Partial purification and properties of e
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K. R. Gunaratna; R. Balasubramanian
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Article
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1994
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Springer
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English
โ 295 KB
An extracellular chitinase of Acremonium obclavatum was partially purified. It had an M r of 45 kDa on SDS-PAGE, and was optimally active at pH 3 to 4 and 50ยฐC. Hg and Mn (10 mM) inhibited activity. The chitinase hydrolysed colloidal chitin more rapidly than crude chitin or isolated A. obclavatum ce