporium sp. RYM-202 |
|---|---|
| Author | Kang, Myoung Kyu · Kwon, Tae Ik¹ · Yang, Young Ki² · Rhee, Young Ha * |
| Address | Department of Microbiology Chungnam National University, Taejon 305-764; ¹Department of Biochemisty Chungnam National University, Taejon 305-764; ³Department of Genetic Engineering, Chosun University, Kwangju 501-759, Korea |
| Bibliography | Journal of Microbiology, 33(2),109-114, 1995, |
| DOI | |
| Key Words | alkaline xylanase, alkalophilic Cephalosporium sp., enzyme purification, characterization |
| Abstract | Alkalophilic Cephalosporium sp. RYM-202 produced multiple xylanases extracellularly. One of these xylanases was purified to electrophoretical homogeneity by chromatography with DEAE-Sephadex A-50, Sephacryl S-200 HR and Superose 12 HR. The purified xylanase differed from most other microbial xylanases in that it had low-molecular weight and acidic isoelectric point. The molecular weight of the xylanase in that it had low-molecular weight and acidic isoelectric point. The molecular weight of the xylanase was 23 kDa by SDS-polyacrylamide electrophoresis and 24 kDa by gel permeation chromatography, and the isoelectric point was 4.3. The xylanase had the highest activity permentation chromatography, and the isoelectric point was 4.3. The xylanase had the highest activity permeation chromatography, and the isoelectric point was 4.3. The xylanase had the highest activity at pH 8.0 and 50℃. It was stable over a wide range of pH and retained more than 80% of its original activity after 24 h of incubation even at pH 12. The Km values of this enzyme on birchwood xylan and oat spelts xylan were 2.33 and 3.45 mg/ml, respectively. The complete inhibition of the enzyme of n-bromosuccinimide suggests the involvement of tryptophan in the active site. The sylanase lacked activity towards crystalline cellulose and carboxymethyl cellulose. |
| Download PDF | Eng_330203_109-114p.pdf |