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Journal : Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam

PEMANFAATAN SELULOSA POPOK BAYI SEBAGAI SUBSTRAT UNTUK PRODUKSI ENZIM SELULASE OLEH ISOLAT BAKTERI S-16 DAN S-22 STRAIN LOKAL RIAU Dahlena, Maya; Dahliaty, Andi; Sy, Silvera Devi
Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam Vol 1, No 2 (2014): Wisuda Oktober 2014
Publisher : Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam

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Abstract

The S-16 and S-22 cellulolytic bacteria isolated from Siak River water were used in this study to produce cellulase with disposable diapers as a substrate. Cotton is the main component in the disposable diapers that can be used as a substrate in the production of cellulase. Cellulase is an enzyme that catalyzes the hidrolisis of β-1-4-glycosidic bond of cellulose. Fermentation was carried out for 10, 20, and 30 days by S-16 and S-22. Enzyme activity was determined using Nelson-Somogyi method. The results showed that the highest enzyme activity obtained at 20 days, with S-16 of (2,654 ± 0,53)x 10 U/mL and S-22 of (13,704 ± 4,91)x 10-3 U/mL.
SINTESIS DAN KARAKTERISASI MEMBRAN BIONANOKOMPOSIT SELULOSA BAKTERI-Ag SEBAGAI MEMBRAN ANTIBAKTERI Dwi Cahyaningsih; Andi Dahliaty; Amilia Linggawati
Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam Vol 2, No 1 (2015): Wisuda Februari 2015
Publisher : Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam

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Abstract

Bacterial cellulose is a potential biopolymer that can be used in the medical field as an antibacterial membrane. Antibacterial membrane was synthesized from bacterial cellulose that was composited with silver nanoparticle that has antibacterial activity. Silver nanoparticles were impregnated into bacterial cellulose membrane to produce bacterial cellulose-Ag bionanocomposite membrane. Synthesis of silver nanoparticles was performed using reduction method with various concentrations of AgNO3 as precursor (0.5 mM, 1 mM, 1.5 mM) and sodium citrate as reducing and stabilizing agent. Bacterial cellulose-Ag bionanocomposite membrane was characterized by Scanning Electron Microscopy-Energy Dispersive X-Ray Spectroscopy (SEM-EDX). The results of SEM-EDX characterization showed that bacterial cellulose-Ag bionanocomposite membrane with AgNO3 0.5 mM has smallest size of silver nanoparticles (30-60 nm) and distributed homogeneously in the bacterial cellulose membrane. Antibacterial test against Staphylococcus aureus and Escherichia coli was carried out by the agar diffusion and turbidimetry method. Bacterial cellulose-Ag bionanocomposite membrane did not show antibacterial activity in the agar diffusion method. In turbidimetry method, bacterial cellulose-Ag bionanocomposite membrane with AgNO3 0.5 mM showed antibacterial activity against Staphylococcus aureus and Escherichia coli. It was able to decrease Optical Density of Staphylococcus aureus (26,69%) and Escherichia coli (22,91%) compared to controls.
PEMEKATAN ENZIM SELULASE Penicillium sp. LBKURCC20 DENGAN PENGENDAPAN AMONIUM SULFAT 80% JENUH Masdalena Sinaga; Titania T. Nugroho; Andi Dahliaty
Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam Vol 1, No 2 (2014): Wisuda Oktober 2014
Publisher : Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam

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Abstract

Cellulase enzyme activity of Penicillium sp. LBKURCC20 Isolate of Riau can beincreased by concentrating the enzyme using 80% saturated solid ammonium sulfate(NH 4 ) 2 SO 4 anhydrous. Precipitated enzyme was redissolved by the addition of acetatebuffer solution pH 5.5 to 1/70 times its original volume. Cellulase enzyme activity wasdetermined using substrates CMC and avicel. CMCase and avicelase enzyme activity ofthe crude enzyme was (0.0164 ± 0.0036) U/mL and (0.003 ± 0.0025) U/mL,respectively. CMCase and avicelase enzyme activity after concentration was (0.219 ±0.0579) U/mL and (0.03 ± 0.03) U/mL, respectively. The test results showed that theactivity of concentrated CMCase increased 13.5 times and avicelase enzyme activityincreased 10 times after concentrating.
ISOLASI BAKTERI SELULOLITIK DARI PERAIRAN DUMAI Waidil Anuar; Andi Dahliaty; Christine Jose
Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam Vol 1, No 2 (2014): Wisuda Oktober 2014
Publisher : Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam

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Abstract

Dumai water samples are estimated to contain cellulolytic microorganisms because of farm waste. Samples 930 from Sei Pakning and 931 from Rupat Strait were water samples containing cellulolytic bacteria taken from Dumai. In this study the production of cellulase enzymes from cellulolytic bacteria in samples of 930 and 931 used CMC as a substrate. Cellulase is an enzyme that catalyses the hidrolisis of β-1-4-glycosidic bond of cellulose. All of the isolates produced cellulase and were able to degrade cellulose. The results indicated that 1% substrate gave the highest activity of Cellulase in the 931-4A (Rupat strait) (1.186 ± 0.319) x 10 -3 U/mL, whereas the highest specific enzyme activity of the bacterial isolates was 930-1C (8.438 ± 0.109) x 10 -3 U/mg.
ISOLASI DAN PEMEKATAN ENZIM SELULASE Trichoderma sp. LBKURCC28 MENGGUNAKAN METODE PENGGARAMAN (NH 4 ) 2SO 4 80% SERTA PENENTUAN AKTIVITAS DAN AKTIVITAS SPESIFIK ENZIM Febry Kurniawan; Titania T. Nugroho; Andi Dahliaty
Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam Vol 1, No 2 (2014): Wisuda Oktober 2014
Publisher : Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam

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Abstract

Cellulase enzyme activity can be increased by concentrating the enzyme using saturated ammonium sulfate ((NH4) 2SO4) 80%. Precipitated enzyme was redissolved by the addition of acetate buffer solution pH 5.5 to 1/70 times its original volume. Cellulase enzyme activity was determined using substrates CMC and avicel. The test results showed that the activity of concentrated CMCase increased 75 times and avicelase enzyme activity increased 9 times. Activity and specific activity concentrated CMCasewas 0,4060±0,0845 U/ml and 0,7306±0,1526 U/mg respectively, while activity and specific activity of concentrated avicelase were 0,0129±0,0182 U/ml and 0,0232±0,0328 U/mg respectively.
HUBUNGAN AKTIVITAS ENZIM DAN KONSENTRASI SUBSTRAT PADA POLA DETEKSI SECARA HPLC HASIL TRANSGLIKOSILASI NARINGENIN OLEH ENZIM SELULASE Penicillium sp. LBKURCC27 Puspita Sari; Titania Tjandrawati Nugroho; Andi Dahliaty
Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam Vol 2, No 1 (2015): Wisuda Februari 2015
Publisher : Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam

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Abstract

Transglycosylation of naringenin was carried out by concentrated cellulase enzyme of Penicillium sp. LBKURCC27. Enzymatic transglycosylation of naringenin was successfully carried out by cellulase from Penicillium sp. LBKURCC27, however the reproducibility of the reaction is low, making detection by reverse phase HPLC (High Performance Liquid Chromatography) difficult when the enzyme activity decreases. It is believe that the flavonoid concentration used in the transglycosylation naringenin by cellulase Penicillium sp. LBKURCC27 influences the detection pattern of transglycosylation product of HPLC. The reaction was carried out for 30 hours at 40°C with acetate buffer 0.05 M pH 5.5 and 170 rpm shaking. Carboxymethyl Cellulose (CMC) was used as glycosyl donor. Results of HPLC analysis showed that cellulase Penicillium sp. LBKURCC27 with an activity of (0.670±0.023 U/mL) were not able to convert naringenin to a detectable glycosylated product when the initial substrate concentration was 6 mg/mL. In the 0.6 mg/mL of naringenin concentration, the glycosylation product was formed with 100% of percent convertion.
OPTIMALISASI pH PRODUKSI SELULASE DARI BAKTERI ENDOFITIK Pseudomonas stutzeri LBKURCC53, Pseudomonas stutzeri LBKURCC54, dan Actinobacter antratus LBKURCC60 Rizki Wulandari; Silvera Devi; Andi Dahliaty
Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam Vol 2, No 1 (2015): Wisuda Februari 2015
Publisher : Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam

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Abstract

Cellulase is an enzyme that can hydrolyze the β-1,4 bonds on cellulose and productionof glucose so that the enzyme is widely used in various industries. Cellulose enzymes can be produced by microorganism such as endophytic bacteria (LBKURCC53, LBKURCC54, and LBKURCC60). The activity of cellulase enzyme was determined by measuring the glucose produced using Nelson-Somogyi method. The optimum activity of cellulase enzyme from theisolates of LBKURCC53, LBKURCC54, and LBKURCC60 we measured at different pH. The enzyme of LBKURCC53 isolate was optimum at pH 7 with enzyme activity of 11,31 ± 1,69 x 10 -3 U/mL. While the enzyme of LBKURCC54 and LBKURCC60 isolates were optimum at pH 6,5 with enzyme activity 14,44 ± 2,94 x 10 -3 U/mL and 8,33 ± 1,11 x 10 -3 U/mL respectively. These comparison of cellulase enzyme activity of isolates LBKURCC53, LBKURCC54, and LBKURCC60 were determined by using Duncan multiple range test at 5% level (α≥0,05).
POTENSI LIMBAH KULIT PISANG KEPOK (Musa paradisiaca) SEBAGAI BAHAN BAKU PEMBUATAN ASAM ASETAT MENGGUNAKAN BERBAGAI MACAM STARTER Ilham '; Itnawita '; Andi Dahliaty
Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam Vol 1, No 2 (2014): Wisuda Oktober 2014
Publisher : Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam

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Abstract

Kepok banana  (Musa  paradisiaca)  peel  waste contain sugar that can  be  changed  to acetic acid using Effective Microorganism (EM-4), kombucha (KO), cassava yeast (RT) and instant yeast  (RI)  (commercial  starter). The Commercial  starter  contains variety of bacteria and yeasts  with different content of microorganism  that will influence  the amount of ethanol  produced.  The aim of this study  to  determine the  potential of kepok banana peel  waste used as the main material  in synthesis  of acetic acid using commercial  starter.  Based on the  fermentation  results  using  the four starter,  cassava yeast  has  a  good  ability  to  be  fermented.  The acetic acid formation was  obtained  under condition which substrate and starter amount are 80% w/v and 5 grams respectively and fermentation  time  4  day.  Based on these conditions  it was found that the amount of organic acid total  determined  by  titrimetric  method  is  4.712±0.066%  and  acetic  acid formed which was determined by Ion Chromatography method is 0.7507± 0.0538%.