| Literature DB >> 9546051 |
E E Deane1, J M Whipps, J M Lynch, J F Peberdy.
Abstract
A chitinolytic enzyme was purified from the culture filtrate of T. harzianum (T198) by precipitation with ammonium sulphate followed by affinity binding to swollen chitin and release with 10% (v/v) acetic acid. The molecular weight of the enzyme was calculated to be 28 and 27.5 kD by gel filtration chromatography and SDS-PAGE, respectively. The isoelectric point of the enzyme was 7.4. The pH optimum for activity was 3.5 and maximum activity was obtained at 50 degrees C. The enzyme displayed activity on a wide array of chitin substrates of more than two N-acetylglucosamine units in length. HPLC analysis of hydrolysis products demonstrated that the enzyme was an exochitinase releasing N-acetylglucosamine only.Entities:
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Year: 1998 PMID： 9546051 DOI： 10.1016/s0167-4838(97)00183-0
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002