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Contact Name
Iman Rusmana
Contact Email
rusmana13@yahoo.com
Phone
+62217560536
Journal Mail Official
microbiology.indonesia@gmail.com
Editorial Address
kPERHIMPUNAN MIKROBIOLOGI INDONESIA (SeKretariat PERMI), Gedung 10.2 Indonesian Life Sciences Center (ILSC), Zona Bisnis Teknologi Puspiptek, Jalan Raya Serpong - Bogor Gunung Sindur, Jawa Barat 16340, Indonesia. Email: microbiology.indonesia@gmail.com
Location
Kota tangerang,
Banten
INDONESIA
Microbiology Indonesia
ISSN : 19783477     EISSN : 20878575     DOI : -
Core Subject : Health, Science,
Microbiology Indonesia provides a unique venue for publishing original researches in microbiology (espesially from Indonesian reseachers), and ensures that authors could reach the widest possible audience. Microbiology Indonesia publishes a wide range of research disciplines on bacteria, archaea, fungi, protozoa, and virus as well as biotechnology related to microbiology. Topics include (but are not limited to): -methods in microbiology, -bioprocess, -environmental microbiology, -food microbiology, -plant-microbe interaction, -animal-microbe interactions, -microbial community, -microbial genetics, -virology, -comparative and functional microbial genomics, -and gene expression in microbes.
Articles 6 Documents
Search results for , issue "Vol. 11 No. 2 (2017): Juni 2017" : 6 Documents clear
Potential MGPB In Optimizing Paddy Straw Mushroom (Volvariella volvacea WW-08) Growth WINDI SILVANI JEMSI; I NYOMAN PUGEG ARYANTHA
Microbiology Indonesia Vol. 11 No. 2 (2017): Juni 2017
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (839.638 KB) | DOI: 10.5454/mi.11.2.2

Abstract

Paddy straw mushroom (Volvariella volvacea) contains high protein content and delicious flavor, makes it highly demand each year. Production of V.volvacea does not merit the requirements due to its limited production. Therefore, approach in increasing production using mushroom growth promoting bacteria (MGPB) are needed. This study aims to obtain MGPB isolate as potential agent to increase V. volvacea strain WW-08 growth. This is experimental research in laboratory that consisted of indigenous bacteria isolation, MGPB screening with dual culture, MGPB inoculum optimization, molecular identification of selected MGPB using 16S rRNA, protein profiling with SDS-PAGE, and fruting body production. Indigenous bacteria obtained from growth medium were 58 isolate, and W34 bacteria at concentration of 106 sel/ml showed most significant result on micellium growth. Sequence of 16S rRNA region showed W34 bacteria is Bacillus cereus. Visualization of SDS-PAGE showed new protein in result of interaction between Bacillus cereus and V. volvacea strain WW-08 with molecule weight of 17kDa. Average of fruting body of V. volvacea strain WW-08 in treatment of B. cereus harvested for 7 days, was 240.19g, whereas without treatment of B. cereus was 82.15g. These findings indicate treatement of B. cereus strain W34 increase V. volvacea WW-08 growth by 300%.
Resistance Test on Aeromonas hydrophila Isolated from African Catfish (Clarias gariepinus) Against Some Antibiotics Groups
Microbiology Indonesia Vol. 11 No. 2 (2017): Juni 2017
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (472.278 KB) | DOI: 10.5454/mi.11.2.5

Abstract

Aeromonas hydrophila is a type of bacteria causing Motile Aeromonads Septicemia (MAS) disease, which infects freshwater fish, including African catfish, and leads to death as well as huge losses to farmers. This research aims to determine the resistance status of various antibiotic classes in A. hydrophila bacteria isolated from African catfish. Bacterial isolates of A. hydrophila were taken from the liver and kidneys of infected African catfishes obtained from Parung, Bogor. Characterization of the bacteria was carried out based on colony morphology and biochemical properties. Meanwhile, bacterial resistance test was conducted using antibiotic disks with Kirby-Bauer method. Based on colony morphology and biochemical properties, the characterization results indicated that the bacterial isolates tested were A. hydrophila. Further examination of the antibiotic resistance test showed that the bacteria were resistant to penicillin antibiotics and macrolides. Future researches are expected to use molecular identification for A.hydrophila bacteria mutant to known the DNA base. 
In Vitro and In Vivo Prebiotic Activities of Purified Oligosaccharides Derived from Various Local Bananas (Musa sp.): Tanduk, Uli, Raja Sereh, and Cavendish
Microbiology Indonesia Vol. 11 No. 2 (2017): Juni 2017
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (247.108 KB) | DOI: 10.5454/mi.11.2.3

Abstract

To evaluate the activity of purified oligosaccharides (POS) as prebiotic from various different local bananas (Musa sp.); Tanduk (T), Uli (U), Raja Sereh (RS), and Cavendish (C); and to investigate their capacity in promoting the growth of Lactobacillus sp., in vivo. In vitro investigation: Oligosaccharides from various different local bananas were purified by 80% ethanol extraction. Subsequently, absolute ethanol was reconstituted before precipitation/centrifugation for glucose removal. Water was also removed by freeze drying. POS from the four bananas were analyzed by Thin Layer Chromatography (TLC). Prebiotic activity of POS was investigated by measurement of Prebiotic Activity Score (PAS).In vivo investigation: Balb/c mice were grouped into 6 groups with different prebiotics supplementation: negative control (4 mice, standard feed), positive control (6 mice, 15 mg of inulin/g/day), and samples (5 mice, 150 mg of T, U, RS, or C banana/g/day) for 40 days. Following 40 days after treatment, fecal viable counts of Lactobacillus sp. and Enterobacteriaceae of Balb/c mice was measured (CFU/g) and analysed. PAS value revealed a positive correlation between the oligosaccharides from bananas and Lactobacillus paracasei, with PAS value for T (0.05), RS (0.15), U (0.33) and C (0.77). Overall data suggest that fecal viable counts of Lactobacillus sp. increased after 25 days administration of U, RS, and C banana when compared to controls. Contrastingly, the fecal viable counts of Enterobacteriaceae decreased after 40 days administration of U, RS, and C banana compared to the control. Different types of local bananas demonstrate diverse prebiotic activities: U and C promote Lactobacillus sp. growth and reduce Enterobacteriaceae count. PAS value of U and C suggest potential prebiotic activity, whereas T and RS do not.
Isolation, Characterization, and Production of Lipase from Indigenous Fungal for Enzymatic Interesterification Process LISA PRATAMA; IS HELIANTI; ANI SURYANI; BUDIASIH WAHYUNTARI
Microbiology Indonesia Vol. 11 No. 2 (2017): Juni 2017
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (750.463 KB) | DOI: 10.5454/mi.11.2.1

Abstract

Lipase catalyses hydrolysis and esterification of lipids. The purpose of this research was to  obtain lipase producing indigenous fungi, to identify the selected fungi, to study optimum temperature and pH of the enzyme activity, as well as the  enzyme ability in interesterification reaction. The isolates used in the experiment were isolated from tempeh, oncom and BPPT laboratory culture collection. The results showed that three fungal isolates which isolated, tempe and oncom and  an isolate of BPPT-CC were positive produced lipase after qualitative assay using Rhodamine B, olive oil and PVA. The morphology identification of the isolates, revealed that R isolate was  Aspergillus sp, T isolate was Neurospora sp. and O isolate was Rhizopus sp. Upon quantitative assay from determination of the media and time production, potato dextro broth (PDB) with olive oil 2% in 48 hours fermentation showed the highest specific activity of the enzymes. Lipase produced from three isolate have the optimum at pH 4, temperatures at 40-45 °C and stable in interesterification reaction (55 °C) for 30-40 min. HPLC analysis after interesterification enzymatic reaction in mixture palm kernel olein (PKOo) and palm stearin (POs) showed that the composition of triglycerides (TAG) do not change if compared with the commercial lipase (Lypozyme TL1M).
Cloning of Lipase Gene From Thermomyces langinosus into Pichia pastoris with its Original Signal Peptide MILANI ANGGIANI; IS HELIANTI; NIKNIK NURHAYATI; ABINAWANTO ABINAWANTO
Microbiology Indonesia Vol. 11 No. 2 (2017): Juni 2017
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (716.728 KB) | DOI: 10.5454/mi.11.2.4

Abstract

Lipase is one of the most important industrial enzymes, which is widely used in the preparation of food additives, cosmetics, and pharmaceutical industries. In the previous study, we have cloned synthetic Thermomyces lanuginosus lipase gene into Bacillus subtilis and Escherichia coli and resulting low expression for enzyme activity. The aim of this research was to construct the Thermomyces lanuginosus lipase (TLL) gene into Pichia pastoris vector expression with TLL original signal peptide. TLL gene was amplified by PCR and contained original signal peptide and then inserted into pPICZα A between XhoI and XbaI site, and transformed into competent cell E.coli DH5α. From the transformant, two of positive recombinants were analyzed by sequencing analysis. As the result,both of two recombinant have a positive target gene which has lipase gene. The correct plasmid was linearized and then was transformed in Pichia pastoris X-33 by electroporation method. Thermomyces lanuginosus synthetic gene lipase has been successfully integrated into chromosome of P. pastoris X-33, which revealed by clear zones arund the colony on Yeast extract Peptone Dextrose Tributyrin (YPD.TB) plate with zeocin. The Thermomyces lanuginosus lipase had an open reading frame of 916bp encoding TLL of 314 amino acids with theoretical molecular mass of 35 kDa. The recombinant enzyme, Thermomyces lanuginosus lipase had optimal temperature at 80˚C and optimal pH at pH 8.
ITA REGISTRATION FORM AND BACK COVER
Microbiology Indonesia Vol. 11 No. 2 (2017): Juni 2017
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1661.804 KB) | DOI: 10.5454/mi.11.2.%p

Abstract

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