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Journal : Teknologi%20Indonesia

OPTIMIZATION OF CELLULASE PRODUCTION FROM MARINE BACTERIUM BACILLUS CEREUS C9 BY SUBMERGED FERMENTATION -, Yopi -; Rahmani, Nanik
Teknologi Indonesia Vol 39, No 1 (2016)
Publisher : LIPI Press

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (0.001 KB) | DOI: 10.14203/jti.v39i1.238

Abstract

Cellulase is one of industrial important enzymes in conversion of lignocellulosic biomass into valuable products such as bioethanol produced by fermentation. Successful bioconversion of cellulosic biomass mainly depends on the nature of cellulose sources of cellulolytic enzyme and optimal conditions for production of enzymes. An extracellular cellulase production by marine bacterium Bacillus cereus C9 was optimized by using submerged fermentation (SMF) on commercial substrate (CMC). The fermentation condition such as substrate concentration, pH medium, temperature fermentation, and carbon source were optimized. The optimum condition found for cellulase production were substrate concentration 2.0% (b/v), pH medium 5, temperature fermentation 30C, and glucose as a carbon source with activity 4.42 U ml-1on 96 hours of fermentation.
PURIFICATION AND PROPERTIES OF MANNANASE FROM Aspergillus ustus BL5 Thontowi, Ahmad; Rahmani, Nanik; Andriani, Ade; Yopi, -
Teknologi Indonesia Vol 37, No 1 (2014)
Publisher : LIPI Press

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (16.051 KB) | DOI: 10.14203/jti.v37i1.214

Abstract

Strain of BL5 was reported as a mannanase producer. The purposes of this study are identification, purification and characterization of mannanase from BL5. The Internal Transcribed Spacer (ITS) regions analysis showed that BL5 strain have 93% similarity with Aspergillus ustus isolate UOA/HCPF 9236. An extracellular mannanase from the culture supernatant of a fungus A. ustus BL5 was purified. SDS-PAGE of the purified enzyme showed a single protein band of molecular mass 50 to 51 kDa. The mannanase exhibited optimum catalytic activity at pH 7.0 and 55C. The metal ions Ca2+, Cu2+ and SDS inhibited complete enzyme activity. The metal ion Mg2+ and EDTA increased complete enzyme activity. The value of Vmax = 5,88 ?mol mannose/min/ml and Kmax = 0.64 mg/ml. Mannanase of A. ustus BL5 be able to hydrolyzed porang mannan.
PECTINASE PRODUCTION BY ASPERGILLUS USTUS BL5 AT SOLID STATE FERMENTATION MEDIUM USING AGRICULTURAL BIOMASS Rahmani, Nanik; Andriani, Ade; Anggraini, Yufi Sara; Yopi, -
Teknologi Indonesia Vol 36, No 3 (2013)
Publisher : LIPI Press

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (16.051 KB) | DOI: 10.14203/jti.v36i3.210

Abstract

This research showed that Indonesian agricultural biomasses, such as Siam orange peel, Medan orange peel, Durian peel and old tea leaves contain a pectin that are a potential material for use as a substrate for pectinase production. From the four types of biomasses used, Medan orange peel produced pectinase activity with the highest value equal to 1.28 U/mL. Optimization of fermentation conditions showed that Aspergillus ustus BL5 pectinase production were affected by the concentration of substrate, media pH, and temperature of the fermentation. Optimization of process showed that the optimum substrate concentration, pH and temperatuter were 10%, 4 and 40C with pectinase activity of 1.37 U/mL, 2.85 U/mL, and 1.92 U/mL respectively. Pectin content in the medium has a proportional relationship with the activity of the enzyme pectinase produced. The high content of pectin in Medanorange peel making pectinase enzyme activity produced on the substrate is also high.
ENZYMATIC HYDROLYSIS OF THE FEC 25 AND ROTI CASSAVA STARCH (Manihot esculenta) VARIETIES BY α-AMYLASE FROM A MARINE BACTERIUM (BREVIBACTERIUM SP.) rahmani, nanik; Andriani, Ade; Hartati, Sri; Yopi, Yopi
Teknologi Indonesia Vol 39, No 3 (2016)
Publisher : LIPI Press

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/jti.v39i3.295

Abstract

Cassava (Manihot esculenta) is one of the food sources that is familiar for Indonesian society. Carbohydrates of cassava can be enzymatically hydrolyzed into small oligosaccharides that can be used as a material for functional food components production. Starch from the FEC 25 and roti cassava starch have been hydrolyzed by α-amylase from marine bacterium, Brevibacterium sp. for maltooligosaccharides production. The best hydrolysis reaction condition of the FEC 25 cassava starch were starch concentration of 6.0% (w/v), the ratio of α-amylase and starch 1:1, 50 mM of sodium phosphate buffer pH 6.6, the reaction temperature at room temperature (30oC) and the reaction time of 8 hours with the highest reducing sugar value of 21.675 ppm. While the best hydrolysis of the Roti cassava starch were starch concentration of 6% (w/v), the ratio of α-amylase and starch 1:1, 50 mM of sodium phosphate buffer pH 6.6 and the reaction temperature at 50oC, the reaction time of 8 hours with the highest reducing sugar value of 13.278 ppm. The results of maltooligosaccharides analysis using thin layer chromatography (TLC) showed that the type of maltooligosaccharides formed on hydrolysis the FEC 25 cassava starch are glucose, maltose and maltotriosa, while Roti cassava starch are glucose, maltose, maltotriose, and maltopentaose. The formation of maltooligosaccharides showed that both of cassava starch can be hydrolyzed by α-amylase from marine bacterium Brevibacterium sp.