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Biotechnology and Applied Biochemistry (2003) 37, (9–14) (Printed in Great Britain)

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Purification of lysozyme from other hen's-egg-white proteins using metal-affinity precipitation

Ipsita Roy, Mukkavilli V. S. Rao and Munishwar N. Gupta¹

Chemistry Department, Indian Institute of Technology, Delhi, Hauz Khas, New Delhi 110016, India

Key words: metal affinity of proteins, protein precipitation.

Abbreviations used: IMAC, immobilized-metal-affinity chromatography; STI, soya bean trypsin inhibitor.

¹To whom correspondence should be addressed (e-mail mn_gupta@hotmail.com).

It was found that the presence of 5 mM Cu²⁺ caused precipitation of protein present in hen's egg white to a large extent. About 85% of lysozyme activity remained in the supernatant and the enzyme was purified by approx. 13-fold. A further gel-filtration step on Sephadex G-75 resulted in an overall yield of 80% for the enzyme with 655-fold purification, and showed a single band on SDS/PAGE.

Received 24 May 2002/28 August 2002; accepted 30 September 2002

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