Recovery of lysozyme from scallop waste.
A crude lysozyme preparation was recovered in waste from the scallop processing industry. Lysozyme was then purified 229-fold in preparative scale by chromatography on S Sepharose and Blue Sepharose. Further purification on Sephacryl S-200 resulted in a lysozyme preparation with a specific activity of 64,000 units/mg protein. The apparent molecular mass of the partially purified lysozyme was 10 kDa as judged by gel filtration. Optimum pH for lysis of Micrococus luteus under the present conditions was 5.2. The enzyme was very active at low temperatures. At 4 degrees C the scallop viscera lysozyme exhibits about 55% of the activity measured at 37 degrees C.
Myrnes
B
B
Norwegian Institute of Fisheries and Aquaculture, Centre of Marine Biotechnology, Tromsø.
Johansen
A
A
D000818:Animals; D002850:Chromatography, Gel / Q000379:methods*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007220:Industrial Waste / Q000032:analysis; D008974:Mollusca / Q000201:enzymology; D009113:Muramidase / Q000302:isolation & purification* / Q000378:metabolism; D012758:Shellfish; D013696:Temperature
D007220:Industrial Waste; D009113:Muramidase