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S. Pudjiraharti

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Author-ID : 3944205

Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Materials Science & Nanotechnology

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Articles

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

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.

PRODUKSI ALFA-AMILASE OLEH ASPERGILLUS ORYZAE DALAM MEDIA PATI SAGU (Metroxylon sp.) S. Pudjiraharti; L. Z. Udin; A. T. Karossi
Jurnal Kimia Terapan Indonesia Vol 7, No 1-2 (1997)
Publisher : Research Center for Chemistry - LIPI

The production 0f alpha-amylase in sago starch media by A. oryzae have-been performed in Biostat-B stirred tank fermentor with working volume of 2 L. The condition was adapted from the fermentation using Biotech fermentor: working volume 4 Liters, temperature 27°e, aeration 0,75 wm and agitation of 300 rpm. The concentrations of inoculum added into the medium were 2,5 - 3% v|v. The maximum enzyme speslfic activites around 300-460 U|g protein was obtained at fermentation using inoculum concentration of 2,5%, while the maximum enzyme specific activity of 850 U|g protein was also obtained at fermentation using inoculum concentration of 3%. The maximum enzyme specific activity was achieved at day 5 or 6 of fermentation.Fermentation using various concentrations of inoculum in erlenmeyer flask scale was carried out to investigate the inoculum concentration which resulting maximal enzyme activity. The concentrations used were 5.0%; 7.5%; 10%; and 12.5% v|v. Fermentation was done at 30°C and agitation of 120 rpm. The highest enzyme activity of 12,640 Vlg protein was resulted at fermentation with inoculum concentration of 12.5% v|v at day-5. Application into fermentator two liters at temperature 30°C, aeration 1.5 vvm and agitation of 500 rpm showed enzyme production in earlier time (one day fermentation) to achievedenzyme activity of around 1000-1300 U|g protein.

AMOBILISASI ENZIM PENISILIN ASILASE SEL TRANSFORMAN ESCHERICHIA COLI SC 50 MENGGUNAKAN GEL POLIAKRILAMIDA S. Pudjiraharti; M. Wirahadikusumah
Jurnal Kimia Terapan Indonesia Vol 4, No 1 (1994)
Publisher : Research Center for Chemistry - LIPI

Results of study on the immobilization of dialysed fraction of penicillin acylase using various concentrations of acrylamide at BIS concentration 0,8 % are described. The study is an effort to increase the stability and efficiency of the enzyme use. The highest specific activity of the immobilized enzyme (1.38 U/mg protein) was found on immobilization using acrylamide 12.5 %. The penicillin acylase used in this study was obtained from the extraction of Escherichia coli Sc 50 cells. The optimum conditions of catalytic reaction of the enzyme were found 65°C and pH 7.00 both for immobilized and free enzymes. Theoptimum catalytic time was 230 minutes for the immobilized enzyme and 100 minutes for the free one. The immobilized enzyme was found more stable against pH, temperature changes, and storage at the experimental conditions and could be used five times repeatedly with remaining activity of 50 %. The Km value of free enzyme was 7.21 mM and the Vmax was 0.065 unol 6APA/mg protein/minute. Immobilization increased the Km value to 20.26 mM, and decreased Vmax to 0,033 unol 6-APA/mg protein/ minute. Phenylacetic acid was found to be a mixed inhibitor for penicillin acylase E. coli Sc 50 with the inhibition constants of Ki 720.31 mM and Ki' 504.31 mM. Immobilization decreased Ki to 176.58 mM and Ki' to 27.61 mM.

SOLASODINE STEROID BIOCONVERSION BY MYCOBACTERIUM PHLEI DSM 43286. S. Pudjiraharti; T. A. Budiwati; J. Kantasubrata; A. T. Karossi
Jurnal Kimia Terapan Indonesia Vol 2, No 1-2 (1992)
Publisher : Research Center for Chemistry - LIPI

Bioconversion of solasodine by Mycobacterium phlei DSM 43286 was conducted to obtain intermediate compounds which might be used as precursor in the production of steroidal drugs, i:e androst-4-en-3, 17-dione (AD) and androsta-l,4-diene-3,17-dione (ADD). M. phlei was firstly grown in nutrient broth medium at 37 °C for 8.5 hours with agitation of 200 rpm. The bacterial culture thus obtained was used as starter to inoculate the conversion medium containing 0,02% solasodine as the substrate and 0.01% 8-hydroxyquinoline as inhibitor. Bioconversion was conducted for 12 days at 37 °C using the same speed of agitation. Analysis of the bioconversion products was carried oUl using samples taken periodically at a 24-hour interval by TLC and HPLC methods. TLC analysis using chloroform-ethyl acetate (80:20) as eluent, measurement of the nuvamum wavelength and molar extinction coefficient value showed that AD and ADD was not found in the fermentation product,, but other intermediau: compound might the present. However, HPLC analysis of the fermentation products using Ik'Porasil column and benzene- ethylacetatechloroform (40:80:10) as eluent, showed -peaks with retention time similar to that of AD (during the 2nd - 9th day of incubation) and, ADD (during the 5th - 6th day offermentation) and, other unknown peaks.

Co-Authors A. T. Karossi J. Kantasubrata L. Z. Udin Linar Z. Udin M. Wirahadikusumah T. A. Budiwati

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