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All Journal International Journal of Renewable Energy Development JURNAL KIMIA SAINS DAN APLIKASI Microbiology Indonesia Jurnal Matematika & Sains Journal of Mathematical and Fundamental Sciences Journal of Engineering and Technological Sciences Jurnal Kimia Riset Berkala Penelitian Hayati International Journal of Renewable Energy Development Bencoolen Journal of Pharmacy
. AKHMALOKA
Institut Teknologi Bandung
Agriculture, Biological Sciences & Forestry Astronomy Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Control & Systems Engineering Earth & Planetary Sciences Electrical & Electronics Engineering Energy Engineering Health Professions Immunology & microbiology Materials Science & Nanotechnology Mathematics Medicine & Pharmacology Nursing Physics Public Health

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ANALISIS 6 DNA REKOMBINAN DENGAN ENZIM EcoR1 Ni Nyoman Tri Puspaningsih; Akhmaloka; Afaf Baktir; Ami Soewandi J.S.; Y. Sriwulan M.
JURNAL PENELITIAN BIOLOGI BERKALA PENELITIAN HAYATI Vol 3 No 1 (1997): June 1997
Publisher : The East Java Biological Society

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.23869/490

Abstract

Amylase enzyme from Endomycopsis fibuligera capable to hidrolize starch into glucose. Insertion of amylase gene from Endomycopsis fibuligera into yeast (Saccharomyces cereviceae) will be able to increase the function of yeast (S.cereviceae) to digest more cheaper substrate, like starch. Before cloning in yeast, recombinant DNA will be made and analyzed in Escherichia coli strain DH5a. The result showed that the sixth transformant consist recombinant DNA that were sensitive to tetracycline medium. Analysis by EcoR1 digestion showed that the size of insertion fragment into Ycp 50 vector are around 0.3 untill 16 kb.
ISOLASI KARAKTERISASI DAN UJI EKSPRESI GEN ALP1 DI Escherichia coli DH5a Ni Nyoman Tri Puspaningsih; Akhmaloka; Sofyan Hadi; Y. Sri Wulan Manuhara; Bambang Irawan
JURNAL PENELITIAN BIOLOGI BERKALA PENELITIAN HAYATI Vol 4 No 2 (1999): June 1999
Publisher : The East Java Biological Society

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.23869/517

Abstract

Amylase gene (ALP1) insertion in YCp 50 cloning vector was detected by Direct Screening PCR. Result of Direct Screening PCR showed one transformants which assumed have amylase gene insert. Characterization of the recombinant DNA by Stu1 and EcoR1 restriction enzymes indicated nucleotide sequence of insert gene. Digestion by BamHI, Cla1, and EcoRV restriction enzymes showed only one band that assumed size of insert gene is about 1500 bp. Gene expression showed that amylase enzyme activity by using Somogyi-Nelson method was 88.0265 Unit. This activity was 10% higher than transformant control (Escherichia coli DH5a which content YCp50).
DNA Polimerase sebagai Model Kajian Biomolekul Enzim Termostabil Isolat Lokal Agustina L. N. Aminin; Akhmaloka Akhmaloka; Hendro Pramono
Jurnal Kimia Sains dan Aplikasi Vol 3, No 2 (2000): Volume 3 Issue 2 Year 2000
Publisher : Chemistry Department, Faculty of Sciences and Mathematics, Diponegoro University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (4090.218 KB) | DOI: 10.14710/jksa.3.2.79-84

Abstract

Ekstremozim merupakan bahan kajian penelitian yang banyak dilakukan dalam dekade terakhir. Enzim ini merupakan biokatalis yang sangat efektif digunakan dalam proses industri. Salah satu sumber ekstremozim yang cukup potensial adalah bakteri termofilik, tumbuh pada sumber air panas. Indonesia merupakan negara yang kaya akan sumber air panas, tetapi sampai saat ini belum banyak peneliti yang mengeksplorasi bakteri termofilik. Salah satu bakteri termofilik dari Cimanggu, suatu sumber air panas di sekitar Bandung yang memiliki suhu sekitar 80°C telah berhasil diisolasi. DNA polimerase dipilih sebagai enzim model untuk mempelajari struktur fungsi dari enzim termostabil. Kloning terhadap gen pengkode DNA polimerase dilakukan dengan pendekatan pustaka genom dan amplifikasi genom menggunakan teknik PCR. Primer dirancang berdasarkan homologi urutan nukleotida gen pengkode DNA polimerase dari Thermus aquaticus dan Thermus thermophilus. Primer P1-P3 mengamplifikasi empat fragmen berukuran 1 kb, 1,4 kb, 1,6 kb dan 1,8 kb yang tidak saling overlap. Dalam hal ini fragmen DNA 1 kb telah ditentukan urutan nukleotidanya.
Bioethanol Production from Sugarcane Bagasse Using Neurospora intermedia in an Airlift Bioreactor Elvi Restiawaty; Kindi Pyta Gani; Arinta Dewi; Linea Alfa Arina; Katarina Ika Kurniawati; Yogi Wibisono Budhi; Akhmaloka Akhmaloka
International Journal of Renewable Energy Development Vol 9, No 2 (2020): July 2020
Publisher : Center of Biomass & Renewable Energy, Diponegoro University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14710/ijred.9.2.247-253

Abstract

Bagasse as solid waste in sugarcane industry can be utilized as one of the potential raw materials in the bioprocess industry. This research aims to investigate the conversion of bagasse to bioethanol using simultaneous saccharification and fermentation in an airlift bioreactor. Neurospora intermedia was used as a biological agent that carried out the saccharification and fermentation of sugarcane bagasse simultaneously for bioethanol production. Cell morphology of N. intermedia in the form of pellet was required to provide free movement in the axial flow of airlift bioreactor. The medium pH strongly affects the morphological shape of N. intermedia. Therefore, the formation of good pellets of inoculum was observed under acidic conditions, i.e. pH 3.0 – 3.5. The effect of the initial concentration of nutrient on the inoculum growth was also investigated. Inoculums cultured in potato dextrose broth (PDB) medium with a half the strength of the common nutrient concentration of PDB qualitatively indicated good growth in terms of the size and density of cells. The inoculums with good morphological form were fed into the airlift bioreactor, which already contained a liquid medium with initial pH of 3.5 and also contained pre-treated bagasse. In experiments using the airlift bioreactor, the pre-treated bagasse was added to various nutrient concentrations of the PDB infusion medium. The highest bioethanol production from bagasse was monitored in the medium culture of half strength PDB infusion. The yield of bioethanol obtained from total sugarcane bagasse and PDB in an air lift bioreactor achieved approximately 40%, which has an infusion medium with a half-strength PDB and initial pH of 3.0. 
Cloning and Characterization of Gene Encoding Thermostable Enzyme from Domas Crater Siti Julia Asyifa; Akhmaloka; Suharti
BENCOOLEN JOURNAL OF PHARMACY Vol. 2 No. 2 (2022): Oktober
Publisher : UNIB PRESS

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.33369/bjp.v2i2.24361

Abstract

This research has been carried out an analysis of the gene encoding thermostable enzymes from natural samples of Domas Crater by using a metagenomic approach. The purpose of this study was to identify the gene encoded thermostable enzyme from natural samples of the Domas Crater. In this study, genes were amplified through random PCR technique from a collection of community DNA that had been isolated previously using a metagenomic approach. Random PCR of total community DNA produced DNA fragments with a size of about 1 kb, and then ligated to the pJET1.2/blunt vector and inserted into E. coli TOP10 for cloning process. The recombinant plasmid was then analysed using restriction enzymes BamHI and EcoRI to confirm the presence of the gene inserted in the cloning vector. Homology analysis of the DNA sequences of the cloned genes showed five groups of proteins that were similar to the ABC Transporter permease protein from archaea with an identity of about 76 – 96%. The grouping of these proteins is shown by the constructed phylogenetic tree.
3D STRUCTURE AND FUNCTION ANALYSIS OF RECOMBINANT ALDII PROTEIN FROM Uncultured Acidilobus sp. USING I-TASSER Meray, Nishia Waya; Suharti, Suharti; Akhmaloka, Akhmaloka
Jurnal Kimia Riset Vol. 9 No. 1 (2024): June
Publisher : Universitas Airlangga, Campus C Mulyorejo, Surabaya, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.20473/jkr.v9i1.56154

Abstract

The AldII protein is a new recombinant protein produced from a novel gene obtained via a metagenome approach. Previous studies showed that this protein is strong and has the same metal binding aspect as the class II Aldolase enzyme. Aldolase is a valuable enzyme used in pharmaceuticals, food processing, and biochemistry. Further investigation is required to comprehend the structure and function of the AldII protein due to its potential. Researchers will conduct sophisticated bioinformatic analysis on the 3D shape and function prediction of AldII using the I-TASSER webserver from Zhanglab. The AldII protein is a new recombinant protein produced from a novel gene obtained via a metagenome approach. Previous studies showed that this protein is strong and has the same metal binding aspect as the class II Aldolase enzyme. Aldolase is a valuable enzyme used in pharmaceuticals, food processing, and biochemistry. Further investigation is required to comprehend the structure and function of the AldII protein due to its potential. Researchers will conduct sophisticated bioinformatic analysis on the 3D shape and function prediction of AldII using the I-TASSER webserver from Zhanglab. The I-TASSER server is an online tool for the automated prediction of protein structure and annotation of functions based on structure. Analysis of the AldII protein using the I-TASSER webserver shows that this protein has a stable structure with the closest structural homology to deoxyribose-phosphate aldolase from Bacillus thuringiensis with PDB code 6btdA. Additionally, the biological structure analysis shows that this protein shares the biological function of the enzyme L-fuculose-1-phosphate aldolase, which is part of the class II Aldolase enzyme that plays a role in the catabolism of arabinose, L-Fuculose, and Rhamnose. The results align with prior research that states the AldII protein is a stable protein with a catalytic side that is homologous to the class II Aldolase enzyme.
Co-Authors A. Suharto A. Suharto AFAF BAKTIR Agustina L.N. Aminin Ami Soewandi J.S. Arina, Linea Alfa Arinta Dewi Bambang Irawan Dewi, Arinta Elvi Restiawaty F Madayanti, F F. M. Warganegara F. M. Warganegara F. Madayanti FIDA MADAYANTI Gani, Kindi Pyta Garaika H. Sutedjo Hadi Sutedjo Hendro Pramono Heni Yohandini I. N. Tika I. N. Tika Katarina Ika Kurniawati Kindi Pyta Gani Kurniawati, Katarina Ika L. Ambarsari Linea Alfa Arina M. R. Moeis M. Sindumarta Meray, Nishia Waya Ni Nyoman Tri Puspaningsih P Aditiawati P. E. Susilowati PINGKAN ADITIAWATI PRIMA ENDANG SUSILOWATI R. Hertadi RUKMAN HERTADI S. Nurbaiti S. Nurbaiti Safika S, Safika Senam Senam Siti Julia Asyifa Sofyan Hadi Suharti Suharti Suharti Y. Sri Wulan Manuhara Y. Sriwulan M. Yogi Wibisono Budhi