Ari Asnani

Publications (10) View all

• Source

  Available from: Ari Asnani

  Article: Kajian Sifat Fisikokimia Ekstrak Rumput Laut Coklat Sargassum Duplicatum menggunakan Berbagai Pelarut dan Metode Ekstraksi

  Aisyah Tri Septiana, Ari Asnani
  [show abstract] [hide abstract]
  ABSTRACT: Sargassum duplicatum contain bioactive component has different polarity. The research was aimed to know the effect solvent types and extraction method toward the psychochemical characteristic of S. duplicatum extract. The result of qualitative analysis showed that all S. duplicatum extract samples contained flavonoid, tannin, saponin, and terpenoid. The best treatment were obtained from methanol treatment using one step extraction method that gave solubility in ethanol was 39.450 percent, solubility in distilled water (aquadest) was 28.283 percent, and total phenol was 297.170 mg/g
  J. Agrointek. 01/2012; 6(1):11-28.
• Conference Proceeding: Screening of Marine Actinomycetes From Segara Anakan Indonesia for Antimicrobial Activity

  Ari Asnani, Dini Ryandini
  The International Conference on Natural Sciences (ICONS) 2011, Batu, East Java, Indonesia; 07/2011
• Source

  Available from: Ari Asnani

  Article: ISOLASI DAN KARAKTERISASI PROTEASE ALKALIN DARI ISOLAT BAKTERI LIMBAH TERNAK DI EXFARM FAKULTAS PETERNAKAN UNSOED

  Zusfahair, Puji Lestari, Ari Asnani
  [show abstract] [hide abstract]
  ABSTRACT: Protease is one of the widely used enzymes for the industry. The potential resource of microorganism that produced protease is milk cow waste. In this research, isolation and characterization has been done toward isolated protease from milk cow waste of the Exfarm’s Animal Husbandry Faculty at University of Jenderal Soedirman, Purwokerto. The research used experiment method and the parameters observed were the genus of bacteria which produce protease and the activity of protease. The characterizations of protease were determination of optimum pH and temperature, the influence of metal ions, EDTA, surfactant, and commercial detergent toward enzyme activity, and also the study of enzyme stability. The results from the research showed that the isolated bacteria from the Exfarm’s of Animal Husbandry Faculty of UNSOED, which produced protease was Salmonella sp. Characterization of isolated Salmonella sp. from 45% ammonium sulphate fraction indicated that the optimum temperature was 50 ºC, optimum pH was 8, the enzyme was activated by Ca2+ dan Mg2+ ion, whereas it was inhibited by Zn2+, Cu2+ ions and EDTA. The addition of Tween-80 with the concentration of 0.2% and 0.4% increased protease activity, however the addition of Tween-80 with concentration higher than 0.6% decreased the protease activity. Enzyme protease from isolated Salmonella sp. was relatively stable with the addition of commercial detergent such as Attack, Surf, and Bukrim.
  Jurnal Ilmiah Kimia MOLEKUL. 01/2011; 6(1):46-56.
• Article: Synthesis of a BSA-Le(x) glycoconjugate and recognition of Le(x) analogues by the anti-Le(x) monoclonal antibody SH1: the identification of a non-cross reactive analogue.

  Jo-Wen Wang, Ari Asnani, France-Isabelle Auzanneau
  [show abstract] [hide abstract]
  ABSTRACT: A Le(x) trisaccharide functionalized with a cysteamine arm was prepared and this synthesis provided additional information on the reactivity of N-acetylglucosamine O-4 acceptors when they are glycosylated with trichloroacetimidate donors activated with excess BF(3)·OEt(2). In turn, this trisaccharide was conjugated to BSA lysine side chains through a squarate-mediated coupling. This BSA-Le(x) glycoconjugate displayed 35 Le(x) haptens per BSA molecule. The relative affinity of the anti-Le(x) monoclonal antibody SH1 for the Le(x) antigen and analogues of Le(x) in which the D-glucosamine, L-fucose or D-galactose residues were replaced with D-glucose, L-rhamnose and D-glucose, respectively, was measured by competitive ELISA experiments. While all analogues were weaker inhibitors than the Le(x) antigen, only the analogue of Le(x) in which the galactose residue was replaced by a glucose unit showed no binding to the SH1 mAb. To confirm that the reduced or loss of recognition of the Le(x) analogues by the anti-Le(x) mAb SH1 did not result from different conformations adopted by the analogues when compared to the native Le(x) antigen, we assessed the conformational behavior of all trisaccharides by a combination of stochastic searches and NMR experiments. Our results showed that, indeed, the analogues adopted the same stacked conformation as that identified for the Le(x) antigen. The identification of a trisaccharide analogue that does not cross-react with Le(x) but still retains the same conformation as Le(x) constitutes the first step to the design of a safe anti-cancer vaccine based on the dimeric Le(x) tumor associated carbohydrate antigen.
  Bioorganic & medicinal chemistry 10/2010; 18(20):7174-85. · 2.82 Impact Factor
• Source

  Available from: Ari Asnani

  Article: PEMBUATAN DEKSTRIN DARI PATI UBI KAYU MENGGUNAKAN ENZIM AMILASE DARI AZOSPIRILLUM sp. JG3 DAN KARAKTERISASINYA

  Dian Riana Ningsih, Ari Asnani, Amin Fatoni
  [show abstract] [hide abstract]
  ABSTRACT: Amylase enzyme is used to hydrolyze starch into simpler molecules such as dextrin. Amylase can be isolated from Azospirillum sp. JG3 bacteria. The purpose of this study was to characterize dextrins from cassava starch (Manihot esculenta) is catalyzed by the enzyme amylase from Azospirillum sp. JG3 bacteria. Stages of this study are: determination of optimum substrat and to analyze the chemical and physical dextrins including moisture content, ash content, dexstrosa equivalent (DE) and the yield obtained. The result of this research showed that optimum condition hydrolysis starch of cassava that using amylase from Azospirillium sp. JG3 bacteria was acquired at substrate concentration 3% and the results of analysis obtained dextrins include yield of 96.67%, water content of 9.39%, 0.25% ash content and dexstrosa equivalent (DE) of 16.55.
  Jurnal Ilmiah Kimia MOLEKUL. 01/2010; 5(1):15-21.