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KMID : 0903519940370010049
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1994 Volume.37 No. 1 p.49 ~ p.55
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Isolation and Properties of a Protein , RCG - 2 , Having Chitinase , β - 1,3 - Glucanase and Lysozyme Activities from Rice Leaves
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Abstract
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An acidic protein, RCG-2, containing chitinase and β-1,3-glucanase activity conccurrently was purified from rice leaves by chromatofocusing and gel slicing. The purified enzyme gave a single band on polyacrylamide gel electrophoresis and its molecular weight was appeared to be 29.7 kd using SDS-PAGE. This enzyme also had lysozyme activity. The optimal temperature for both enzyme activities was 40℃, optimal pH were 4.0 for chitinase activity and 7.0 for β-1,3-glucanase activity. K_M and V_(max) values for chitinase were 7.86 mM and 0.025 μM/min., and those for β-1,3-glucanase were 5.95 mM and 0.16 μM/min. respectively. TLC analysis of the enzyme hydrolysates of chitooligosaccharides indicated that this enzyme acts as endochitinase.
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