CHARACTERIZATION OF Α -AMYLASE FROM MARINE VIBRIO SP. B10.2.8

• Main Author: Pratiwi (NIM: 105 03 025), Margareth
• Format: Final Project
• Language: Indonesia
• Online Access: https://digilib.itb.ac.id/gdl/view/6422
• Institution: Institut Teknologi Bandung

Abstract Amylases are responsible for hydrolysis of D-(1,4) glycosidic linkage in starch to produce oligosacharides. These enzymes have been used widely in many industrial fields, such as starch processing, textile, pharmacy, and detergent. An Indonesian marine isolate identified as Vibrio sp. B10.2.8 produces extracellular amylase. This research was conducted to characterize amylase of Vibrio sp. B10.2.8 which includes growth profile, temperature, and pH and temperature dependent profiles, molecular weight identification, and its ability to hydrolize raw starch. A 225 mL culture supernatant of Vibrio sp. B10.2.8 was precipitated by 70% saturated ammonium sulphate and the resulted ammonium sulphate fraction has a total activity of 2364,12 Units. Amylase of Vibrio sp. B10.2.8 secretion was growth associated with maximum activity occured at late exponential phase. The Vibrio sp. B10.2.8. amylase has optimal pH and temperature of pH 6 and 50 derajat C, respectively. SDS-PAGE (Sodium Dodecyl Sulphate Polyacrylamid Gel Electrophoresis) and zymograph analysis showed that the enzyme have molecular weight of 53,2 kDa. Furthermore, on it was found that amylase Vibrio sp. B10.2.8 can not hydrolize raw starch granule.