Purification and Some Properties of Three cereale ) Chitinases from the Seeds of Rye ( Slecale

Three chitinases, designated RSC-a, -b, and -c, were purified from the seeds of rye (Slecale cereal) using ammooium sulfate precipitation, CM-cellulose column chromatography, gel fi1tration on Sephadex G-75, and S-Sepharose column ehromatography. RSC-a, -b, and -c are basic' proteins having molecular masses of 33kDa, 26kDa, and 26kDa, and iseelectric points Qf 9.7, 10, anq >10, respectiyely. RSC-b and -c were found to be homologous proteins having similar amino acid compositions and N-terrninal sequences. RSC-a contains more Thr, Ser, Glu, Pro, Gly, and Cys than RSC-b and -c and has a different N-terminal sequence from them. They hydrolyze glycolchitin and celloidal chitin, but not cell walls of Mierececeus lysodethticus. These enzymes are stable at pH 4-8 and their optimum pHs toward glycolchitin are 5.