| Autor: | Nyun-Ho Park, Yasuyuki Kawabata, Hyeon-Jin Sun, Shigeki Yoshida, Isao Kusakabe |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
chemistry.chemical_classification
animal structures biology medicine.diagnostic_test Streptomycetaceae Proteolysis technology industry and agriculture food and beverages Bioengineering macromolecular substances General Medicine biology.organism_classification Applied Microbiology and Biotechnology Xylan Streptomyces carbohydrates (lipids) Papain chemistry.chemical_compound Enzyme chemistry Biochemistry medicine Xylanase Actinomycetales Biotechnology |
| Zdroj: | Biotechnology Letters. 24:595-601 |
| ISSN: | 0141-5492 |
| DOI: | 10.1023/a:1015055624662 |
| Popis: | Limited proteolysis of papain on the intact family F/10 β-xylanase (45 kDa) led to the isolation of catalytic domain (32 kDa) and xylan-binding domain (15 kDa). The two truncated protein fragments were purified by gel filtration to homogeneity. The purified catalytic domain was fully active against 4-O-methyl-d-glucurono-d-xylan, and the action mode on xylan was the same as the intact xylanase. However, the removal of xylan-binding domain reduces dramatically the capability of adsorption for xylan. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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