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- Title
Purification and characterization of lysozyme from purple washington clam Saxidomus purpurata.
- Authors
MIYAUCHI, Kouji; MATSUMIYA, Masahiro; MOCHIZUKI, Atsushi
- Abstract
Lysozyme was purified from purple washington clam Saxidomus purpurata by sequential procedures using Chitopearl Basic BL-01 affinity and TSKgel ODS-120T column chromatographies. Molecular mass of the purified enzyme was estimated to be 12 kDa by SDS-PAGE. Optimum pH of the enzyme was 5.2 toward Micrococcus lysodeikticus cells. The optimum temperature was 50°C. The enzyme was stable in the range of pH 4.8–6.8 and 20–90°C. Further, the N-terminal amino acid sequence of the enzyme showed similarity to lysozymes from invertebrates. However, the specific activity of the enzyme toward M. lysodeikticus cells and p-nitrophenyl penta- N-acetyl- β-chitopentaoside was 143 times and 12 times higher than that of hen egg white lysozyme, respectively.
- Subjects
LYSOZYMES; CLAM fisheries; BIVALVES; INVERTEBRATES; AMINO acids; CHROMATOGRAPHIC analysis; ENZYMES; MICROCOCCUS luteus; CELLS
- Publication
Fisheries Science, 2006, Vol 72, Issue 6, p1300
- ISSN
0919-9268
- Publication type
Article
- DOI
10.1111/j.1444-2906.2006.01289.x