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PURIFIKASI DAN KARAKTERISASI ENZIM PEKTINASE DARI ASPERGILLUS USTUS BL5 Yopi, Yopi; Rahmani, Nanik; Andriani, Ade; Dewi, Fitria; Meryandini, Anja
BERITA BIOLOGI Vol 12, No 3 (2013)
Publisher : Research Center for Biology-Indonesian Institute of Sciences

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/beritabiologi.v12i3.646

Abstract

Pectinase is an enzyme that could hydrolyze pectin into galacturonic acid. Natural pectinase was produced by microbes such as bacteria, yeast, fungi and Actinomycetes. Application of pectinase in industry were mainly in juice industry, textile, pulp, tea, cocoa and coffee fermentation. In this research, we conducted purification and characterization of pectinase produced by Aspergillus ustus BL5 in submerged fermentation using commercial pectin. The result showed that the optimum of pectinase production was reached at 120 hours fermentation process with specific activity 0.59 U/mg. The crude extract of pectinase was then concentrated using PEG 6000 and purified by Sephadex G-75 gel filtration chromatography. There were 2 fractions contained pectinase which the activity was 4.15 U/mg (pectinase A) and 3.3 U/mg (pectinase B), respectively. Compare to crude extract, the yield product of pectinase A and B increased 6.94 and 5.53 times, respectively. The purified pectinase A have optimum temperature at 50 oC and optimun pH at 5.
SELEKSI DAN IDENTIFIKASI BAKTERI ENDOFIT POTENSIAL PENGHASIL ENZIM PROTEASE DARI TAMAN NASIONAL GUNUNG HALIMUN - (The Selection and Identification of Potential Endophyte Bacteria as Protease Enzyme Producer from Halimun Mount National Park) Melliawati, Ruth; Rohmattusolihat, Rohmattusolihat; Nuryati, Nuryati; Rahmani, Nanik; Yopi, Yopi
Biopropal Industri Vol 7, No 2 (2016)
Publisher : Balai Riset dan Standardisasi Industri Pontianak

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (416.906 KB)

Abstract

Endophytic bacteria have an equal chance to bacteria that live outside the plant tissue as potential bacteria. The selection has done towards 326 bacterial endophyte isolates. This research aimed to find and identify proteolytic potential isolates. The proteolytic selection of endophytic bacteria had done using solid skim milk. The capability of endophytic bacteria to agglomerate milk was tested using liquid skim milk which incubated for 7 days at room temperature. Enzyme production of four selected isolates was made through fermentation in GYS medium. The results showed that 86 isolates have proteolytic potential. Isolate HL.29B.63 had highest protease enzymes activity (65.918 U/mL). Medium optimization was able to increase the enzyme activity into 89.94% (125.04 U/mL). The analysis used 16s rDNA showed that isolate HL.29B.63 was Bacillus amyloliquefacient subs. plantarum strain FZB42.Keywords: endophytic bacteria, fermentation, identification, protease, selection ABSTRAKBakteri endofit mempunyai peluang yang sama dengan bakteri yang hidup diluar jaringan tanaman sebagai bakteri potensial. Seleksi dilakukan terhadap 326 isolat bakteri endofit. Tujuan penelitian ini adalah mencari isolat yang berpotensi proteolitik dan mengidentifikasinya. Seleksi proteolitik terhadap bakteri endofitik menggunakan skim milk padat. Uji kemampuan bakteri endofitik dalam menggumpalkan susu menggunakan medium skim milk cair yang diinkubasi selama 7 hari pada suhu ruang. Produksi enzim terhadap empat isolat terseleksi dilakukan melalui fermentasi dalam medium GYS. Hasilnya menunjukkan bahwa 86 isolat mempunyai potensi proteolitik. Isolat HL.29B.63 mempunyai aktif enzim protease tertinggi (65,918 U/mL). Optimasi medium dapat meningkatkan aktivitas enzim sebesar 89,94% (125,04 U/mL). Analisis menggunakan 16s rDNA menunjukkan bahwa isolat HL.29B.63 adalah Bacillus amyloliquefaciens subs. plantarum strain FZB42.Kata kunci: bakteri endofit, fermentasi, identifikasi, protease, seleksi
Isolats Bakteri Indigenous Penghasil Milk-Clotting Protease untuk Fermentasi Keju Rahmani, Nanik; Sari, Yana Nurita; Palupi, Nurheni Sri; Yopi, Yopi
JURNAL BIOLOGI INDONESIA Vol 9, No 2 (2013): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (316.729 KB) | DOI: 10.14203/jbi.v9i2.166

Abstract

The aims of this research is to isolation of bacteria that potential to produce of milk clotting protease enzymes fromfermented food that will be used as a substitute for rennet in cheese making. There are five food fermentations suchas tauco, tempeh, red oncom, sticky tape, and pickled mustard greens that are used as a source for isolation of bacteriathat could produce milk clotting protease. The results obtained four isolates proteolytic bacteria from two fermentedfood samples, three isolates bacteria from tauco (TCN 1, TCN 2, TCN 3) and one isolate from pickledmustard greens (DSN 1). Based on 16S rDNA, these isolates were identified as Bacillus sp. Bacterial isolate TCN 1has a milk clotting activity of 29.17 U/mL, whereas bacteria isolates of TCN 2, TCN 3 and DSN 1 have activities of70 U/mL achieved at the 24 hours incubation, respectively. The proteolytic activities of bacteria isolates TCN 1,TCN 2, TCN 3 and DSN 1 at the 24 hours fermentation process were 0.0117 U/mL, 0.0021 U/mL, 0.0150 U/mL,and 0.200 U/mL, respectively. The ratio of milk clotting protease activity and the proteolytic activity for bacteriaisolates TCN 1, TCN 2, TCN 3 and DSN respectively were 5402, 175000, 7292, and 3333. This showed that theenzyme from bacterial isolates TCN 2 can be used as an alternative to rennin in cheese making.Keywords: milk clotting protease, cheese, calf rennet, fermentation food
Pemurnian Parsial dan Karakterisasi Amilase dari Bakteri Laut Arthrobacter arilaitensis LBF-003 Rahmasari, Dianti; Wijanarka, Wijanarka; Pujiyanto, Sri; Rahmani, Nanik; Yopi, Yopi
JURNAL BIOLOGI INDONESIA Vol 12, No 1 (2016): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/jbi.v12i1.2323

Abstract

Starch is an abundant carbon source in nature, and ?-amylase (1, 4-?-D-glucanohydrolase; EC 3.2.1.1), which hydrolyzes ?-1, 4-glucosidic linkage in starch-related molecules. Microbe ?-amylase production is a hydrolytic enzyme and one ofinterest in its microbial production has increased dramatically due to its wide spread use in food, textile, baking anddetergent industries in recent years. Here we report ?-amylase from marine bacterium which was purified andcharacterized, as well as analyzed its hydrolysis product on starch. The enzyme of Arthrobacter arilaitensis partiallypurified by acetone precipitation with 90% and ion exchange chromatography produced specific activity 0.25 U/mg and0.38 U/mg, and it’s purity rate increased until 1.14 fold compared with former crude extract. Purifed extracelluler amilasehad an optimum activity at temperature 50°C and pH 9.0. An apparent molecular mass was between 50-75 kDa, asestimated by zimogram electrophoresis. Hydrolysis products of this enzyme on starch were maltose, maltotriose andmaltoheptaose.Keywords: alfa amylase, marine bacterium, Arthrobacter arilaitensis, purification, charaterization
Polyaromatic Hydrocarbon Degradation and Dioxygenase Gene Detection from Alteromonas alvinellae Bt05 Thontowi, Ahmad; Rahmani, Nanik; Yopi, Yopi
ANNALES BOGORIENSES Vol 17, No 1 (2013): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.1234/75

Abstract

Bt05 is marine bacterium which was isolated from the Jakarta Bay, Indonesia. The aim of this study was to characterize PAHs-degrading property, molecular identification by partial analysis of 16S rRNA gene and to partially analyze dioxygenase gene of Bt05 isolate. Our further study on this isolate revealed that it could degrade three PAHs (phenanthrene, dibenzothiophene, fluorene) between 60%–90% within 11 days at 100 ppm level. This finding indicated the potential of the isolate for bioremediation of PAHs. The isolate was identified as Alteromonas alvinellae by phylogenetic analysis of 16S rRNA gene sequence. Sequence analysis of the PCR product of PAH dioxygenase genes amplified using two primer set (iiDA and ppAH) of the isolate were identified 97% as naphthalene dioxygenase gene (phaAc) and 58% as 1,2-dioxygenase.
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.
ISOLATS BAKTERI INDIGENOUS PENGHASIL MILK-CLOTTING PROTEASE UNTUK FERMENTASI KEJU Rahmani, Nanik; Sari, Yana Nurita; Palupi, Nurheni Sri; Yopi, Yopi
JURNAL BIOLOGI INDONESIA Vol 9, No 2 (2013): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/jbi.v9i2.166

Abstract

The aims of this research is to isolation of bacteria that potential to produce of milk clotting protease enzymes fromfermented food that will be used as a substitute for rennet in cheese making. There are five food fermentations suchas tauco, tempeh, red oncom, sticky tape, and pickled mustard greens that are used as a source for isolation of bacteriathat could produce milk clotting protease. The results obtained four isolates proteolytic bacteria from two fermentedfood samples, three isolates bacteria from tauco (TCN 1, TCN 2, TCN 3) and one isolate from pickledmustard greens (DSN 1). Based on 16S rDNA, these isolates were identified as Bacillus sp. Bacterial isolate TCN 1has a milk clotting activity of 29.17 U/mL, whereas bacteria isolates of TCN 2, TCN 3 and DSN 1 have activities of70 U/mL achieved at the 24 hours incubation, respectively. The proteolytic activities of bacteria isolates TCN 1,TCN 2, TCN 3 and DSN 1 at the 24 hours fermentation process were 0.0117 U/mL, 0.0021 U/mL, 0.0150 U/mL,and 0.200 U/mL, respectively. The ratio of milk clotting protease activity and the proteolytic activity for bacteriaisolates TCN 1, TCN 2, TCN 3 and DSN respectively were 5402, 175000, 7292, and 3333. This showed that theenzyme from bacterial isolates TCN 2 can be used as an alternative to rennin in cheese making.Keywords: milk clotting protease, cheese, calf rennet, fermentation food