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Application of Response Surface Method in Optimization of Medium Composition for Xylanase Production by Bacillus halodurans CM1 in Submerged Fermentation SARA GUSTIA WIBOWO; IS HELIANTI; ANI SURYANI; BUDIASIH WAHYUNTARI
Microbiology Indonesia Vol. 10 No. 3 (2016): September 2016
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.5454/mi.10.3.5


A two level factorial design was performed to optimized xylanase production by alkalothermophilic Bacillus halodurans CM1 using response surface method. The variables involved in this experiment were carbon (X), 1 nitrogen source (X) concentration, and pH (XCorn cob and fish powder were use as carbon and nitrogen source 2 3 respectively. Statistical analysis of the experimental results in the range studied, only carbon source gave significant effect on xylanase production.  A second-order model was proposed to represent the enzyme activity as a function of xylan concentration (X) and pH (X).  The optimum corn cobs concentration was 4.37% (w/v), 1 3 fish powder P concentration was 1.75% (w/v) and pH 9. These conditions were tested and validated experimentally since the maximum growth rate achieved with these parameters, and the highest xylanase activity.
Cyclodextrin Glycosyl Transferase and its application in industries Budiasih Wahyuntari
Jurnal Teknologi dan Industri Pangan Vol. 16 No. 3 (2005): Jurnal Teknologi dan Industri Pangan
Publisher : Departemen Ilmu dan Teknologi Pangan, IPB Indonesia bekerjasama dengan PATPI

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Cyclodextrin glycosyl transferase (CGT-ase) is mainly produced by Bacilli. Systematical name of the enzyme is E.C. -1,4 glucan-4-glycosyl transferase. The enzyme catalyzes hydrolysis of starch intramolecular, and intermolecular transglycosylation of -1,4, glucan chains. Cyclodextrins are -1,4 linked cyclic oligosaccharides resulting from enzymatic degradation of starch by cyclodextrin glycosyl transferase through untramolecular transglycosylation. The major cyclodextrins are made up of 6, 7 and 8 glucopyranose units which are known as -, -, and -cyclodextrin. All CGT-ase catalyze three kinds of cyclodextrins, the proportion of the cyclodextrins depends on the enzyme source and reaction conditions. The intermolecular transglycosylation ability of the enzyme has been applied in transfering glycosyl residues into suitable acceptor. Transglycosylation by the enzymes have been tested to improve solubility of some flavonoids and to favor precipitation ci some glycosides. Keywords : cyclodextrin, cyclodextrin glycosyltransferase
The Effect of Growth Medium pH towards Trypsin-Like Activity Produced by Lactic Acid Bacteria DYAH WULANSARI; BUDIASIH WAHYUNTARI; TRISMILAH TRISMILAH; ASTUTIATI NURHASANAH
Microbiology Indonesia Vol. 6 No. 2 (2012): June 2012
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.5454/mi.6.2.1


In cases of pancreatic disease, trypsin deficiency often occurs due to reduced expression of trypsin in the pancreas. Patients with pancreatic problem can be treated with a supplement containing digestive enzymes, including trypsin. However, most of the enzymes currently used for the treatment are derived from porcine and bovine sources. On the other hand, lactic acid bacteria are also known to show trypsin-like activity. In the previous work, our group screened 11 lactic acid bacteria isolates, which had previously been proven to show serine protease activity, for trypsin-like activity. The strains were initially grown in MRS (de Mann, Rogosa and Sharpe) medium before being transferred directly to the production medium to produce trypsin. During the previous study, the initial pH of the production medium was set at 6 (the same as the MRS medium pH), which is the optimum pH for the cell growth of lactic acid bacteria. However, most trypsin has an optimum pH of around 8. In this study, we altered the production medium pH to 8 and we harvested the lactic acid bacteria from MRS medium by centrifugation prior to their inoculation to the production medium. Observation of the culture growth and enzyme activity indicated that the new strategy improved the enzyme activity expressed by some strains.
Selection of Methods for Microbiological Extraction of Chitin from Shrimp Shells JUNIANTO JUNIANTO; BUDIASIH WAHYUNTARI; SISWA SETYAHADI
Microbiology Indonesia Vol. 7 No. 2 (2013): June 2013
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.5454/mi.7.2.5


Chitin extraction from shrimp shells involves two processing steps that are demineralization followed by deproteination process. Lactobacillus acidophilus FNCC 116 and Bacillus licheniformis F11.1 were used in demineralization and deproteination respectively. The overall objectives of this experiment were to determine fermentation systems which resulted in the highest mineral and protein removal. The demineralization experiments consisted of three different batch fermentation designs: batch fermentation (Am ); subsequent batch fermentation 1, in which 100% medium was replaced with fresh medium after 24 h fermentation (Bm ); and subsequent batch fermentation 2, in which 50% medium was replaced with the same amount of fresh medium after 24 h fermentation (Cm ). The demineralization was conducted at 30±2 °C, 50 rpm for 60 h. The deproteination experiments consisted of 3 different batch fermentation designs: batch fermentation 1, inoculum was added once at the beginning of the fermentation (A p); batch fermentation 2, inoculum was added twice, at the beginning and after 24 h fermentation (Bp ); and subsequent batch fermentation, 100% medium was replaced with fresh medium after 24 h fermentation (Cp ). The deproteination was carried out at 55 °C, pH 7.8-8.0, aeration 2.3 vvm, and agitation 275 rpm for 96 h. The experimental results showed that in the demineralization process, fermentation design B gave the highest ash removal. Ash removed in the fermentation design A , B , and C was 97.19, 99.69, and 97.69%, respectively. The protein removed in the fermentation design A , B , and C was 94.42, 94.51, and 95.37%, respectively.
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 | DOI: 10.5454/mi.11.2.1


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).
Effect of pH, Temperature and Medium Composition on Xylanase Production by Bacillus sp. AQ-1 and Partial Characterization of the Crude Enzyme BUDIASIH WAHYUNTARI; NISA RACHMANIA MUBARIK; SISWA SETYAHADI
Microbiology Indonesia Vol. 3 No. 1 (2009): April 2009
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.5454/mi.3.1.3


Bacillus sp. AQ-1 was isolated from household aquarium sediment. The isolate produced extracellular xylanolytic enzymes on xylan containing agar medium. Based on morphological, and physiological analysis, the isolate was identified as Bacillus sp. AQ1. The effect of temperature and pH on isolate growth and xylanase production were observed. The best condition observed for the enzyme production in Luria Broth supplemented with 0.5% oat spelt xylan medium was at 40 °C pH 7. The maximum enzyme production was 0.23 U mL-1 after 20 h of fermentation. Two different medium compositions (A and B) were examined for xylanase production. The maximum growth of the isolate and the xylanase production was better in A medium. Replacing oat spelt xylan in medium A with fruitless oil palm bunch in the medium caused the growth slightly slower than that of in the original formula. However, the xylanase production was 3 times higher in fruitless oil palm bunch medium. Optimum activity of the crude enzyme was observed at 60 °C and pH 7. Each ml of the crude enzyme contained 55.21 U xylanase, 8.12 U amylase and 0.50 U carboxymethylcellulase
Cloning of α-L-arabinofuranosidase Genes and Its Expression in Escherichia coli: A Comparative Study of Recombinant Arabinofuranosidase Originatingin Bacillus subtilis DB104 and Newly Isolated Bacillus licheniformis CW1 MOCHAMAD NURCHOLIS; NIKNIK NURHAYATI; IS HELIANTI; MARIA ULFAH; BUDIASIH WAHYUNTARI; AGUSTIN KRISNA WARDANI
Microbiology Indonesia Vol. 6 No. 1 (2012): March 2012
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.5454/mi.6.1.1


Arabinofuranosidase (Abfa) is one of the most important enzymes involved in degradation of lignocelullose biomass.  Two genes encoding α-L-Arabinofuranosidase (abfA), each from Bacillus subtilis DB104 (abfAa1) and an indigenous Indonesian B. licheniformis CW1 (abfAb3), were cloned by the PCR approach  and expressed in Escherichia coli. Sequences analysis of abfAa1 and abfAb3 revealed that each consists of 1721 and 1739 base pairs long DNA, respectively. Each clone contains a hypothetical open reading frame of 1503 and 1509 bp that encode an Abfa protein of 500 and 502 amino acids for abfAa1 and abfAb3, respectively. The deduced amino acid sequence of AbfaB3 shares 75% identity to that of AbfaA1. The recombinant enzymes were expressed constitutively in E. coli. Partial characterization of those enzymes revealed that the AbfaA1 and AbfaB3 were optimally active at 50 ºC and 60 ºC at pH 6, respectively. Thermostability studies of the recombinant enzymes with p-nitrophenyl α-L-arabinofuranoside at their optimal conditions showed that up to 50% AbfaA1 activity was lost after 5 h incubation at 50  ºC, whereas the AbfaB3 retained its activity over 75% after 12 h pre-incubation oat 60 ºC. This thermostability study of recombinant AbfaB3 showed for the first time that the arabinofuranosidase from B. licheniformis is a thermostable enzyme. The recombinant enzyme showed a higher optimal reaction temperature (60 ºC) in comparison to the previously reported thermostable arabinofuranosidase. The thermostable AbfaB3 has a potential to be applied to the degradation of lignocellulose biomass synergistically with thermostable xylanases, for instance in the production of xylo-oligosaccharides.