Claim Missing Document
Check
Articles

Found 4 Documents
Search
Journal : VALENSI

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.
Cloning of the GOX-Xho Gene IPBCC 08.610 into Plasmid pTA2 and Its Characterization Aryani, Hanifah; Akbar, Nadhira Fathiaz; Fuad, Asrul Muhamad; Ambarsari, Laksmi; Kurniatin, Popi Asri
Jurnal Kimia Valensi Jurnal Kimia VALENSI, Volume 10, No. 2, November 2024
Publisher : Syarif Hidayatullah State Islamic University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15408/jkv.v10i2.39602

Abstract

Glucose oxidase (GOX) from Aspergillus niger catalyzes the oxidation of β-D-glucose to δ-gluconolactone and hydrogen peroxide, making it valuable for industrial applications. Intracellular GOX exhibits higher activity than its extracellular counterpart. This study focuses on enhancing the extracellular production of GOX through recombinant DNA technology. This study aimed to reconstruct the GOX gene by adding XhoI sites at both ends, inserting a glu-ala-glu-ala spacer at the 5' end, and introducing an XbaI site at the 3' end. These modifications facilitate the cloning of the GOX-Xho gene into the pTA2 vector and its subsequent ligation into the pPICZαB expression vector, allowing for extracellular production of GOX through fusion with the α-mating factor (α-MF) signal peptide. The GOX-Xho gene was successfully amplified, cloned, and characterized. The pTA2-GOX-Xho recombinant plasmid was verified through sequencing and restriction analysis, confirming the present and correct orientation of the 1797 bp GOX-Xho gene. However, sequencing revealed several point mutations, necessitating further computational analysis to predict their impact on the enzyme's structure and function before recombinant protein expression.
Cloning of the GOX-Xho Gene IPBCC 08.610 into Plasmid pTA2 and Its Characterization Aryani, Hanifah; Akbar, Nadhira Fathiaz; Fuad, Asrul Muhamad; Ambarsari, Laksmi; Kurniatin, Popi Asri
Jurnal Kimia Valensi Jurnal Kimia VALENSI, Volume 10, No. 2, November 2024
Publisher : Department of Chemistry, Faculty of Science and Technology Syarif Hidayatullah Jakarta State Islamic University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15408/jkv.v10i2.39602

Abstract

Glucose oxidase (GOX) from Aspergillus niger catalyzes the oxidation of β-D-glucose to δ-gluconolactone and hydrogen peroxide, making it valuable for industrial applications. Intracellular GOX exhibits higher activity than its extracellular counterpart. This study focuses on enhancing the extracellular production of GOX through recombinant DNA technology. This study aimed to reconstruct the GOX gene by adding XhoI sites at both ends, inserting a glu-ala-glu-ala spacer at the 5' end, and introducing an XbaI site at the 3' end. These modifications facilitate the cloning of the GOX-Xho gene into the pTA2 vector and its subsequent ligation into the pPICZαB expression vector, allowing for extracellular production of GOX through fusion with the α-mating factor (α-MF) signal peptide. The GOX-Xho gene was successfully amplified, cloned, and characterized. The pTA2-GOX-Xho recombinant plasmid was verified through sequencing and restriction analysis, confirming the present and correct orientation of the 1797 bp GOX-Xho gene. However, sequencing revealed several point mutations, necessitating further computational analysis to predict their impact on the enzyme's structure and function before recombinant protein expression.
Co-Authors -, Suryani . SURYANI A.E. Zainal Hasan Ade Heri Mulyati Adrian Adiva Adriansyah Nanda Putra Agnia Nurul Jannati Agung Isnanto Agustina L.N. Aminin Ahmad Irvan Pratama Ainia Hanifitri Aisyah Girindra Akbar, Nadhira Fathiaz Akhiruddin Maddu Akhmad Endang Zainal Hasan Alifia Mutiara Annisa Alimah, Shobiroh Nuur ANINDA INDRIANI Anja Meryandini Annisa Dhiya Athiyyah Khanza Aqilah, Rifany Fairuz Aris Tri Wahyudi Arwansyah Arwansyah Aryani, Hanifah Asrul Muhamad Fuad, Asrul Muhamad Assifah Eryandini Azhari, Muhammad Alwin Azzara Putri Elvaza Chelsea Chelsea, Chelsea Chelsy Narita Choirunnisa Miftahul Jannah Deki Geraldi Dewi Seswita Zilda Diana Widiastuti DIMAS ANDRIANTO Djarot Sasongko Hami Seno DWI NINGSIH SUSILOWATI DWI NINGSIH SUSILOWATI Dwi SUBIYARTI Dwiningsih Susilowati Edy Djauhari Purwakusumah Edy Djauhari Purwakusumah Efi Sanfitri Harahap Faliha Arinda Lestari Farhan Azhwin Maulana Fathin, Muhammad Faris Fatriani, Rizka 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, . 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 Ilham Kurniawan Ilham Kurniawan Imelia Dewi Imron RIYADI Inayah, Mazidah Noer Inda Setyawati, Inda Irma Rahmayani Isnanto, Agung Jaya Hardi Kapitan, Origenes Boy Karichsa Hariana Latifah K Darusman Lestari, Faliha Arinda Liliyani , Ni Putu Peggy Lisa Giovanny Made Suhandana Madyastuti, Rini Marfira, Nurul Mega Safithri Miantika, Shafillah Muhamad Rifai Muhamad Rifai Muhammad Alwin Azhari Muhammad Faris Fathin Muhammad Halim Mustika Luthfia Mustika Permatasari Mustopa, Syahrul Nabila Nur Nafiati NISA RACHMANIA MUBARIK Novia Winarti Nur Qadri Rasyid Nurhidayat Nurhidayat Nurul Marfira Nuur’Alimah, Shobiroh Okta Vino Pratama, Ahmad Irvan Purwantiningsih Sugita Puspa Julistia Puspita Putri, Ike Wahyuni Radika Evita Hidayah Rahayu, Dyah Utami Cahyaning Rasyid, Nur Qadri Ridho Pratama Rifany Fairuz Aqilah Riki Riki Riksa Nur Wahyuni Rini Kurniasih, Rini Rini Novita Riska Febrianti Rury Eryna Putri Sanro Tachibana Sarmila Sarmila Setyanto Tri Wahyudi Shobiroh Nuur' Alimah Shobiroh Nuur'Alimah Siti Nur'aeni Siti Nurjanah Siti Warnasih Soekarno Mismana Putra Steffanus Gozales Suryani - Suryani Suryani Syamsul Falah TATI NURHAYATI Tirta Setiawan Tony Sumaryada Trah Yudha Tri Puji Priyatno Tri Puji Priyatno Uswatun Hasanah Wahyuni, Riksa Nur Wanda Hamidah Waras Nurcholis Yadi Suryadi Yadi Suryadi Zahra Silmi Muscifa Zuniar Subastian