Purification and characterization of two lysozymes from rainbow trout (Salmo gairdneri)

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Abstract
Two different lysozymes, designated I and II, were purified from the kidney of rainbow trout. The enzymes had isoelectric points of approximately 9.5 and 9.65, and differed in their binding characteristics to a cation exchanger. Lysozyme II had the highest specific activity against Micrococcus luteus. By sodium dodecyl sulphate gel electrophoresis, a molecular mass of 14.4 kDa was established for the two lysozymes. For both type I and II enzymes, optimum pH under the present conditions was 5.5 and optimum temperature (at pH 6.2) around 45°C. N‐terminal amino acid sequence determination indicated that the two trout lysozymes were c‐type lysozymes. The fish lysozymes had a much higher rate of diffusion in agar than did the other lysozymes tested (possibly due to less interaction with agarose). This implies that a foreign lysozyme, such as hen egg white lysozyme, should not be used as a standard when assaying lysozyme activity with the lysoplate technique.

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