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All Journal Jurnal Riset Kimia Jurnal Kimia Terapan Indonesia Jurnal Ilmiah Berkala: Sains dan Terapan Kimia
Linar Z. Udin
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Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Materials Science & Nanotechnology

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PRODUKSI GLUKOAMILASE DARI RHIZOPUS ORYZAE SKALA FERMENTASI 2 LITER DAN 4 LITER Linar Z. Udin; Ngadiman Ngadiman; A. T. Karossi
Jurnal Kimia Terapan Indonesia Vol 4, No 1 (1994)
Publisher : Research Center for Chemistry - LIPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (3253.368 KB) | DOI: 10.14203/jkti.v4i1.253

Abstract

Production of glucoamylase by R. oryzae has been conducted in erlenmeyer flasks using medium containing sago starch as carbon source and soybean meal as nitrogen source. It was known that 2 % of sago starch and 0.5 % of soybean meal in the medium is the best composition for the production of glucoamylase. At the present study, the optimal condition for maximal production of glucoamylase fermentation from R. oryzae was investigated using sago starch medium in the 2L and 4L scale. The results showed that the maximum production of glucoamylase at 600-1500 ml fermentation scale was reached at day-8 of incubation time. At this condition, the enzyme specific activity was 0.85 U/mg protein - 1.50 U/mg protein. Forglucoamylase production within 4000 ml fermentation scale, the maximum enzyme specific activity, 2.58 U/mg protein, was obtained at day-S of fermentation with 300 rpm agitation, while the maximum activity of 3.47 U/mg protein and 4.71 Ulmg protein were achieved at day-6 and day-5 of fermentation process with 500 rpm and 700 rpm agitation, respectively. At this maximum condition, the use of sago starch reached 94 - 98 %, and biomass production at the end of fermentation process was 4.80 - 7.90 g [dry weight)/L medium.
KLON GEN PENISILIN ASILASE PADA COSMID pHC79 Linar Z. Udin; Hadi Sutedjo
Jurnal Kimia Terapan Indonesia Vol 6, No 1-2 (1996)
Publisher : Research Center for Chemistry - LIPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (4081.855 KB) | DOI: 10.14203/jkti.v6i1-2.236

Abstract

Penicillin acylase plays an important role in the catalysis of benzylpenicillin hydrolytic reaction, prodeucing 6-aminopenicilanic acid (6- APA), a precursorfor the formation of penicillinderivatives. Cloning of the penicillin acylase gene of Escherichia coli B130 chromosomal DNA on pHC79 cosmid vector to increase the enzyme activity has been investigated. The cloning was cooducted with several steps, including isolation of the chromosomal DNA. digestion by restriction enzyme, ligation by T4-DNA ligase, transformation of the recombinant DNA, and selection of the transformans. Microbial assay utilizing Serratia marcescens was carried out for screening the penicillin acylase colony, whereas the determination of the enzyme activity was examined based on Kornfeld method. From 2070 colonies screened by S. marcescens, only 4 positive colonies were obtained. The enzyme activity of these colonies was 4-6 fold higher than the penicillin acylase activity from E. coli B 130.
PRODUKSI PROTEASE ALKALI DAN KERATINASE DARI Brevibacillus agri A-03 TERMOFILIK Anthoni Agustien; Jetty Nurhajati; Linar Z. Udin; Pingkan Aditiawati
Jurnal Riset Kimia Vol. 4 No. 1 (2010): September
Publisher : Universitas Andalas

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.25077/jrk.v4i1.44

Abstract

 ABSTRAK Protease alkaline and keratinase are a group of protease enzym which have important value in detergen industry and skin tannery. Brevibacillus agri A-03 is thermophilic bacteria isolate that comes from Ambayan Sumatera Barat hot spring and has the ability to produce protease and keratinase. The purpose of this research is to get protease alkaline and thermostable keratinase from Brevibacilus agri-A03. thermostable enzym is produced from enzym production enzym that contains kasein and keratin at various medium pH, inoculum incubation temperature and medium type. Enzym activity is measured by modified Walker methode, protein content is measured by Lowry methode. Protease alkaline is produced at exponential phase, maximum at 18th hours of incubation and keratinase is produced at stationer phase, maximum at 22nd hours. Both enzym is produced optimically at medium pH condition 9.0; incubation temperature 55°C, inoculum 5% by using modified Johnvesly and Naik medium with each protease and keratinase specific activity 1.927 and 1.047 U/mg  Keywords: Protease alkaline, Keratinase, Thermofilic, Brevibacillus agri A-03   
EFFECTS OF MEDIUM COMPOSITION ON OXYTETRACYCLINE PRODUCTION BY STREPTOMYCES RIMOSUS ATCC 33022 Linar Z. Udin; S. Pudjiraharti; A. T. Karossi
Jurnal Kimia Terapan Indonesia Vol 2, No 1-2 (1992)
Publisher : Research Center for Chemistry - LIPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (2869.601 KB) | DOI: 10.14203/jkti.v2i1-2.281

Abstract

The economical production of antibiotics to some extent depends on the availabilily of cheap substrates. The work reported in the present paper deals with the fermentative production of oxytetracycline by Streptomyces rimosus ATCC 33022 using commerciol high fructose syrup (HFS), vitamin B complex and citric acid of technical grode. The effects of concentration of high fructose syrup (0.5 - 2.5 %, v/v), commercial vitamin B complex (0.03 - 0.07 %, w/v) and the citric acid (0.34 - 1.28 %. w/v) were examined in this study. It was found that fermentation medium (medium-MHFS) containing high fructose syrup 1.0 % produced maximum activily of oxytetracycline after 4 days incubation period. Fermentation tnedium (mediwn-MBpleJ containing 0.05 % commerciol vitamin B complex showed maximum acrivily after 3 days incubation. While the addition of citric acid (0.64 %) to the fermentation medium (medium-MCA) was found optimumfor production oxytetracycline.
PENGARUH PENINGKATAN LIPOFILISITAS PADA SENYAWA ANALOG UK-3A DALAM MENGHAMBAT PERTUMBUHAN SEL KANKER P-388 Hanafi M; Y Anita; AMJ. Putra; A. Darmawan; N. Artanti; Linar Z. Udin
Jurnal Kimia Terapan Indonesia Vol 11, No 1 (2009)
Publisher : Research Center for Chemistry - LIPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (3926.945 KB) | DOI: 10.14203/jkti.v11i1.173

Abstract

Antibiotic UK-3A contains a 9-membered dilactone ring. It had been isolated as a minor component from the mycelium of 5trepyomyces sp. 51701.The antibiotic was hypothesized to be potential to inhibit the growth of leukemia cancer cell line of P388 and KB with ICso 38 and 20 Dg/mL, respectively. To understand the effect of lipophilicity increase of the analogues on their anticancer activities based on QSAR parameter (Log P) and binding energy to BcL-xL protein. To produce analogues of UK-3A, 3hydroxypicolinyl serine methyl ester (A) was synthesized from 3-hydroxypicolinic acid and L-serine methyl ester. The product was then esterified by pentanoic (1), hexanoic (2), heptanoic (3), and octanoic (4). The final products were confirmed with IHand 13C FT-NMR and FTIR spectra, and also MS spectra. Then they were tested against P388 Murine Leukemia cells. The result of bioassay showed lipophilicity increase of3hydroxypicolinyl serine methyl octhyl ester (PSMOE) correlated positively with their anticancer activity increase, withICso 15.4mg/mL against P388 cell lines.Keywords: Anticancer, Streptomyces sp 517-02, UK-3A, Analog UK-3A and P388
RADIASI SINAR ULTRA VIOLET STRAIN ASPERGILLUS ORYZAE UNTUK MENINGKATKAN PRODUKSI ALFA AMILASE Yetti M.lskandar; Linar Z. Udin; A. T. Karossi
Jurnal Kimia Terapan Indonesia Vol 5, No 1 (1995)
Publisher : Research Center for Chemistry - LIPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (2699.427 KB) | DOI: 10.14203/jkti.v5i1.244

Abstract

Mutation of Aspergillus oryzae was carried out by ultra violet irradiation at 254 nm. The mutans obtained with 0, 10, 20,30, 40 and 50 minutes irradiation were screened for their amylolytic activity and alpha amylase production. The latter was carried out by aerobic fermentation using sago (Metroxylon spy starch in shake flasks for five days at 30°C with orbital shake at 120 rpm. The observation indicated that the mutant resulted from 10 minute irradiation demonstrated a maximum alpha amylase activity of 1675 Unit/g protein at day-d. The amylase activity was assayed at 40°C for 30 minute incubation. The starch utilization was 87% and 3.84 g dry weight of biomass per L medium was produced. The specific activity of alpha amylase obtained from untreated parental strain was 1069 Unitlg protein. Starch consumption and biomass production was 80% and 3.62 g dry weight/ L medium, respectively. The increase of alpha amylase specific activity at 10 minute irradiation time was 56%.
PEMURNIAN GLUKOAMILASE DARI HASIL FERMENTASI KAPANG RHIZOPUS ORYZAE Linar Z. Udin; Rini Noviyanti; A. Sidik; A. T. Karossi
Jurnal Kimia Terapan Indonesia Vol 4, No 1 (1994)
Publisher : Research Center for Chemistry - LIPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (2799.989 KB) | DOI: 10.14203/jkti.v4i1.250

Abstract

Purification of the glucoamylase R. oryzae was carried out by addition of ammonium sulfate 80% saturation, on the fermentation broth at 4°C. The precipitate formed by centrifugation at 9000 rpm was then dialyzed in buffer solution and then concentrated using freeze dryer. It was found that the specific activity of the enzyme was around three-fold higher the crudeenzyme from fermentation broth and the purity of the enzyme was almost twelve-fold.purer than the crude enzyme. The molecular weight of the glucoamylase was found to be 36,000 as determined by SDS gel electrophoresis. The optimum pH witli soluble starch as substrate was at pH 4.5 and the optimum temperature was 55°C while the Km Value was 0.027%.
PRODUKSI POLI-Γ-ASAM GLUTAMAT DARI Bacillus subtilis B112 DENGAN VARIASI KONSENTRASI AMONIUM SUFAT SEBAGAI SUMBER NITROGEN DALAM MEDIA FERMENTASI Abubakar Sidik; Linar Z. Udin; Safri Ishmayana
Jurnal Sains dan Terapan Kimia Vol 5, No 1 (2011)
Publisher : Program Studi Kimia, Universitas Lambung Mangkurat

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (502.744 KB) | DOI: 10.20527/jstk.v5i1.2088

Abstract

Poli-γ-asam glutamat (PGA) dan hasil degradasinya aman bagi manusia sehingga dapat dimanfaatkan sebagai bahan pengental, pelembab, pelepas berjangka atau sebagai pembawa obat. Meskipun banyak digunakan pada berbagai bidang industri, bahan ini masih diimpor dari luar negeri. Oleh karena itu, perlu dikembangkan suatu proses untuk memproduksi PGA secara efektif dan efisien. Penelitian ini dilakukan untuk menentukan konsentrasi optimum amonium sulfat sebagai sumber nitrogen untuk menghasilkan PGA dalam jumlah yang banyak. Produksi PGA dilakukan dengan fermentasi menggunakan bakteri Bacillus subtilis B112. Analisis yang dilakukan selama proses fermentasi meliputi pengukuran pH, derajat kekeruhan, berat kering sel dan viskositas media. Isolasi PGA dilakukan dengan tahapan sentrifugasi, pengendapan dengan metanol, dialisis dan liofilisasi. PGA yang telah diisolasi kemudian ditentukan berat molekulnya dengan meggunakan SDS-PAGE, sedangkan komposisi asam amino PGA ditentukan dengan menggunakan metode KLT. Hasil penelitian menunjukan bahwa konsentrasi ammonium sulfat yang optimum untuk menghasilkan PGA adalah 0,75% b/v. PGA yang diperoleh dengan variasi 0,75% amonium sulfat sebanyak 61,6 mg. Penentuan berat molekul dengan menggunakan SDS-PAGE menunjukan bahwa PGA yang diproduksi oleh B. Subtilis B112 memiliki berat molekul sekitar 205 kDa. Kata Kunci: Asam L-glutamat, amonium sulfat, B. Subtilis B112, PGA 
Co-Authors A. Darmawan A. Sidik A. T. Karossi Abubakar Sidik AMJ. Putra Anthoni Agustien Hadi Sutedjo Hanafi M Jetty Nurhajati N. Artanti Ngadiman Ngadiman Pingkan Aditiawati Rini Noviyanti S. Pudjiraharti Safri Ishmayana Y Anita Yetti M.lskandar