| Autor: |
Kubačková, M., Karácsonyi, S., Bilisics, L., Toman, R. |
| Zdroj: |
Folia Microbiologica; May1978, Vol. 23 Issue 3, p202-209, 8p |
| Abstrakt: |
Some properties of purified endo-l,4-β- D-xylanase (1,4-β-D-xylan xylanohydrolase, EC 3.2.1.8) from the ligniperdous fungus Trametes hirsuta were investigated. The enzyme was stable between pH 4.0 and 8.0 with optimum activity at pH 5.0-5.5. The temperature optimum was 50 °C and the enzyme was stable for up to 30 min at 45 °C; however, it was denatured at higher temperatures. The K for 4-O-methylgluourono-D-xylan was 6.36. 10 equivalents of D-xylose per litre, the activation energy was 28 kJ mol. The molecular weight determined by means of gel chromatography was 22000-24000. The enzyme was activated by Ca and inhibited by Ag and Hg. On the basis of the effect of 2-hy-droxy-5 nitrobenzyl bromide, N-bromosuccimmide and N-aeetyhmidazole it may be assumed that trytophan and possibly tyrosine residues influence the enzyme catalysis. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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