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All Journal Jurnal Pilar Sains Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam Jurnal Online Mahasiswa (JOM) Bidang Perikanan dan Ilmu Kelautan Jurnal Online Mahasiswa (JOM) Bidang Teknik dan Sains Jurnal Inovasi Pendidikan dan Sains Unri Conference Series: Community Engagement
Andi Dahliaty
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Agriculture, Biological Sciences & Forestry Humanities Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Earth & Planetary Sciences Education Engineering Materials Science & Nanotechnology Mathematics Physics

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Modifikasi Amilosa dari Pati Tapioka dan Garut Menjadi Amilosa Asetat Erna, Maria; Eryanti, Yum; Dahliaty, Andi
Jurnal Pilar Sains Vol 7, No 1 (2008)
Publisher : Jurnal Pilar Sains

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It has been done modification of amylose from starch tapioca and garut and then it has been changed to beamylose acetate which is degradable biopolymer. Amylose was separated from starch by method of butanolas complexing on high temperature and pressure. The yielded amylose was then acetylated by anhydrideacetate acid in glacial acetate acid solution with catalyst of concentrated sulfuric acid. Characterization wascarried out based on spectrometry of Fourier Transform Infrared Spectroscopy (FTIR). The result of amilosaspectrum showed that peak of group -OH was on 3437.25 cm and amilosa acetate spectrum had peak on1749.91 cm and it proved that acetyl reaction occurred. In this research, modification of starch tapioca wassuccessful but starch garut unsuccessful.Key words : amylose, acetate amylose.
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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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.
Produksi Enzim Lakase Oleh Jamur Trichoderma Asperellum Lbkurcci Dengan Variasi Penambahan CuSO4 Menggunakan Bioreaktor Tray Secara Solid State Fermentation (SSF) Nurliati, Ivanna; Helianty, Sri; Dahliaty, Andi
Jurnal Online Mahasiswa (JOM) Bidang Teknik dan Sains Vol 5 (2018): Edisi 2 Juli s/d Desember 2018
Publisher : Jurnal Online Mahasiswa (JOM) Bidang Teknik dan Sains

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Laccase is one of the ligninolityc enzymes that capable to degrade lignin. This ability can be used for the pretreatment of lignocellulosic materials in the bioethanol production and lignin degradation in pulp. There are diverse sources of laccase producing like fungi, plants and bacteria. This research is, conducted to the production of laccase enzyme using Trichoderma asperellum LBKURCC1 with bioreactor tray using solid state fermentation (SSF) method with rice straw substrate. The research was purposed to determine the effect of CuSO4 inducer and know the best fermentation time on production of enzyme by Trichoderma asperellum LBKURCC1. Fermentation was carried out with time variations that are 5-10 days and variations of CuSO4 that are 0,25-0,75 g/L with substrate size ±0,5 cm, the bed depth on the tray 3 cm. Fermentation using room temperature and pH is 5,5. The result showed that the highest laccase enzyme activity was obtained on CuSO4 inducer 0,50 g/L and 7 days fermentation with average laccase enzyme activity was 19,270 U/L.Keywords: Inducer, Laccase, Rice straw, Solid state fermentation, Trichoderma asperellum.
Produksi Enzim Lakase Oleh Jamur Trichoderma Asperelloides LBKURCC2 Menggunakan Substrat Jerami Padi Secara Fermentasi Kultur Padat Dengan Variasi Waktu Fermentasi Dan Laju Aerasi 1,5 L/M Iwara, Bangkit Swadi; Helianty, Sri; Dahliaty, Andi
Jurnal Online Mahasiswa (JOM) Bidang Teknik dan Sains Vol 8 (2021): Edisi 1 Januari s/d Juni 2021
Publisher : Jurnal Online Mahasiswa (JOM) Bidang Teknik dan Sains

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Laccase (benzenediol:oxygen oxidoreductase, EC 1.10.3.2) is classified as blue copper oxidase enzyme. Laccase generally found in plant, insect, bacteria and filamentous fungus. One of filamentous fungus that able to degradates lignin is Trichoderma. Lignin is available in biomass such as rice straw, that contains around 18% lignin. The technique of producing laccase enzymes in this study is solid state fermentation. Solid state fermentation allows microorganisms to grow in conditions close to or similar to their natural habitat, with relatively better product than submerged state fermentation. In this study, the effect of giving force aeration on variations in fermentation time was studied in order to obtain optimum conditions for the production of laccase enzyme by solid state fermentation using the fungus Trichoderma asperelloides LBKURCC2 with rice straw substrate on a tray bioreactor. The fermentation is carried out with variation of the fermentation time 6, 8, and 10 days with incubation temperature of 30 ± 2 ºC, acetate buffer solution pH 5.5 (0.05 M), substrate size 1 cm, addition of 0.5 g / l CuSO4.7H2O inducer, bed height 3 cm, and aeration rate 1.5 l / m. The highest laccase enzyme activity was obtained during the production time of 8 days, with an average 7.78 x 10-6 U / L. The 8th day is considered to be the best growth time where the enzyme activity has reached its peak and is in a stagnant condition after the increase that occurred on the 6th and 7th days. Meanwhile, on the 9th and 10th days there was a significant decrease in the activity of the laccase enzyme due to the greater repression of catabolites.Keywords: Laccase, Solid State Fermentation, Tray Bioreactor, Force Aeration, FermentationTime
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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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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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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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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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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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).
Co-Authors Adolf Hiskia Nainggolan Amilia Linggawati Anita R Sidabutar Christine Jose Dwi Cahyaningsih Febry Kurniawan Feliatra Halida Sophia Haryati Haryati Ilham ' Itnawita ' Iwara, Bangkit Swadi Maria Erna Kustyawati Masdalena Sinaga Maya Dahlena Muhamad Fajri Nasution, Nurul Iflah Novianty, Riryn Nur Azlina Nurliati, Ivanna Nurul Khumaida Popy Wardani Puspita Sari Rizki Wulandari Silvera Devi Siregar, Siti Saidah Sri Helianty Susilawati, Susilawati Titania T. Nugroho Titania Tjandrawati Nugroho Waidil Anuar Yuana Nurulita Yum Eryanti