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All Journal HAYATI Journal of Biosciences Jurnal Ilmu dan Teknologi Kelautan Tropis Buletin Kimia VALENSI CAKRA KIMIA (Indonesian E-Journal of Applied Chemistry) JURNAL KIMIA SAINS DAN APLIKASI Current Biochemistry Journal The Journal of Pure and Applied Chemistry Research Jurnal Riset Kimia JSDH BERITA BIOLOGI BIOMA Indonesian Journal of Chemistry EKOLOGIA : Jurnal Ilmiah Ilmu Dasar dan Lingkungan Hidup Menara Perkebunan JURNAL ILMU KEFARMASIAN INDONESIA Jurnal Jamu Indonesia Indonesian Journal of Applied Research (IJAR) Jurnal Pusat Inovasi Masyarakat (JPIM)
LAKSMI AMBARSARI
Department Of Biochemistry, Faculty Of Mathematics And Natural Sciences, IPB University, Bogor, Indonesia
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Computer Science & IT Decision Sciences, Operations Research & Management Earth & Planetary Sciences Education Electrical & Electronics Engineering Engineering Environmental Science Immunology & microbiology Library & Information Science Materials Science & Nanotechnology Mathematics Medicine & Pharmacology Social Sciences Other

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AMPLIFIKASI GEN 16S-rRNA BAKTERI TERMOFILIK DARI SUMBER AIR PANAS, GUNUNG PANCAR BOGOR -, Suryani; Ambarsari, Laksmi; Harahap, Efi Sanfitri
Jurnal Riset Kimia Vol 3, No 1 (2009): September
Publisher : Universitas Andalas

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.25077/jrk.v3i1.97

Abstract

 ABSTRACT Exploration of thermophilic bacteria that produce thermostable enzyme is most useful in application for enzyme base industrial. The aim of of this research is to isolate and amplificate the 16S-rRNA gene from thermophilic bacteria isolate at hotspring, Mount of Pancar, Bogor. The research steps consist of bacteria isolation, chromosomal DNA extraction, and amplification of 16S-rRNA gene. The water sample as source for bacteria was collected from four cauldrons. Temperature and pH for each cauldron are red cauldron 75-80°C, pH 7; black cauldron 55°C, pH 7; white cauldron 57°C, pH 7; and saline cauldron 25°C, pH 6, respectively. The bacteria were cultivated at Luria Bertani (LB) and Thermus media. The chromosomal DNA have been extracted. Gene amplification of 16 S-rRNA have been carried out by using universal primer (Bac F1 and Uni B1). The size of amplicon is ± 1.5kb. Keywords : thermophilic bacteria, chromosomal DNA extraction, amplification of 16S-rRNA gene
KARAKTERISASI ß-1,3-1,4-GLUKANASEBAKTERI ENDOFITIK BURKHOLDERIA CEPACIA ISOLATE76 ASAL TANAMAN PADI Manzila, Ifa; Priyatno, Tri Puji; Fathin, Muhammad Faris; Ambarsari, Laksmi; Suryadi, Yadi; Samudera, I Made; Susilowati, Dwi Ningsih
BERITA BIOLOGI Vol 14, No 2 (2015)
Publisher : Research Center for Biology-Indonesian Institute of Sciences

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/beritabiologi.v14i2.1819

Abstract

Pathogenic fungus is one of the constraints to increase crop production. Chemical control using fungicides caused negative effects either to the environment or increased pathogen resistance to fungicide. Biological control using microbial-producing ß glucanase is an alternative method to inhibit the growth of pathogenic fungus. The aim of this study was to characterize ß-1,3-1,4-glucanase produced by rice endophytic bacterium, B. cepacia E76. Purification was carried out by ammonium sulphate precipitation, dialysis, and ion exchange chromatography using DEAE sepharose Fast Flow. A further characteristic of the enzyme activity was studied using oatmeal-glucan substrate.Results showed that precipitation using saturated 80% ammonium sulphate generated a good yield with the purity increased by 11 fold and yield of 66%.After chromatography step, the ß-1,3-1,4-glucanase of B. cepacia was successfully purified with an increasedof purity up to 33 fold and yield of 4%. Based on 10% SDS-PAGE, the enzyme profiles had the molecular weight of 15, 48 and 55 kDa.Of the three isozymes, only the 48 kDa isozyme showed the strongest glucanase activity when grown on media containing glucan as substrate.
Bioflocculant producing-bacteria from tapioca waste water were characterized. Two bacterial isolates i.e. LT-5 and LT-6 isolates had high flocculation activity, with activity of 68.92 and 71.38% respectively. The flocculation activity of LT-5 isolate increased at pH 2.0-4.0 (acidic condition), however the activity of LT-6 increased at pH 6.0-8.0 (neutral). Addition of 0.05% of AlCl3 as cation was the most effective and had important role in flocculation activity. Based on the morphological prope . SURYANI; LAKSMI AMBARSARI; I MADE ARTIKA; HARTUTIK EKA SUSANTI
HAYATI Journal of Biosciences Vol. 18 No. 4 (2011): December 2011
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.18.4.193

Abstract

Bioflocculant producing-bacteria from tapioca waste water were characterized. Two bacterial isolates i.e. LT-5 and LT-6 isolates had high flocculation activity, with activity of 68.92 and 71.38% respectively. The flocculation activity of LT-5 isolate increased at pH 2.0-4.0 (acidic condition), however the activity of LT-6 increased at pH 6.0-8.0 (neutral). Addition of 0.05% of AlCl3 as cation was the most effective and had important role in flocculation activity. Based on the morphological properties, LT-5 isolate was identified as Chromobacterium violaceum and LT-6 isolate was identified as Citrobacter koseri.
Structure Identification and Quality Assessment of Laccase (Lac InaCC) from Neurospora crassa by Using a Structure Prediction Rini Kurniasih; Laksmi Ambarsari; Setyanto Tri Wahyudi
HAYATI Journal of Biosciences Vol. 28 No. 1 (2021): January 2021
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.28.1.1

Abstract

Laccases are multi-copper oxidase enzyme, developed for being applied widely. The laccase gene in this study was isolated from local isolates of Neurospora crassa (LAC inaCC). The structure of this enzyme has not been known and there is no laccase structure of Neurospora crassa based on protein structure development in database. Here, we aimed to analyze the characteristics of the sequence and prediction structure, the structure quality after refinement through the molecular dynamics (MD) simulation method. LAC inaCC has been identified with typical sequence motifs (HWH, HSH, HXXH) which played role in copper-binding on 274(HWH)G-DG-T-CP on CBL-1, 314GT-WY(HSH)FS-QYG-G on CBL-2, and 607HPIHL on CBL-3. The four copper atoms have an important role in the catalytic activity. LAC inaCC is a multi-subunit enzyme consisted of three functional domains with structural motifs of Greek-key β barrel which is typical structure motif. Refinement in the prediction structure through the MD simulation showed that this method was proven to be able to improve the structure quality. The increase on the most favoured area on Ramachandran plot, clashcore percentile score, and molprobity score showed that the laccase structure headed to conformation change, to be more stable conformation with better resolution compared to earlier prediction structure.
Children’s Opinion on Vegetables Consumption: A Qualitative Study on School-Agers in City of Semarang Akhmad Endang Zainal Hasan; Laksmi Ambarsari; Karichsa Hariana
Indonesian Journal of Applied Research (IJAR) Vol. 2 No. 2 (2021): Indonesian Journal of Applied Research (IJAR)
Publisher : Universitas Djuanda

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.30997/ijar.v2i2.129

Abstract

Dates is fruit of palm trees that mostly grow in the Middle East. Dates contain phenolic acids and flavonoids that have antioxidants and potentially inhibit the ability of xanthine oxidase. The purpose of this research to determine the molecular interactions of xanthine oxidase by ligand of phenolic acids and flavonoids to inhibiting the production of uric acid. This research was conducted by site directed docking method. The size of the center of retardation used in this research is x = 26.569, y = 9.985, and z = 113.088 and the retardation volume of x = 14, y = 14, and z = 16. Inhibition by flavonoid and phenolic acid compounds has produces good inhibition strength shown by Gibbs free energy which is negative. The compound with the highest Gibbs free energy value is the anthocyanins compound which is -7.3 kCal / mol, the value is higher than the comparator ligand, allopurinol. Based on the bond analysis that is formed, the best compound in inhibiting xanthine oxidase is syringic acid.
Isolation and Characterization of Dextransucrase from Bacterial Isolate Sugar Cane A.E. Zainal Hasan; Laksmi Ambarsari; . Hasim; Aisyah Girindra
Indonesian Chemistry Letter Vol 1 No 1 (2001): Buletin Kimia
Publisher : Department of Chemistry

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (849.776 KB) | DOI: 10.29244/bk.1.1.1-6

Abstract

Dextransucrase is a glucasyltransferase that catalyzes the transfer of an alpha-D-glucopyranosyl group from sucrose to dextran and releasing the fructose. Enzyme activity was determined by measuring the initial reaction rate of fructose released from sucrose. A standard unit (U) is defined as the amount of enzyme that catalyzes the formation of 1 umol of D-fructose per mg of protein per minute. Dextransucrase was produced by fed-bath cultures of isolate bacterial from sugar cane in a mixture containing sucrose (10 % b/v) in themedium fermentation. Extracellular dextransucrase was obtained from bacterial isolate from sugar cane. Final culturedextransucrase activity was 0,2776 Ulmg of protein. Dextransucrase purified by ethanol 80 % showed activity of 4,2077 Ulmg of protein or activity increase 1515,75 %. Temperature optimum was 40 OC and pH optimum was 7.6. All of the metal increased the activity, except HgC12. Dectransucrase kinetics constants, Km is 3,00 mM and Vmaks is 3,5559 unit/mg of proteinlmin. Molecular weight is 95.155 kDa.
Characteristics of Glucose Oxidase Gene (GGOx) from Aspergillus niger IPBCC 08.610 Popi Asri Kurniatin; Laksmi Ambarsari; Annisa Dhiya Athiyyah Khanza; Inda Setyawati; Djarot Sasongko Hami Seno; Waras Nurcholis
Jurnal Kimia Valensi Jurnal Kimia VALENSI Volume 6, No. 1, May 2020
Publisher : Syarif Hidayatullah State Islamic University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (763.755 KB) | DOI: 10.15408/jkv.v6i1.9440

Abstract

Glucose oxidase is used in various industries for the development of enzymatic fuel cell. Based on prior studies, this compound is sourced from the local isolates of Aspergillus niger IPBCC 08.610, although investigations on the encoding gene have not been conducted. The purpose of this research, therefore, is to identify and characterized the gene responsible for encoding glucose oxidase, in the aspect of sequence, length, and restriction patterns. This experiment involved the amplification of genomic DNA using specific primers for gene recognition, which was followed by the restriction technique with EcoRI and PstI endonucleases. Furthermore, the gene is inserted into vector pGEM®T-Easy and transformed into competent E. coli DH5α cells, in an attempt to perform sequencing. The glucose oxidase gene from A. niger IPBCC 08.610 was confirmed to possess a size of 1848 bp, and a GC content of 57.8%, with a possibility of restriction into two fragments of size 908 bp and 980 bp, using the EcoRI restriction.
In Silico Analysis of Glucose Oxidase H516r and H516d Mutations for an Enzymatic Fuel Cell Puspa Julistia Puspita; Laksmi Ambarsari; Adrian Adiva; Tony Ibnu Sumaryada
Jurnal Kimia Valensi Jurnal Kimia VALENSI Volume 7, No. 2, November 2021
Publisher : Syarif Hidayatullah State Islamic University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15408/jkv.v7i2.20733

Abstract

Glucose oxidase (GOx) is an oxido-reductase enzyme that catalyzes glucose into hydrogen peroxide and glucono delta-lactone (GDL). GOx has the potential to be used in the medical field. Numerous research concerning the usage of GOx to create enzymatic biofuel cells have been done, nevertheless the results obtained have not been optimal. This research aims to increase the Km values of GOx in order to increase its potential as a material for an enzymatic fuel cell. The amino acid histidine in position 516 is a residue in the active site that plays an important part in the process of glucose oxidation. In this research we mutated H516 by in silico twice resulting in the mutants R516 and D516. The mutations resulted in a change of the docking area for both mutants and in the docking affinity for H516D resulting in higher Km values. This shows that the H516 residue plays an important part in the functions of glucose oxidase and mutation into aspartate could improve glucose oxidase based enzymatic fuel cells.
Bioethanol Production by Using Detoxified Sugarcane Bagasse Hydrolysate and Adapted Culture of Candida tropicalis Inda Setyawati; Laksmi Ambarsari; Siti Nur'aeni; Suryani Suryani; Puspa Julistia Puspita; Popi Asri Kurniatin; Waras Nurcholis
Current Biochemistry Vol. 2 No. 1 (2015)
Publisher : IPB University

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

Ethanol is considered as the most promising alternative fuel, since it can be produced from a variety of agriculturally-based renewable materials, such as sugarcane bagasse. Lignocellulose as a major component of sugarcane bagasse is considered as an attractive renewable resource for ethanol production due to its great availability and relatively low cost. The major problem of lignocellulose is caused by its need for treatment to be hydrolyzed to simple sugar before being used for bioethanol production. However, pretreatment using acid as hydrolyzing agent creates some inhibitor compounds that reduce ethanol production because these compounds are potential fermentation inhibitors and affect the growth rate of the yeast. Reduction of these by-products requires a conditioning (detoxification and culture starter adaptation). Thus, the aim of this study was to evaluate bioethanol production by fermentation with and without detoxified sugarcane bagasse acid hydrolysate using adapted and non-adapted culture of C. tropicalis. According to this study, the highest ethanol amount was obtained about 0.43 % (v/v) with an ethanol yield of 2.51 % and theoretical yield of 4.92 % by fermentation of sugarcane bagasse hydrolysate with detoxification using the adapted strain of C. tropicalis at 72 hours fermentation time. Furthermore, the addition of 3 % glucose as co-substrate on detoxified-hydrolysate media only achieved the highest ethanol concentration 0.21 % after 24 hours fermentation with the ethanol yield 0.69 % and theoretical ethanol yield 1.35 %, thus it can be concluded that the addition of glucose could not increase the ethanol production.
The Addition Effects of Glucose as a Co-substrate on Xylitol Production by Candida guilliermondii Laksmi Ambarsari; Suryani Suryani; Steffanus Gozales; Puspa Julistia Puspita
Current Biochemistry Vol. 2 No. 1 (2015)
Publisher : IPB University

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

High cost production is one of the constraints of the commercial xylitol production due to high energy needed and pure raw materials. Therefore, it is necessary to improve the xylitol production eficiently with lower production cost by using microorganisms. The research objectives were to determine the optimum xylitol production from xylose by metabolism of C. guilliermondii and effect of glucose as a co-substrate in fermentation medium. The ratio of glucose : xylose (g/L) was 1:25, 1:12, 1:5 and 1:2.5 respectively. The xylitol concentration was measured by spectrophotometer method (D-sorbytol/D-xylitol kit). The result showed that the exponential phase of Candida guilliermondii was 12 h to 36 of incubation and optimum of incubation time to produce the highest xylitol was 72 h. The best ratio- of glucose : xylose to produce xylitol was 9 g/L glucose : 45 g/L xylose (1 : 5). The xylitol concentration produced from medium with the addition of glucose was 2.85 g/L. This concentration increased five times compared to that in the medium without addition of glucose that only reached 2.85 g/L. According to this study, the addition of glucose as a co-substrate could increase the xylitol production.
Co-Authors -, Suryani . SURYANI A.E. Zainal Hasan Ade Heri Mulyati Adrian Adiva Adriansyah Nanda Putra Agung Isnanto Agustina L.N. Aminin Ahmad Irvan Pratama Aisyah Girindra Akhiruddin Maddu Akhmad Endang Zainal Hasan Alifia Mutiara Annisa Anja Meryandini Annisa Dhiya Athiyyah Khanza Aqilah, Rifany Fairuz Arwansyah Arwansyah Arwansyah Arwansyah, Arwansyah Assifah Eryandini Azhari, Muhammad Alwin Azzara Putri Elvaza Chelsea Chelsea, Chelsea Chelsy Narita Choirunnisa Miftahul Jannah Deki Geraldi Diana Widiastuti Djarot Sasongko Hami Seno DWI NINGSIH SUSILOWATI DWI NINGSIH SUSILOWATI Dwi SUBIYARTI Dwiningsih Susilowati Dyah Utami Cahyaning Rahayu Edy Djauhari Purwakusumah Edy Djauhari Purwakusumah Efi Sanfitri Harahap Faliha Arinda Lestari Farhan Azhwin Maulana Fathin, Muhammad Faris Febrianti, Riska G Jeni christi A Genta Asvarhoza GIA PERMASKU Giovanny, Lisa Gustini Syahbirin H. M. Mochtar Hanhan Dianhar Harahap, Efi Sanfitri HARTUTIK EKA SUSANTI Hasim - Hayati Minarsih Heri Purwoto Hidayat, Radika Evita Husnawati Husnawati Husnawati Husnawati I MADE ARTIKA I Made Artika I Made Samudera I Made Samudera, I Made I MADE SAMUDRA Ifa Manzila Ifa Manzila Ika Yuni Astutik Ika Yuni Astutik, Ika Yuni Ike Wahyuni Putri Imron RIYADI INAYAH NOER MAZIDAH Inda Setyawati, Inda Irma Rahmayani Isnanto, Agung Jaya Hardi Karichsa Hariana Latifah K Darusman Lestari, Faliha Arinda Lisa Giovanny Made Suhandana Marfira, Nurul MEGA SAFITHRI Muhamad Rifai Muhammad Alwin Azhari Muhammad Faris Fathin Muhammad Halim Mustika Luthfia Mustika Permatasari Ni Putu Peggy Liliyani Novia Winarti Nur Qadri Rasyid Nurul Marfira Okta Vino Pratama, Ahmad Irvan Purwantiningsih Sugita Puspa Julistia Puspita Puspa Julistia Puspita Putri, Ike Wahyuni Radika Evita Hidayah Ridho Pratama Rifany Fairuz Aqilah Riki Riki Riksa Nur Wahyuni Rini Kurniasih Rini Kurniasih Rini Novita Riska Febrianti Sarmila Sarmila Setyanto Tri Wahyudi Shobiroh Nuur' Alimah Siti Nur'aeni Siti Warnasih Soekarno Mismana Putra Steffanus Gozales Sumaryada, Tony Suryani - Suryani Suryani Syamsul Falah TATI NURHAYATI Tirta Setiawan Trah Yudha Tri Puji Priyatno Tri Puji Priyatno Uswatun Hasanah Wahyuni, Riksa Nur Wanda Hamidah Waras Nurcholis Yadi Suryadi Yadi Suryadi Zuniar Subastian