Garuda - Garba Rujukan Digital

All

Jurnal Kimia Terapan Indonesia

InaJAC
Website

Published by Lembaga Ilmu Pengetahuan Indonesia

ISSN : 08532788 EISSN : 25277669 DOI : -

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

Arjuna Subject : -

Articles 9 Documents

Search results for , issue "Vol 4, No 1 (1994)" : 9 Documents clear

DAYA INHIBISI TRIPSIN BEBERAPA EKSTRAK TANAMAN SUKU LEGUMINOSA Sri Hartati; Hadiman Hadiman
Jurnal Kimia Terapan Indonesia Vol 4, No 1 (1994)
Publisher : Research Center for Chemistry - LIPI

In search of potensial protease inhibitor, especially those which inhibit trypsin activity, preliminary screening of some plant extracts of Legumlnoceae family has been carried out. From 9 (nine) plant extracts examined, those which gave potential enzyme inhibition, were leaf and bark extracts of Caesalpinia pulcherima, and Caliandra chaemotocepala, and bark extract of Delonic regia, Leucaena glauca, and Sesbanla grandlflora . Thin layer chromatographic analysis of the leaf and barkextracts of the plants considered to have the most potensial inhibitor activity indicated that the active principles were of peptide and polyphenollc compounds.

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

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.

ISOLASI GENISTEIN DARI TEMPE SECARA KROMATOGRAFI Wuryani Wuryani
Jurnal Kimia Terapan Indonesia Vol 4, No 1 (1994)
Publisher : Research Center for Chemistry - LIPI

The presence of genisteln in tempe (fermented soybean) could be detected by using various chromatographic techniques, such as Thin-Layer, Column and High Pressure Liquid Chromatography. In this experiment, TLC was chosen for the isolation and purification of genistein from tempe. Spectrophotometry, Mass Spectrometry, spraying with chromogenic reagents and hydro- lysis were carried out for identifying genistein. Quantification was carried out spectrophotometrlcally and it was shown that the laboratory prepared tempe (l00 g) contained 13.80 mg ofgenisteln.

COMPUTER-ASSISTED STRUCTURE ELUCIDATION OF HUMULENE EPOXIDE AND CARYOPHYLLENE EPOXIDE MIXTURE OF TURRAEA BROWNII Tahid Tahid; J. D. Connolly
Jurnal Kimia Terapan Indonesia Vol 4, No 1 (1994)
Publisher : Research Center for Chemistry - LIPI

An experiment was carried out to isolate active material from Turraea brownli for biological insectislde. The isolated component obtained by using TLC was elucidated with iH NMR, and 13C NMR techniques. It was found that the compound was unknown triterpenoid (C30H48O). Further elucidation using 2D NMR with COSY, HMBC, and HMQC combined with computer techniques showed that the component was an approximately equimolar mixture of two sesqulterpenes (C15H24O) which were identified as humulene epoxide and B-caryophyllene epoxide.

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

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%.

THE INFLUENCE OF CATALYST AND FEEDSTOCK ON PRODUCT DISTRIBUTIONS FOR CRACKING OF c8 PARAFFINS ON HY AND HZSM-5 ZEOLITES Zainurlis Zainuddin
Jurnal Kimia Terapan Indonesia Vol 4, No 1 (1994)
Publisher : Research Center for Chemistry - LIPI

Catalytic cracking of n-octane and 2-methylheptane, as well as mixtures of these paraffins, has been studied on HY and HZSAI-5 zeolites, and also on combinations of the catalysts. For cracking on individual zeolites, both feedstock and catalyst influence the resulting product distributions. For all feedstocks, product distributions are shifted towards smaller fragments for reaction on HZSM-5 compared to HY. Ratios of branched to linear paraffins are much more strongly influenced by catalyst type and feedstock than the corresponding ratios for olefinic products. For reactions on catalyst mixtures, distributions of the Iota I products by carbon number correspond well to a summation of contributions on the individual catalysts. However, a greater departure from prediction is seen for individual distributions of paraffins, olefins and aromatics, as well as for ratios of branched 10 lineal' paraffins, showing that hydrogen transfer processes and isomerization must occur. The addition of pentasil has also resulted in enrichment of the linear saturates at 101-,'ercarbon number which is due to preferential cracking of linear paraffins over the branched isomers.

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.

CHARACTERIZATION OF RUBBER-MODIFIED POLYPROPYLENE Nuri Astrini; E. L. Bedia; A. Sudarisrman
Jurnal Kimia Terapan Indonesia Vol 4, No 1 (1994)
Publisher : Research Center for Chemistry - LIPI

Blending of 10, 20, 30, 40, and 50% ethylene-propylene random copolymer known as EPM with polypropylene (PP) was conducted and the blends were characterized using wide-angle x-ray scattering (WAXS), differential scanning calorimetry (DSC), scanning electron microscope (SEM), Tensile and Impact tester. As shown in WAXS diffractograms, PP retains its crystalline structure when blended with EPM. DSC analysis suggests that the polymer blend consists of two phase systems, one crystalline and one amorphous. Morphological observation of the polymer blend using SEM shows that the EPA-f globular structure cavitates the PP matrix which further indicates that the polymer blend is only partially compatible. As EPM increases, the tensile yield stress, stress-strain curve and modulus of elasticity decrease. Impact strength on the other hand, increases and showed remarkable effect at 30% EPM - 70% PP.

FERMENTASI ALFA AMILASE DARI ASPERGILLUS ORYZAE PADA MEDIA SAGU METROXYLON Yetti M. Iskandar; Dine Agustine; A. Sidik; Linar Z.Udin; A. T. Karossi
Jurnal Kimia Terapan Indonesia Vol 4, No 1 (1994)
Publisher : Research Center for Chemistry - LIPI

Alpha amylase is an extracellular enzyme which can be obtained from Aspergillus oryzae fermentation. The production of the alpha amylase in fermentation of sago starch media (Metroxylon sp)in 600, 800 and 1500 ml scale at 30°C for 7 to 9 days in aerobic condition has been conducted. The observations at day-3 indicated that the maximum enzyme specific activity assayed at 40°C for 30 minutes incubation, was 1096 U/g protein, 963 U/g protein and 810 U/g protein for 600, 800 and 1500 ml scale respectively. At this condition starch utilization for growth reached 69% for the 600 and 800 ml scale and 71% for the 1500 ml scale and the biomass production was 6.03 g dry weight/L media, 4.03 g dry weight/L media and 5.66% g dry weight/L media for the 600, 800 and 1500 ml scale respectively.

Page 1 of 1 | Total Record : 9

Filter by Year

1994 1994

Filter By Issues

All Issue Vol 24, No 1 (2022): Jurnal Kimia Terapan Indonesia Vol 23, No 2 (2021): Jurnal Kimia Terapan Indonesia Vol 23, No 1 (2021) Vol 22, No 1 (2020) Vol 21, No 2 (2020) Vol 21, No 1 (2019) Vol 20, No 2 (2018) Vol 20, No 1 (2018) Vol 19, No 2 (2017) Vol 19, No 1 (2017) Vol 18, No 02 (2016) Vol 18, No 01 (2016) Vol 17, No 2 (2015) Vol 17, No 1 (2015) Vol 16, No 2 (2014) Vol 16, No 1 (2014) Vol 15, No 2 (2013) Vol 15, No 1 (2013) Vol 14, No 2 (2012) Vol 14, No 1 (2012) Vol 13, No 2 (2011) Vol 13, No 1 (2011) Vol 12, No 2 (2010) Vol 12, No 1 (2010) Vol 11, No 2 (2009) Vol 11, No 1 (2009) Vol 10, No 1-2 (2000) Vol 9, No 1-2 (1999) Vol 8, No 1-2 (1998) Vol 7, No 1-2 (1997) Vol 6, No 1-2 (1996) Vol 5, No 1 (1995) Vol 4, No 2 (1994) Vol 4, No 1 (1994) Vol 3, No 2 (1993) Vol 3, No 1 (1993) Vol 2, No 1-2 (1992) Vol 1, No 2 (1991) Vol 1, No 1 (1991) More Issue

Home Page

OAI Link

Editorial Team

Contact

Reviewer

Google Scholar

Contact Name
-

Contact Email
-

Phone
-

Journal Mail Official
-

Editorial Address
-

Location
Kota adm. jakarta selatan,

Dki jakarta

INDONESIA

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Home Page

OAI Link

Editorial Team

Contact

Reviewer

Google Scholar

Contact Name -

Contact Email -

Phone -

Journal Mail Official -

Editorial Address -

Location Kota adm. jakarta selatan, Dki jakarta INDONESIA

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Contact Name
-

Contact Email
-

Phone
-

Journal Mail Official
-

Editorial Address
-

Location
Kota adm. jakarta selatan,

Dki jakarta

INDONESIA