Pemurnian dan Karakterisasi Pektinase dari Aspergillus ustus BL5

Abstract

Pectinase, an extracellular enzymes that degrades pectin to galacturonic acid and pectinat acid. Aspergillus has been reported as a fungi that can produce secondary metabolite and extracellular of enzymes such as hemiselulase, selulase and pectinase. Pectinase plays a vital role in processing industries such as in the production of fruit juice, in fermentation tea leaves and used also at paper and textile industry. This study aimed to purify and characterize the extracellular pectinase from Aspergillus ustus BL5. Extracellular pectinase showed optimum activity with 2% substrate concentration and pH 7, in 120 hours of incubation time with 0,6 U/mg specific activity. The crude enzyme was concentrated with PEG-6000 and ultrafiltration. The crude enzyme of pectinase was purified using Sephadex G-75 gel filtration chromatography. The partial purified enzyme has specific activity 4,14 U/mg. The purity had increase 6,94 than crude enzymes. The optimum temperature and pH were 500 C and 5. The Addition of 0.05 mM CuSO4 can increased enzyme activity to 163.87%.