PRODUCTION OF AN EXTRACELLULAR PROTEASE BY ACETOBACTER ACETIDEENA MENDEZ, A.V.M. KUTTY1 AND S.R. PRASAD
An extracellular protease was identified and partially purified from Acetobacter aceti MTCC 3246. The protease production by this organism was monitored 24 hourly for a period of five days using casein as substrate. Maximum production of proteolytic activity was observed on the fourth day (66Units/mL/min) in comparison to day one (06Unit / mL/min). The protease produced by this organism was further tested for substrate specificity, temperature and pH stability studies. The analysis of the results indicated that the protease could hydrolyze N-Acetyl L-tyrosine ethyl ester but had no detectable activity on Succinyl tri-LAlanyl p-nitroanilide and L-N-BenzoylDZ arginine p-nitroanilide. The data showed that the extracellular enzyme produced by this strain of Acetobacter could belong to chymotrypsin like serine protease. The pH and thermal stability studies indicated that the enzyme was stable over a wide range of pH (3.0 to 8.0) and exhibited maximal activity at 37oC .The enzyme was stable in the temperature range of 280C to 45oC and lost its activity above 60oC significantly.
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