Klon Gen Penisilin Asilase Pada Cosmid Phc79

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

Effects of Medium Composition on Oxytetracycline Production by Streptomyces Rimosus Atcc 33022

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 PROTEASE ALKALI DAN KERATINASE DARI Brevibacillus agri A-03 TERMOFILIK

 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  

Pemurnian Glukoamilase Dari Hasil Fermentasi Kapang Rhizopus Oryzae

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%

In Silico Screening and Designing Synthesis of Cinchona Alkaloids Derivatives as Potential Anticancer

P-glycoprotein (P-gp) resistance in cancer cells decreases intracellular accumulation of various anticancer drugs. This multidrug resistance (MDR) protein can be modulated by a number of non-cytotoxic drugs. We have screened 30 chincona alkaloids derivatives as a potent P-gp inhibitor agent in silico. Hereby, we report the highest potential inhibitions of P-gp is Cinchonidine isobutanoate through molecular docking approach. with affinity energy -8.6 kcal/mol and inhibition constant, Ki is 4.89 x 10-7 M. Cinchonidine isobutanoate is also known has molecular weight below 500, Log P value 3.5, which is indicated violation free of Lipinski`s rule of five. Thus, Cinchonidine isobutanoate is the most potent compound as anticancer compare to other Cinchona alkaloids. Ultimately, we design Cinchonidine isobutanoate for further lead synthesis by using DBSA, act as a combined Brønsted acid-surfactant-catalyst (BASC) to obtain high concentration of organic product by forming micellar aggregates which is very powerful catalytic application in water environment