ACCELERATING CHEESE RIPENINC WITH BACTERIAL PROTEINASES

Abstract

I- P otease enzymes of B. subtilis and P. fluorestens were rodhced, purified and c aract±.erized. Based on our results the allowing conclusions can be drawn: 1- 'Iilhe specific activityfor B. subtilis and P. fluorescens proteases in the cultureslpermeate was 3.58 and2.45 :units/mg. When the culture permea.tes were concentrated us:i!ng 10 Kd Millipore membrane, the ispecffic activity was increased to I 9.13 and 6.30 unlts/mg, respec'tlvely. The recovery·was about 88 % f6r the two strainsl . : 2- ,urification of the to pr teases resulted in 1i-fold and 16-flold with specific a1tivitt: of 60.91 and 40.50 iunits/mg, for B. subtilis and P. Iluorescens proteases, respectively. The recovery was about 2'9 % for the two strains. 3- Both proteases were heat-stable. They retained 7:5 %and 80 % I their original . y after heat-treated at 2.5°C for ofi actlvlt 30 mI in. 4- fptim<>l temperature yas 37°C at pH around 7.5 hen using casein as a substrate fdr both proteases.