Claim Missing Document
Check
Articles

Found 29 Documents
Search

Hidrolisis Xilan Bagas Menggunakan Xilanase Bacillus subtilis XJ28 dan Karakterisasi Enzimnya A, Gading Wilda; ., Yopi; Meryandini, Anja
JURNAL BIOLOGI INDONESIA Vol 11, No 1 (2015): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (2865.185 KB) | DOI: 10.14203/jbi.v11i1.2150

Abstract

Xylanase extracellular enzyme is produced by various microbes. Hydrolysis of bagasse xylan can produced xylooligosaccharide. The main components of hemicellulose was xylan at bagasse. IdentificationBacillus subtilisXJ28 using primer 16S RNA. The qualitative test used Congo-Red stainning, whereas quantitative test used Dinitrosalicyclic Acid (DNS) methode. The hydrolyzing product was analysed used TLC (Thin Layer Chromatography). This research aims were to characterized xylanase from isolate XJ28 and analyzing the hidrolyzing product from xylan bagasse. Pretreatment process included delignification using sodium hypochlorite 1% and xylans extraction using alkaline (NaOH 15%) as the solvent. The result of the xylans extracted from bagasse was 9,9% xylan and after purification was obtained 3,4% soluble xylan. Xylanase activity has the highest activity at 96 h of incubation time with activity 11,3 U/mL. Xylanase Bacillus subtilis XJ28has the optimum condition at pH 7 and 50 ºC and stable up to 72 hr of  incubation time at room temperature and 4 ºC. The hydrolysis product using xylanase crude enzyme was reducing sugar with molecular weight around  of sucrose and oligosaccharide. Keywords: xylanase, xylan bagasse, hydrolysis, TLC. 
Isolasi dan Seleksi Bacillus sp. dari Ikan Lele (Clarias sp.) serta Potensinya sebagai Probiotik ., Hamtini; ., Widanarni; Meryandini, Anja
JURNAL BIOLOGI INDONESIA Vol 11, No 1 (2015): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (2778.371 KB) | DOI: 10.14203/jbi.v11i1.2151

Abstract

The aims of this study was to isolate and select Bacillus from the gut of catfish as probiotic candidates in the fish feed production. Isolation was conducted by heating samples at 80 °C for 10-15 minutes using Triptone Soy Agar (TSA) media which have been added with 1% skim milk for proteolytic activity and 1% starch for amylolytic activity. Selection was conducted based on pathogenicity test, antibiotic susceptibility test and total suspended solids. Isolate that have ability to degrade feed would be made the growth curves, analysis of protease and amilase activites and also combination of bacteria isolate with feed. Selected isolates as candidate probiotic were identified furthermore using 6S-rRNA gene. Among 16 isolates, there were 7 isolates that have gamma hemolytic activity (PTB 1.1, PTB 1.2, PTB 1.4, PTB 1.7, STB 1.6, STB 1.1 and STB 2.1). Antibiotic susceptibility test showed that 3 isolates were sensitive to the tested antibiotics (PTB 1.4, PTB 1.7 and STB 1.6). These three selected isolates were tested for their ability to degrade fish feed. PTB 1.4 isolate was able to degrade the feed with the smallest residue on the filter paper (0.0068 g). PTB 1.4 isolate also has proteolytic and amylolytic index of 0.61 and 0.60, respectively. Amylase activity of PTB 1.4 isolate added with 1.2% feed reached the highest peak in 120-hour of observation time (0.399 µ/mL) and the highest protease activity was in 72-hour of observation time (6.595  µ/mL). PTB 1.4 isolate has the ability to degrade the feed with the amount of 106 CFU/mL inoculum. Based on 16S-rRNA gene sequences isolate PTB 1.4 was 99% homolog with Bacillus megaterium. Isolation and selection of probiotic candidate from Clarias sp. get PTB 1.4 was a best isolate that there were not pathogenic, sensitive to antibiotic test, had protease and amilase activities. PTB 1.4 isolate had capability to degrade the feed. Keywords: Bacillus, Clarias sp., probiotic, feed 
Characterization of Ethanolic Extract of Streptomyces sp. as a Pancreatic Lipase Inhibitors Produced by Endophytic Streptomyces sp. AEBg12 Fitri, Lenni; Meryandini, Anja; Iswantini, Dyah; Lestari, Yulin
Biosaintifika: Journal of Biology & Biology Education Vol 9, No 2 (2017): August 2017
Publisher : Department of Biology, Faculty of Mathematics and Sciences, Semarang State University . Ro

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15294/biosaintifika.v9i2.8907

Abstract

Endophytic Streptomyces sp. AEBg12 isolated from Zingiber cassumunar (Bangle) is known to produce pancreatic lipase inhibitory compound. However, the characteristics of this active compound has not been reported yet. This study aimed to determine the characteristics of pancreatics inhibitory compound produced by Streptomyces sp. AEBg12 and to assess the role of endophytic actinobacteria in producing pancreatic lipase inhibitor using endophytic-free bangle tissue culture, wild bangle and compared with the activity of Streptomyces sp. AEBg12 endophytes. Supernatant of Streptomyces sp. AEBg12 was extracted using ethanol, ethyl acetate, and n-hexane solvents. Toxicity test was performed using larvae of shrimp Artemia salina. The results showed that the best solvent to obtain pancreatic lipase inhibitor compounds was ethanol. Phytochemical analysis showed that ethanolic extract of endophytic Streptomyces sp. AEBg12 contained flavonoids. IC50 value of ethanol extract was 180.83 g/ml. The result of TLC showed that ethanolic extract of Streptomyces AEBg12 had a blue luminescence band indicated that there were either flavone, flavanones, flavonols or isoflavones. Inhibitory activity of Streptomyces sp. AEBg12 was higher than wild bangle and bangle tissue culture. The information from this study can be be used as a basic data for further characterization of the active compound, which might be developed as an antiobesity agent through its pancreatic lipase inhibitory activity.
Exploration of Potential Actinomycetes from CIFOR Forest Origin as Antimicrobial, Antifungus, and Producing Extracellular Xylanase Sipriyadi, Sipriyadi; Lestari, Yulin; Wahyudi, Aris Tri; Meryandini, Anja; Suhartono, Maggy Thenawidjaja
Biosaintifika: Journal of Biology & Biology Education Vol 8, No 1 (2016): March 2016
Publisher : Department of Biology, Faculty of Mathematics and Sciences, Semarang State University . Ro

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15294/biosaintifika.v8i1.5052

Abstract

This study aimed to isolate and explore the actinomycetes of CIFOR forest origin as an antimicrobial and antifungal agent, to produce an extracellular xylanase, and to identify isolates based on 16S rRNA gene sequences. Actinomycetes were isolated using Humic-acid Vitamin-B agar (HV) media. Actinomycetes colonies that grow on the medium HV was subsequently purified by growing them on yeast malt agar (YMA) media), then an antagonistic test of selected bacteria against Bacillus sp., Escherichia coli, Fusarium oxysporum, and Sclerotium sp was performed. Xylanase activity test was detected by observing a clear zone, followed by identification. Total of 35 isolates of actinomycetes isolated based on their colony morphology characteristics and diverse types of spore chains showed Streptomyces spp. of isolates CFR-06, CFR-15, CFR-17, CFR-18, and CFR-19 were able to inhibit the growth of Bacillus sp.. The highest inhibition zone has a diameter of 10.1 mm (isolate CFR-17). Isolates CFR-01 and CFR-15 were able to inhibit the growth of E. coli with the highest inhibition zone diameter of 5.1 mm (isolate CFR-15). Isolates CFR-29 and CFR-12 were able to inhibit the growth of F. oxysporum while isolate CFR-35 were able to inhibit the growth of Sclerotium sp.. Xylanase activity test showed that isolates CFR-12, CFR-20, CFR-22, CFR-24, CFR-25, CFR-30, CFR-33, CFR-34 have an ability to produce extracellular xylanase enzyme. Actinomycetes isolate (Xyl_22) as a potential xylanase enzyme producer was closely related with Streptomyces drozdowicii by the maximum similarity of 99%.How to CiteSipriyadi, S., Lestari, Y., Wahyudi, A., Meryandini, A., & Suhartono, M. T. (2016). Exploration Potential CIFOR Forest actinomycetes origin as Antimicrobial, Anti Fungus and Producing Enzymes Extracellular Xylanase. Biosaintifika: Journal of Biology & Biology Education, 8(1), 94-102.
Pectinase Production and Clarification Treatments of Apple (Malus Domestica) Juice Berutu, Cocok Ana Maryani; Fahrurrozi, Fahrurrozi; Meryandini, Anja
ANNALES BOGORIENSES Vol 21, No 2 (2017): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (351.911 KB) | DOI: 10.14203/ab.v21i2.311

Abstract

Pectinases are a group of an enzyme that break down pectin, a polysaccharide that is found in plant cell walls. Today, the application of pectinolytic enzymes plays an important role in food technology for the maceration of fruits and vegetables, including for the extraction and clarification of juice. This research aimed to produce pectinase enzyme for clarifying of apple juice. A microbial culture was selected from cocoa bean fermentation samples and identified as Bacillus sp.. The highest enzyme activity was investigated after 48 hours of incubation. Citrus pectin as the carbon source and peptone as the nitrogen source was found as the best component for pectinase production. The optimum condition of pectinase activity was observed at pH 5, temperature 40 °C and the crude enzyme had the higher activity at one hour storage. Apple juice was treated with the enzyme at different concentrations (0%, 0.5%, 1%, 2%, 4%). Apple juice clarification was evaluated for its percent clarity and viscosity. The result showed that enzyme treatment at 4% in apple juice promoted juice clarification and decreased pH and viscosity. In conclusion, the quality of apple juice can be improved by enzymatic treatment using pectinase.
Optimization of Culture Conditions for Production of β-Mannanase by Strain Nonomuraea sp. ID06-379 using Submerged Substrate Fermentation Ratnakomala, Shanti; Yopi, Yopi; Suhartono, Maggy T; Meryandini, Anja; Prasetya, Bambang
ANNALES BOGORIENSES Vol 18, No 2 (2014): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (685.031 KB) | DOI: 10.1234/96

Abstract

The objective of this study was to investigate the effect of media compositions on the production of β-mannanase by Nonomuraea sp.ID06-379. The study was focused on the influence of carbon, nitrogen,phosphorus and detergents on β-mannanase synthesis through manipulating media compositions on production medium. The results indicated that for carbon sources, locus bean gum (0.745 ± 0.036 U/ml) showed maximum mannanase activity. Malt extract was the best nitrogen source for producing β-mannanase (1.075 ± 0.006 U/ml),(NH4)2HPO4 as phosphate source (1.733 ± 0.026 U/ml) and Tween 80 (1.145 ± 0.003 U/ml) as surfactants effect on increasing permeability of bacterial cell membrane, enhancing membrane transport and excretion of extracellular enzymes into the production media. The results showed that 1% malt extract, 0.5% locus bean gum and 0.05% (NH4)2HPO4 were good substances for nitrogen source, carbon source and phosphate respectively. The highest production of β-mannanase by Nonomuraea sp. ID06-379 (5.33 U/mg) was reached in the medium optimization (Vogel’s minimal medium) contained the following ingredients: 0.5% locus bean gum, 1% malt extract and 0.05% (NH4)2HPO4, under submerged fermentation with shaking at 120 rpm and 28 C for 2 days incubation.
PENINGKATAN KUALITAS BIJI KAKAO (Theobroma cacao L) MELALUI FERMENTASI MENGGUNAKAN Lactobacillus sp. dan Pichia kudriavzevii Meryandini, Anja; Basri, Asrianti; Sunarti, Titi Candra
Jurnal Bioteknologi & Biosains Indonesia (JBBI) Vol 6, No 1 (2019): June 2019
Publisher : Badan Pengkajian dan Penerapan Teknologi (BPPT)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (848.014 KB) | DOI: 10.29122/jbbi.v6i1.3048

Abstract

The Improvement of Cacao Beans Quality through Fermentation by Using Lactobacillus sp. and Pichia kudriavzeviiABSTRACTIndonesia is one of the main cacao producers in the world. Indonesian cacao product is, however, relatively of low quality. Quality improvement of cacao beans is thus needed to increase added value of the product through such method as fermentation using bacteria and yeast. This study was conducted using four fermentation treatments, namely F1 (spontaneous fermentation without the addition of inoculum), F2 (addition of lactic acid bacteria inoculum), F3 (addition of yeast inoculum), F4 (addition of mixed lactic acid bacteria and yeast inoculum). The fermentation was carried out for 5 days. The parameters measured were the microbial cell number, pH, ethanol, total reducing sugar, and total acid concentration, as well as cacao seed quality. Results showed that, compared to the other treatments, the F4 treatment gave the best result, namely 83% of the cacao seeds being fermented, 2% non-fermented, 14% unfermented, 1% moldy, and 2% germinated. The liquid produced during the fermentation contained the highest reducing sugar of 123.38 mg·mL-1, the highest total acid of 24.42 mg·mL-1, and 3.57% ethanol.Keywords: cacao beans, fermentation, lactic acid bacteria, starter, yeast ABSTRAKIndonesia adalah salah satu penghasil kakao utama di dunia. Namun berdasarkan mutu, produk kakao Indonesia masih relatif tergolong rendah. Peningkatan kualitas biji kakao diperlukan untuk memberikan nilai tambah pada produk melalui metode seperti fermentasi menggunakan bakteri dan khamir. Penelitian ini dilakukan dengan empat perlakuan fermentasi yaitu F1 (fermentasi secara spontan tanpa penambahan inokulum), F2 (dengan penambahan inokulum bakteri asam laktat (BAL)), F3 (dengan penambahan inokulum khamir), F4 (dengan penambahan inokulum campuran bakteri asam laktat dan khamir). Fermentasi dilakukan selama 5 hari, dan parameter yang diukur selama fermentasi adalah jumlah mikroba, pH, kadar etanol, gula pereduksi, total asam serta kualitas biji. Hasil menunjukkan bahwa, dibandingkan perlakuan lainnya, perlakuan F4 memberikan hasil terbaik yaitu 83% biji terfermentasi, 2% tidak terfermentasi, 14% terfermentasi sebagian, 1% berjamur, dan 2% berkecambah. Cairan fermentasi tersebut mengandung gula reduksi yang paling tinggi 123,38 mg·mL-1, total asam tertinggi 24,42 mg·mL-1, dan kadar etanol mencapai 3,57%.Kata Kunci: bakteri asam laktat (BAL), biji kakao, fermentasi, khamir, starter
Isolasi Bakteri Mananolitik dan Karakterisasi Mananasenya Meryandini, Anja; Anggreandari, Rizky; Rachmania, Nisa
Biota : Jurnal Ilmiah Ilmu-Ilmu Hayati Vol 13, No 2 (2008): June 2008
Publisher : Universitas Atma Jaya Yogyakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (189.098 KB) | DOI: 10.24002/biota.v13i2.2675

Abstract

Isolate RA05 has the highest mannanolytic index and mannanase activity which isolated from copra soil waste from Pasaman, West Sumatra. The best growth condition that produces best mannanase activity of isolate RA05 was achieved from 500 ml flask containing 100 ml medium with 100 rpm agitation. Isolate RA05 showed its mannanase activity in medium containing Locust Bean Gum and coconut meal but not in medium containing kolang kaling. This mannanase had the highest activity on medium containing 2% of coconut meal with optimum condition temperatur 800C and pH 2.5. Adding of 5 mM MnCl2 on the crude enzym increased the activity near 300%. Other kation (Ca2+, Zn2+, Cu2+, Mg2+, Fe2+ dan Co2+) did not display great effect on the activity.
Karakterisasi Protease Ekstraseluler Clostridium spp. T11-3 Natalia, Loli; Nathalia, Lily; Meryandini, Anja
Biota : Jurnal Ilmiah Ilmu-Ilmu Hayati Vol 11, No 1 (2006): February 2006
Publisher : Universitas Atma Jaya Yogyakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (264.063 KB) | DOI: 10.24002/biota.v11i1.2822

Abstract

Protease is one of the leather commercial enzymes which is widely used such in food processing, medicine and leather industry. Clostridium sp T11-3 was isolated from Tiu Jeruk River in Nusa Tenggara Barat. Sequence analysis of 16S rRNA indicated that Clostridium spp T11-3 was closely related to C. bifermentans. This isolate produced maximum protease activity after 18 hours of cultivation in liquid media. Protease of Clostridium spp 11-3 displayed maximum activity at pH 5 and 60oC with casein as substrate. In the presence of 1 mM divalent ion Mg2+ the enzym activity increased to 141 %, while others ion divalent (Ca2+, Zn2+, Cu2+, Fe2+, and Co2+) inhibited protease activity.
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.