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Soeka, Yati Sodaryati
Research Center for Biology-Indonesian Institute of Sciences
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology

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KARAKTERISASI BAKTERI PENGHASIL a-AMILASE DAN IDENTIFIKASI ISOLAT C2 YANG DIISOLASI DARI TERASI CURAH SAMARINDA, KALMANTAN TIMUR [Characterization bacteria Producing a- amylase and Identification of Strains C2 Isolated from bulk shrimp-paste in Samarinda, East Kalimantan] Soeka, Yati Sodaryati
BERITA BIOLOGI Vol 15, No 2 (2016)
Publisher : Research Center for Biology-Indonesian Institute of Sciences

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (3537.778 KB) | DOI: 10.14203/beritabiologi.v15i2.2290

Abstract

Enzymes a-amylase is one of the enzymes used in process of starch degradation. This present study was aimed to characterize and identify of a-amylase producing strain isolated from bulk shrimp-paste in Samarinda, East Kalimantan was carried out. An experiment was conducted to examine influences of incubation, carbon source, substrate concentration temperature for incubation, pH of media, and addition of metal ions. Identification of strain C2 was carried out by using Wizard Genomic DNA Purification Kit (Promega). The result showed that optimum activity of a-amylase from C2 after six days incubation was 18.93 U/mL. Tests on the type of substrate , soluble starch was the best source to produce a- amylase (14.51 U/mL). However, at concentration of 2 % and incubation temperature at 40°C, enzymatic activity was decreased to 12.56 U/mL and 12.79 U/mL, respectively within residual activity of 74.75%. The enzyme activity was 16.43 U/mL and its residual activity was 39.14 % when it was assayed at pH 8.5. Addition of metal ions in the form of divalent and monovalent cations (1 mM) showed that the enzyme could be activated by ion Ca2+ while ion Cu2+, Co2+, Mg2+, Zn2+ , Na+  decrease the activity of the enzyme. Identification of strain C2 using molecular characterization demonstrated that partial sequences of 16S rDNA reffered to as Bacillus subtilis.
KARAKTERISASI ENZIM PROTEASE DARI BAKTERI Stenotrophomonas sp. ASAL GUNUNG BROMO, JAWA TIMUR [Characterization of Protease Enzymes of Stenotrophomonas sp. bacteria from Bromo Mountain, East Java] Soeka, Yati Sodaryati; Sulistiani, Sulistiani
BERITA BIOLOGI Vol 16, No 2 (2017)
Publisher : Research Center for Biology-Indonesian Institute of Sciences

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/beritabiologi.v16i2.2940

Abstract

Protease is an enzyme that can hydrolyze protein into simpler compounds, i.e peptides and amino acids. Microbial Proteases have the  potency to be applied in industries such as detergents, skins, silver recovery, dairy, baking, beverages and pharmaceutical industries. These hydrolytic enzyme are efficiently involved in the food industry to increase the nutritional value, digestibility, palatability, flavour and reducing allergenic compounds as well as in the management of domestic and industrial wastes. The purpose of this study was to investigate the ability of Stenotrophomonas sp. isolated from Mount Bromo, East Java in producing protease. Protease activity of the bacterial isolate was qualitatively determined by formation of a clear zone surrounded their colonies on media containing skim milk (1%). We analyzed its  proteolic activity against some effects of the incubation period, pH, temperatures and addition of monovalent and divalent metal ionsquantitatively using a spectrophotometer at ? 280 nm.The results showed that the optimum activity after incubation for two days was 315.88 U/ mL. The enzyme has continued to its activity at pH 8 (419.68 U/mL) and maintained its stability at 398.22 U/mL with activities decreased to 94.87%, while its activity at 60°C was 519.86 U/mL and could maintain its stability at 419.58 U/ mL, the activity decreased to 74.75%. The addition of Ca2+ could activated its enzyme activity at the amount of 424.33U/mL, while without addition of the ion its activity was 400.29 U/mL. The addition with ion Mn²+, K+, Na+ and Cu 2+ could act as inhibitors that might reduced the activity of the enzyme.  
Co-Authors Sulistiani Sulistiani, Sulistiani