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Purification and characterization of an endo-1,3-β-glucanase from Arthrobacter sp.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Pang, Zhongcun Otaka, Kodo Suzuki, Yasunori |
| Copyright Year | 2004 |
| Abstract | An endo-1,3-β-glucanase from Arthrobacter sp. was purified by ammonium sulfate precipitation, anion-exchange and gel-filtration chromatographies. SDS/PAGE and gel-filtration chromatography suggested a monomer enzyme with molecular mass of 32,500. N-terminal sequence for 10 residues was APGDLLWSDE. Stable and optimum pHs were 5 to 8 and 6.5, respectively. Optimum temperature was 55°C , however, above 50°C its activity was lost rapidly. The Michaelis constant Km for laminaritetraose, laminaripentaose, laminarihexaose, laminariheptaose, and laminarin were 0.12, 0.11, 0.067, 0.066mM, and 0.16mg/ml, respectively. Curdlan and lichenan were also hydrolyzed. The purified enzyme did not give product by digestion with endoglycosidase H (Streptomyces griseus), indicating that the carbohydrate moiety was little consisted in the enzyme protein, if any, with N-linked chain or other type linkage. It was suggested that the enzyme belong to the family 16 of glucosyl hydrolase from the properties as above mentioned. |
| Starting Page | 57 |
| Ending Page | 66 |
| Page Count | 10 |
| File Format | PDF HTM / HTML |
| Volume Number | 4 |
| Alternate Webpage(s) | http://www.jsb.gr.jp/jbm/2004/0402_2.pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
