cover
Article Per Year (5 Year)
All
Home Page
OAI Link
Editorial Team
Contact
Reviewer
Google Scholar
Contact Name
-
Contact Email
-
Phone
-
Journal Mail Official
-
Editorial Address
-
Location
Kab. sleman,
Daerah istimewa yogyakarta
INDONESIA
Indonesian Journal of Chemistry
Published by Universitas Gadjah Mada
ISSN : 14119420     EISSN : 24601578     DOI : -
Core Subject : Science, Engineering,
Chemical Engineering, Chemistry & Bioengineering Chemistry
Indonesian Journal of Chemistry is an International, peer-reviewed, open access journal that publishes original research articles, review articles, as well as short communication in all areas of chemistry including applied chemistry. The journal is accredited by The Ministry of Research, Technology and Higher Education (RISTEKDIKTI) No : 21/E/KPT/2018 (in First Rank) and indexed in Scopus since 2012. Since 2018 (Volume 18), Indonesian Journal of Chemistry publish four issues (numbers) annually (February, May, August and November).
Arjuna Subject : -
Articles 25 Documents
 1   2   3 
Search results for , issue "Vol 9, No 1 (2009)" : 25 Documents clear
THE ISOTHERMIC ADSORPTION OF Pb(II), Cu(II) AND Cd(II) IONS ON Nannochloropsis sp ENCAPSULATED BY SILICA AQUAGEL Zipora Sembiring; Buhani Buhani; Suharso Suharso; Sumadi Sumadi
Indonesian Journal of Chemistry Vol 9, No 1 (2009)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (967.546 KB) | DOI: 10.22146/ijc.21556

Abstract

The research on the adsorption process of metal ions of Pb(II), Cu(II) and Cd(II) on Nannochloropsis sp biomass encapsulated by silica aquagel has successfully been done. The research was carried out in a series of experiments using batch method to obtain the capacity and adsorption energy values of the metal ions. The analysis of metal contents was done by atomic absorption spectrometry. The results showed that the adsorption capacities of Pb(II), Cu(II) and Cd(II) ions were 322.58; 0.033 and 0.0322 mmole/g adsorbent, respectively, at 27 °C and contact time of 30 min. The interaction between Pb(II), Cu(II) and Cd(II) ions and Nannochloropsis sp biomass encapsulated by silica aquagel is chemical interaction with the adsorption energy in the range of 20.55 - 22.70 kJ/mole.
METHYL MERCURY IN GREEN MUSCLE (Mytilus viridis L.) FROM FISH MARKET MUARA ANGKE : BEFORE AND AFTER COOKING Ermin K. Winarno; Winarti Andayani; Agustin Sumartono
Indonesian Journal of Chemistry Vol 9, No 1 (2009)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1170.265 KB) | DOI: 10.22146/ijc.21565

Abstract

The determination of methyl mercury content in green muscle (Mytilus viridis L.) that were taken from Pasar Pelelangan Ikan Muara Angke, Jakarta Bay has been carried out. Sampling was taken in November 2005 and March 2006, the samples were bought from the green muscle sellers. The aim of this research is to know the effect of cooking on the content of methyl mercury in green muscle. Samples were homogenized, weighed and washed with aceton and toluene. After washing, the homogenized material was added with HCl solution, extracted with toluene, then the methyl mercury content in toluene extract was analyzed using gas chromatography. The results of this research showed that methyl mercury concentration in raw and cooked green muscle respectively were 0.803 + 0.019 mg/g and 0.443 + 0.035 mg/g (in November 2005) and 0.096 + 0.014 mg/g and 0.079 + 0.016 mg/g (in March 2006) respectively. The methyl mercury content in raw (in November 2005) was higher than in cooked green muscle as permitted concentration in the sea biota by WHO and FAO, it is 0.5 ppm (mg/g), on the other hand the result of the second sampling in March 2006 showed that methyl mercury content in green muscle was lower than permitted concentration. Cooking process of the green muscle decreased methyl mercury content 44.85% (sampling in November 2005) and 17.71% (sampling in March 2006), because methyl mercury that bonded to protein were distributed to boiling water. Methyl mercury content in green muscle after cooking was still lower than the permitted concentration.
BIOSURFACTANTS PRODUCTION BY Pseudomonas aeruginosa USING SOYBEAN OIL AS SUBSTRATE Venty Suryanti; Sri Hastuti; Tutik Dwi Wahyuningsih; Mudasir Mudasir; Dina Ika Muliawati
Indonesian Journal of Chemistry Vol 9, No 1 (2009)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1183.444 KB) | DOI: 10.22146/ijc.21570

Abstract

Optimization condition of the biosurfactants production by P. aeruginosa using soybean oil as substrate has been examined. The media containing 10% v/v of the soybean oil and 6 days of the fermentation time was the optimum condition for the biosurfactants production. The extraction technique using different solvent polarity (n-hexane, chloroform, ethyl acetate and buthanol, respectively) was applied for the isolation of the biosurfactants. The biosurfactant was found in the extract chloroform of the crude biospasoy (biosurfactants obtained from soybean oil as substrate) which then is called chlo-biospasoy. The chlo-biospasoy was identified as rhamnolipids which had oil in water (o/w) emulsion type, had the CMC of 860 mg/L and could reduced the surface tension of the water from 72 mN/m to 52 mN/m. The chlo-biospasoy could be used as an emulsifier to form emulsion between water and hydrocarbon such as palm oil, benzene, premium or toluene with various stability. The results indicated that chlo-biospasoy could be used as an emulsifying and emulsion-stabilizing agent.
DOCKING STUDIES OF CURCUMIN AS A POTENTIAL LEAD COMPOUND TO DEVELOP NOVEL DIPEPTYDYL PEPTIDASE-4 INHIBITORS Enade Perdana Istyastono
Indonesian Journal of Chemistry Vol 9, No 1 (2009)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (962.362 KB) | DOI: 10.22146/ijc.21574

Abstract

Interaction of curcumin to dipeptydyl peptidase-4 (DPP-4) has been studied by employing docking method using Molecular Operating Environment (MOE) and AutoDock as the docking software applications. Although MOE can sample more conformational spaces that represent the original interaction poses than AutoDock, both softwares serve as valid and acceptable docking applications to study the interactions of small compound to DPP-4. The calculated free energy of binding (DGbinding)results from MOE and AutoDock shows that curcumin is needed to be optimized to reach similar or better DGbinding compare to the reference compound. Curcumin can be considered as a good lead compound in the development of new DPP-4 inhibitor. The results of these studies can serve as an initial effort of the further study.
INHIBITORY POTENTIAL OF SOME SYNTHETIC CINNAMIC ACID DERIVATIVES TOWARDS TYROSINASE ENZYME Lanny Hartanti; Henry Kurnia Setiawan
Indonesian Journal of Chemistry Vol 9, No 1 (2009)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1511.645 KB) | DOI: 10.22146/ijc.21579

Abstract

Cinnamic acid is one of known tyrosinase inhibitors. This study investigated the inhibition of tyrosinase activity of some cinnamic acid derivatives, i.e. 4-buthoxy-cinnamic acid, 4-n-butylcinnamic acid and 4-phenylcinnamic acid. Each inhibitor used in this research had the same type of inhibition towards enzymatic activity, i.e. mixed type inhibition of competitive and non competitive type. The potential sequence of tyrosinase inhibition based on the ratio of its IC50 compared to cinnamic acid, from the lowest to the highest were 4-buthoxycinnamic acid, 4-phenylcinnamic acid and 4-n-butylcinnamic acid. Based on the obtained results of this research, it was disclosed that n-butyl substituent on para position did not increase the inhibition effect of cinnamic acid towards tyrosinase enzymatic reaction. But in the other hand, buthoxy and phenyl substituent on para position could increase the inhibition effect of cinnamic acid towards tyrosinase enzymatic reaction because buthoxy substituent increased the similarity of its structure with the substrate of enzymatic reaction while phenyl susbtituent blocked the substrate-enzyme reaction.

Page 3 of 3 | Total Record : 25

 1   2   3 

Filter by Year

2009 2009


Reset
Filter By Issues
All Issue Vol 26, No 1 (2026) Vol 25, No 5 (2025) Vol 25, No 4 (2025) Vol 25, No 3 (2025) Vol 25, No 2 (2025) Vol 25, No 1 (2025) Vol 24, No 6 (2024) Vol 24, No 5 (2024) Vol 24, No 4 (2024) Vol 24, No 3 (2024) Vol 24, No 2 (2024) Vol 24, No 1 (2024) Vol 23, No 6 (2023) Vol 23, No 5 (2023) Vol 23, No 4 (2023) Vol 23, No 3 (2023) Vol 23, No 2 (2023) Vol 23, No 1 (2023) Vol 22, No 6 (2022) Vol 22, No 5 (2022) Vol 22, No 4 (2022) Vol 22, No 3 (2022) Vol 22, No 1 (2022) Vol 22, No 2 (2022) Vol 21, No 6 (2021) Vol 21, No 5 (2021) Vol 21, No 4 (2021) Vol 21, No 3 (2021) Vol 21, No 2 (2021) Vol 21, No 1 (2021) Vol 20, No 6 (2020) Vol 20, No 5 (2020) Vol 20, No 4 (2020) Vol 20, No 3 (2020) Vol 20, No 2 (2020) Vol 20, No 1 (2020) Vol 19, No 4 (2019) Vol 19, No 3 (2019) Vol 19, No 2 (2019) Vol 19, No 1 (2019) Vol 18, No 4 (2018) Vol 18, No 3 (2018) Vol 18, No 2 (2018) Vol 18, No 1 (2018) Vol 17, No 3 (2017) Vol 17, No 2 (2017) Vol 17, No 1 (2017) Vol 16, No 3 (2016) Vol 16, No 2 (2016) Vol 16, No 1 (2016) Vol 15, No 3 (2015) Vol 15, No 2 (2015) Vol 15, No 1 (2015) Vol 14, No 3 (2014) Vol 14, No 2 (2014) Vol 14, No 1 (2014) Vol 13, No 3 (2013) Vol 13, No 2 (2013) Vol 13, No 1 (2013) Vol 12, No 3 (2012) Vol 12, No 2 (2012) Vol 12, No 1 (2012) Vol 11, No 3 (2011) Vol 11, No 2 (2011) Vol 11, No 1 (2011) Vol 10, No 3 (2010) Vol 10, No 2 (2010) Vol 10, No 1 (2010) Vol 9, No 3 (2009) Vol 9, No 2 (2009) Vol 9, No 1 (2009) Vol 8, No 3 (2008) Vol 8, No 2 (2008) Vol 8, No 1 (2008) Vol 7, No 3 (2007) Vol 7, No 2 (2007) Vol 7, No 1 (2007) Vol 6, No 3 (2006) Vol 6, No 2 (2006) Vol 6, No 1 (2006) Vol 5, No 3 (2005) Vol 5, No 2 (2005) Vol 5, No 1 (2005) Vol 4, No 3 (2004) Vol 4, No 2 (2004) Vol 4, No 1 (2004) Vol 3, No 3 (2003) Vol 3, No 2 (2003) Vol 3, No 1 (2003) Vol 2, No 3 (2002) Vol 2, No 2 (2002) Vol 2, No 1 (2002) Vol 1, No 3 (2001) Vol 1, No 2 (2001) Vol 1, No 1 (2001) ARTICLE IN PRESS Article in press More Issue