Article Per Year (5 Year)
p-Index From 2021 - 2026
1.606
P-Index
This Author published in this journals
All Journal VANOS Journal of Mechanical Engineering Education Edumatsains Jurnal Dinamika Pendidikan Prosiding SNFA (Seminar Nasional Fisika dan Aplikasinya) Jurnal Pengabdian Masyarakat MIPA dan Pendidikan MIPA Journal of Educational Research and Evaluation Jurnal Sains dan Edukasi Sains International Journal of Educational Management and Innovation (IJEMI) Jurnal ComunitA Servizio Al Jahiz: Journal of Biology Education Research Makara Journal of Science Dharma Pengabdian Perguruan Tinggi (DEPATI) Jurnal Pengabdian Pada Masyarakat Jurnal Laboratorium Sains Terapan
Manogari Sianturi
Universitas Kristen Indonesia
Religion Aerospace Engineering Agriculture, Biological Sciences & Forestry Arts Humanities Astronomy Automotive Engineering Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Civil Engineering, Building, Construction & Architecture Computer Science & IT Control & Systems Engineering Decision Sciences, Operations Research & Management Dentistry Earth & Planetary Sciences Economics, Econometrics & Finance Education Electrical & Electronics Engineering Energy Engineering Environmental Science Health Professions Immunology & microbiology Industrial & Manufacturing Engineering Languange, Linguistic, Communication & Media Law, Crime, Criminology & Criminal Justice Library & Information Science Materials Science & Nanotechnology Mathematics Mechanical Engineering Medicine & Pharmacology Neuroscience Nursing Physics Public Health Social Sciences Transportation Veterinary Other

Published : 18 Documents Claim Missing Document
Claim Missing Document
Check
Articles

Found 2 Documents
Search
Journal : Edumatsains

 1 
Analisa Jembatan Garam untuk Meningkatkan Kestabilan Termal Enzim Xilanase Aspergillus niger Nya Daniaty Malau; Manogari Sianturi
EduMatSains : Jurnal Pendidikan, Matematika dan Sains Vol 1 No 2 (2017): Januari
Publisher : Fakultas Keguruan dan Ilmu Pendidikan, Universitas Kristen Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.33541/edumatsains.v1i2.243

Abstract

Enzymes are the same biomolecules such as proteins, has only a functional difference. Enzymes are biocatalyst that recently applied to many industrial fields. To be applied in the field of industrial enzymes should be enhanced stability against temperature. Analysis of the salt bridge is able to demonstrate the potential of residues mutated to improve thermal stability. Molecular dynamics simulations performed by observing the unfolding process. Variations in temperature used is 400 K, 450 K and 500 K, respectively performed for 2.5 ns. Then analyzed the pair a salt bridge is formed. There are 25 pairs of salt bridges at a temperature of 400 K, 24 pairs of salt bridges at a temperature of 450 K, and there are 30 pairs of the salt bridge is formed at a temperature of 500 K. To determine the salt bridge partner is a key enzyme kesstabilan we then plotted salt bridge between distances (Ã… ) with time (ns) only at a temperature of 500 K, for allegedly at these temperatures has been a process of unfolding. Of the 30 pairs of the salt bridge that had plotted the distance with time, the pair obtained a salt bridge that pattern similar to the pattern chart graph analysis Root-mean-square deviation (RMSD). There are three curves salt bridge that pattern is similar to the pattern of RMSD curve and SASA, namely the salt bridge Glu84-Arg134, Asp104-Arg134 and Asp113-Arg115. The sharp rise in the value of RMSD and the resulting rupture SASA three pairs of the salt bridges. So when carried mutations in-silico candidate mutants that will be transferred is the amino acid residues are thought to play a role in electrostatic interactions and replace it with another amino acid residue on the basis of structural similarities. Keywords: Salt bridge, Electrostatic bond, Mutation, Unfolding
Analisa Interaksi Hidrofobik terhadap Kestabilan Termal Enzim Xilanase Aspergillus niger Nya Daniaty Malau; Manogari Sianturi
EduMatSains : Jurnal Pendidikan, Matematika dan Sains Vol 3 No 2 (2019): Januari
Publisher : Fakultas Keguruan dan Ilmu Pendidikan, Universitas Kristen Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.33541/edumatsains.v3i2.890

Abstract

Xylanase is one type of enzyme that has an important role in the field of industry. One way that can be done to improve the thermostability of an enzyme is by protein engineering . Mutation of these proteins can be done by studying the structure of proteins through molecular dynamics simulation approach. In this research, thermal stability analysis on the structure of Aspergilus niger Wild Type xylase (AnX) was performed. This study aims to study the thermal stability characteristic of Aspergilus niger xylanase enzyme through molecular dynamics simulation approach. Molecular dynamics simulations of AnX were performed using NAMD (Not Just Another Molecular Dynamic) software at at a temperature of 300-500 K. This study focused on studying the thermal stability characteristic of the enzymes to obtain information on residues that are responsible for the characteristic. Selection of residues to be mutated, based on the results of Hydrophobic Interactions. Based on the analysis results, the design of mutant Xylanase enzyme that is more thermostable than the Wild Type Xilanase Enzyme, so it can provide suggestions a more stable Xilanase mutation design that can be implemented into wet experiments to genetically engineer the Aspergilus niger xylanase enzyme. Xylanase Aspergillus niger enzyme is unfolded at 500 K at 9.5 ns. The residues responsible for the thermal stability of Xilanase Aspergilus niger enzyme based on hydrophobic interaction analysis are Alanine at residue 60. This residue is in segment / chain 3. The best mutant that can increase thermal stability is indicated by the Alanin 60 residue replaced with Methionin. The mutant Alanin 60 residue that replaced with a methionine mutant obtained ΔΔGsolv value of -21.10345. Thus the Ala60Met mutant is the most stable mutant supposed to increase thermal stability of Aspergillus niger Xilanase Enzyme. Keywords : enzyme, thermostability, mutation, molecular dynamics
Co-Authors Agnes Sadja Anawati, Anawati Areli Elona Bambang Widodo Budiarto Dedi Juliasman Sakatsila Ditasona, Candra Elferida Sormin Erni Murniarti Erni Murniarti, Erni Estomo, Rene Etika Nyaman Giawa Familia Novita Simanjuntak Faradiba Faradiba Faradiba Faradiba Giawa, Etika Nyama Handayani, Ida Sri Hasanudin, Nurlaila HOTMAULINA SIHOTANG Junsay, Merle L. Juwono, Ariadne Laksmidevi Laia, Setiana Lase, Fan Damai Sejahtera Lumbantobing, Septina Severina Manullang, Nathasya Grisella Medyawanti Pane N. Aruan, Bunga Ngia Masta Nurafni Prapitasari Nya Daniaty Malau Olla, Yufran Meliando Purba, Santri Chintia Rahmad Samosir Sakatsila, Dedi Juliasman Samuel Gideon Seprianus Seprianus Septina Severina Lumbantobing Septina Severina Lumbantobing Simbolon, Kerdid Stevi Natalia, Stevi Sumiati Sumiati Sumiati Sumiati Sunarto Sunarto Taat Guswantoro, Taat Tris Kurniawati Laia Tugelida, Nel Bryan C Wahyuningtyas, Riska Septia