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Yeast Isolation for Bioethanol Production RURIANI, EKA; SUNARTI, TITI CANDRA; MERYANDINI, ANJA
HAYATI Journal of Biosciences Vol 19, No 3 (2012): September 2012
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (53.245 KB) | DOI: 10.4308/hjb.19.3.145

Abstract

We have isolated 12 yeast isolates from five different rotten fruits by using a yeast glucose chloramphenicol agar (YGCA) medium supplemented with tetracycline. From pre-screening assay, four isolates exhibited higher substrate (glucose-xylose) consumption efficiency in the reaction tube fermentation compared to Saccharomyces cerevisiae dan Saccharomyces ellipsoids as the reference strains. Based on the fermentation process in gooseneck flasks, we observed that two isolates (K and SB) showed high fermentation efficiency both in sole glucose and mixed glucose-xylose substrate. Moreover, isolates K and SB produced relatively identical level of ethanol concentration compared to the reference strains. Isolates H and MP could only produce high levels of ethanol in glucose fermentation, while only half of that amount of ethanol was detected in glucose-xylose fermentation. Isolate K and SB were identified as Pichia kudriavzeevii (100%) based on large sub unit (LSU) ribosomal DNA D1/D2 region.
Characterization of Xylanase Streptomyces spp. SKK1-8 MERYANDINI, ANJA; HENDARWIN, TRIO; SAPRUDIN, DEDEN; LESTARI, YULIN
HAYATI Journal of Biosciences Vol 13, No 4 (2006): December 2006
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (134.007 KB) | DOI: 10.4308/hjb.13.4.151

Abstract

Streptomyces spp. SKK1-8 producing xylanase was isolated from soil sample from Sukabumi West Java. The xylanase have an optimum condition at pH 6 and 50 0C. Addition of 5 mM Cu2+ decreased the xylanase activity up to about 77%, whereas not by other cations. The xylanase was stable at 3 0C for 48 hours, and the enzyme half lifetime was 1 hour 45 minute at 50 0C. This xylanase showed the highest activity on oatspelt xylan, and their molecular masses were estimated approximately 16.80, 15.21, and 13.86 kDa. HPLC analysis showed that xylosa and arabinosa were the main hydrolytic product of birchwood xylan. Key words: xilanase, Streptomyces spp., characterization, zymogram and SDS-PAGE, stability
Characterization of Xylanase from Streptomyces spp. Strain C1-3 MERYANDINI, ANJA
HAYATI Journal of Biosciences Vol 14, No 3 (2007): September 2007
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (52.565 KB) | DOI: 10.4308/hjb.14.3.115

Abstract

Xylan is the major constituent of hemi cellulose. Several enzymes are needed to hydrolyse xylan completely, including xylanase. Currently, there is an increasing use of this enzyme. This study was carried out to characterize the xylanase from Streptomyces spp. strain C1-3. Results showed that the xylanase displayed its highest activity at pH 3 and 90 0C and was stable up to 10 hours at this conditions. Its activity increased after the addition of Cu2+, Fe2+, and Co2+ under concentration of 1 and 5 mM, respectively. The activity however, decreased after the addition of Mg2+, Ca2+ at 1 mM and Zn2+ at 5 mM. After a test with five kinds of xylan (i.e. from Birchwood, Beechwood, Arabinoxylan, Oat spelt and CMC), the xylanase of Streptomyces spp. C1-3 showed its preferences to Birchwood- and Arabino-xylan. The results showed that the xylanase of Streptomyces spp. C1-3 was characterized as a thermostable acid xylanase. Key words: xylanase, Streptomyces, stability, CMCase
Immobilization of Extracellular Xylanase from Streptomyces sp. 45 I-3 for Hydrolysis of Corncob Xylan Sunarti, Titi Candra; Mutia, Ferry; Gusmawati, Niken Financia; Lestari, Yulin; Meryandini, Anja
Jurnal Teknologi Dan Industri Pangan Vol 20, No 1 (2009): Jurnal Teknologi dan Industri Pangan
Publisher : Departemen Ilmu dan Teknologi Pangan, IPB Indonesia bekerjasama dengan PATPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (290.721 KB) | DOI: 10.6066/313

Abstract

PENGGUNAAN  XILANASE  Streptomyces sp. 45 I-3 AMOBIL UNTUK HIDROLISIS XILAN TONGKOL JAGUNG [Immobilization of Extracellular Xylanase from Streptomyces sp. 45 I-3 for Hydrolysis of Corncob Xylan ] Anja Meryandini1),2), Titi Candra Sunarti3), Ferry Mutia3), Niken Financia Gusmawati4), dan Yulin Lestari2) 1)Pusat Penelitian Sumberdaya Hayati dan Bioteknologi IPB,Gedung PAU, Kampus IPB Darmaga 16680 2)Departemen Biologi, FMIPA-IPB, Gedung Fapet Lt 5 Wing 1, Kampus IPB Darmaga 16680 3)Departemen Teknologi Industri Pertanian, FATETA-IPB, Kampus IPB Darmaga 16680 4)PS Bioteknologi-Sekolah Pasca Sarjana IPB,  Gedung PAU, Kampus IPB Darmaga 16680 Autor korespondensi: ameryandini@yahoo.com Diterima 15 Desember 2008/Disetujui 13 Juni 2009 ABSTRACT   Xylan extraction from corncob is done by using alkaline as solvent. Xylan extraction from corncob could give the yields as 10.9%. One percent of corncob xylan is used as substrate to produce the xylanase, compared to oatspelt xylan. Immobilization of xylanase was performed using 1% EudragitTM S100 solution (w/v), with 5:1 volume ratio of xylanase and 1 % EudragitTM S100 (w/v). Activity of the immobilized xylanase was decreased to 23.97% compared with free xylanase. Immobilized xylanase have optimum pH and temperature at 6.0 and 40°C  respectively, have also thermal stability at 30–40°C for an hour. Immobilized xylanase could be reused, but its activity decreased to 52.38% after 3 times application.   Key words : xilanase, Streptomyces, amobile
Screening of Proteolytic Enzymes of Streptomyces sp. Local Strain and Their Characterization YURATMOKO, DERI; MUBARIK, NISA RACHMANIA; MERYANDINI, ANJA
Microbiology Indonesia Vol 1, No 2 (2007): August 2007
Publisher : Indonesian Society for microbiology

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Abstract

Protease of two Streptomyces sp. strain were chosen for characterization because of the large clear zone surrounding the colony in nutrient agar media containing 1% (w/v) skim milk. Extracellular protease from the two isolates SLW 8-1 and 45I-3 were characterized following incubation of the isolate in Nutrient Broth media containing skim milk or chicken feather (1%). The optimum activity of the protease SLW 8-1 was at pH 9 and 80 ºC, whereas that of the keratinase was at pH 6.5 and 70 +C. Protease of strain 45I-3 showed its optimum activity at pH 7.5 and 50 ºC whereas the keratinase was at pH 8.5 and 80 ºC.
Activity of Proteolytic and Amylolytic Enzymes from Bacillus spp. Isolated from Shrimp Ponds JAMILAH, IT; MERYANDINI, ANJA; RUSMANA, IMAN; SUWANTO, ANTONIUS; MUBARIK, NISA RACHMANIA
Microbiology Indonesia Vol 3, No 2 (2009): August 2009
Publisher : Indonesian Society for microbiology

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Abstract

Accumulation of feed excess in commercial shrimp ponds due to overfeeding could decrease water quality. Protein and starch are the primary components of shrimp feed. This study was conducted to characterize extracellular proteases and amylases of Bacillus spp. isolated from shrimp ponds. 72 proteolytic and amylolytic Bacillus spp. isolates were screened from shrimp ponds in Karawang, West Java. Ten isolates were selected for further characterization for their growth and ability to reduce total suspended solid generated from commercial shrimp feed. Bacillus sp. DA 5.2.3 and L5 showed excellent activity in reducing total suspended solid, by 37 and 30% respectively. Protease and a-amylase activities of Bacillus sp. DA 5.2.3 isolate were consistently higher than that of L5. Maximum total and specific protease activity of DA 5.2.3 isolate was 2.0 U mL-1 and 40.9 U mg-1 respectively, while the activities of the L5 isolate were 2.1 U mL-1 and 23.0 U mg-1 respectively. Based on its 16S rRNA gene sequences, Bacillus sp. DA 5.2.3 showed 99% similarity to Bacillus cereus XHJ-2-6. Bacillus sp. DA 5.2.3 could potentially be applied to maintain water quality by reducing total suspended solid in water columns of shrimp ponds.
Enzymatic Hydrolysis of Porang by Streptomyces violascens BF 3.10 Mannanase for the Production of Mannooligosaccharides Safitri, Azizah Hikma; Meryandini, Anja; -, Yopi
Media Peternakan - Journal of Animal Science and Technology Vol 37, No 3 (2014): Media Peternakan
Publisher : Faculty of Animal Science, Bogor Agricultural University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (846.166 KB) | DOI: 10.5398/medpet.v37i3.8024

Abstract

Porang (Amorphophallus muelleri Blume) is an indigenous Indonesian plant containing high hemicellulose as a source of glucomannan. An alternative way to produce a good quality of mannooligosaccharides was through hydrolysis of glucomannan by endo-β mannnase from actynomicetes. Based on 16S rRNA analysis, BF 3.10 isolate, isolated from Bukit Duabelas National Park soil, Jambi was identified as Streptomyces violascens BF 3.10. Reducing sugar was analyzed by dinitrosalicylic acid methods. The highest reducing sugar was achieved at the 72 hours of incubation. Mannanase of isolate BF 3.10 had the highest activity at pH 6 and temperature of 70 °C with enzyme activity of 16.38 U/mL and was stable at 4 °C for 48 h. During 5-hour of hydrolysis with substrate concentration of 0.25%, 0.5%, and 1% porang glucomannan dissolved in 10 mL enzyme, mannooligosaccharides were produced with the degree of polymerization of 2-3. Visualization of the products by using thin layer chromatography (TLC) and high performance liquid chromatography (HPLC) methods showed that mannooligosaccharides produced comprised of glucose, mannobiose, mannotriose, and mannotetraose. The degree of polymerization and the simple sugars produced indicated that mannanase produced by S. violascens actively catalyzed the hydrolysis of 1.4-β-D-mannoside linkage from β-1.4-mannan backbone, that eventually produced simple sugars of mannooligosaccharides. Key words: glucomannan, mannanase, mannooligosaccharides, porang, Streptomyces violascens
Selection of Lactic Acid Bacteria as Probiotic Candidate for Chicken Hamida, Fathin; Wiryawan, Komang G; Meryandini, Anja
Media Peternakan - Journal of Animal Science and Technology Vol 38, No 2 (2015): Media Peternakan
Publisher : Faculty of Animal Science, Bogor Agricultural University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (657.302 KB) | DOI: 10.5398/medpet.v38i2.9275

Abstract

Lactic acid bacteria (LAB) regarded as safe microorganisms; they can naturally live in gastrointestinal tract, so appropriately used as a probiotic for chicken. This study aimed to select six isolates of LAB (E1223, E3, E4, E5, E7, and E8) to obtain the isolates potentially as probiotic candidate for chicken. The six isolates were derived from spontaneous fermented corn obtained from Laboratory of Animal Biotechnology and Biomedical, PPSHB, Bogor Agricultural University, Indonesia. LAB isolates were tested their susceptibility to antibiotics (bambermycin, erythromycin, chloramphenicol, and tetracycline) then were examined in vitro for their tolerance to gastrointestinal pH (2, 3, 4, and 7.2) and 0.5% bile salt condition, antimicrobial activity against Salmonella enteritidis and Enterococcus casseliflavus, and ability to adhere to chicken ileal cells. The results showed the isolates E5, E7, and E8 were sensitive to tetracycline and chloramphenicol, they could survive at pH 2, 3, 4, and 7.2, could survive at 0.5% bile salts, produced antimicrobial activity, and able to adhere to ileal cells (9.40±0.00 Log CFU/cm2 of E8) and were significantly (P<0.05) higher than those of control (5.30±0.14 Log CFU/cm2). In conclusion, this study showed that isolate E8 had better potential compared to isolates E5 and E7 in most in vitro assays as a probiotic candidate for chicken. E5, E7, and E8 were closely related with Pediococcus pentosaceus based on 16S rRNA gene. Key words: LAB, probiotic, chicken, in vitro
Enzymatic Hydrolysis of Copra Meal by Mannanase from Streptomyces sp. BF3.1 for The Production of Mannooligosaccharides ARIANDI, .; YOPI, .; MERYANDINI, ANJA
HAYATI Journal of Biosciences Vol 22, No 2 (2015): April 2015
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1826.954 KB) | DOI: 10.4308/hjb.22.2.79

Abstract

Copra meal contained high polysaccharide mannan. Mannanase Streptomyces sp. BF3.1 efficiently hydrolyzed copra meal to mannooligosaccharides. This research determined the optimum conditions of enzyme mannanase Streptomyces sp. BF3.1 to hydrolyze copra meal. The results of the hydrolysis products were analyzed concentrations of reducing sugars, total sugars and the degree of polymerization. In order to determine the type of product, mannooligosaccharides  were analyzed by thin layer chromatography and high performance liquid chromatography. The mannanase had an optimum condition at 70 °C and pH 6. Optimum conditions of hydrolysis was 10% copra meal concentration with incubation time of 5 h at 30 °C which able to produce a variety of mannooligosaccharides products. Under such conditions, the yield of reducing sugar was 3.83 mg/mL with polymerization degree of 4. Analysis of mannooligosaccharides by thin layer chromatography and high performance liquid chromatography revealed mannobiose, mannotriose, mannotetrose, mannopentose, and mannoheksose.
Enzymatic Hydrolysis of Porang by Streptomyces violascens BF 3.10 Mannanase for the Production of Mannooligosaccharides Safitri, Azizah Hikma; Meryandini, Anja; -, Yopi
Media Peternakan Vol 37, No 3 (2014): Media Peternakan
Publisher : Faculty of Animal Science, Bogor Agricultural University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (846.166 KB) | DOI: 10.5398/medpet.2014.37.3.190

Abstract

Porang (Amorphophallus muelleri Blume) is an indigenous Indonesian plant containing high hemicellulose as a source of glucomannan. An alternative way to produce a good quality of mannooligosaccharides was through hydrolysis of glucomannan by endo-? mannnase from actynomicetes. Based on 16S rRNA analysis, BF 3.10 isolate, isolated from Bukit Duabelas National Park soil, Jambi was identified as Streptomyces violascens BF 3.10. Reducing sugar was analyzed by dinitrosalicylic acid methods. The highest reducing sugar was achieved at the 72 hours of incubation. Mannanase of isolate BF 3.10 had the highest activity at pH 6 and temperature of 70 °C with enzyme activity of 16.38 U/mL and was stable at 4 °C for 48 h. During 5-hour of hydrolysis with substrate concentration of 0.25%, 0.5%, and 1% porang glucomannan dissolved in 10 mL enzyme, mannooligosaccharides were produced with the degree of polymerization of 2-3. Visualization of the products by using thin layer chromatography (TLC) and high performance liquid chromatography (HPLC) methods showed that mannooligosaccharides produced comprised of glucose, mannobiose, mannotriose, and mannotetraose. The degree of polymerization and the simple sugars produced indicated that mannanase produced by S. violascens actively catalyzed the hydrolysis of 1.4-?-D-mannoside linkage from ?-1.4-mannan backbone, that eventually produced simple sugars of mannooligosaccharides.Key words: glucomannan, mannanase, mannooligosaccharides, porang, Streptomyces violascens