Research Interests: Chemistry, Dengue Virus, Antibodies, Circular Dichroism, Absorption spectroscopy, and 15 moreComplexation, Antibody, Conformations, Binding Characteristics, CD Spectra, Chiral Structures, Circularly Polarized Light, Complex Solution, Conformational Change, Antigens, Data Storage Equipment, Dichroism, Antigen, epitope, and Circularly polarized
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Fatty acid desaturase catalyzes the desaturation reactions by insertion of double bonds into the fatty acyl chain, producing unsaturated fatty acids. Though soluble fatty acid desaturases have been studied widely in advanced organisms,... more
Fatty acid desaturase catalyzes the desaturation reactions by insertion of double bonds into the fatty acyl chain, producing unsaturated fatty acids. Though soluble fatty acid desaturases have been studied widely in advanced organisms, there are very limited studies of membrane fatty acid desaturases due to the difficulty of generating recombinant desaturase. Brassica napus is a rapeseed, which possesses a range of different membrane-bound desaturases capable of producing fatty acids including Δ3, Δ4, Δ8, Δ9, Δ12, and Δ15 fatty acids. The 1155 bp open reading frame of Δ12 fatty acid desaturase (FAD12) from Brassica napus codes for 383 amino acid residues with a molecular weight of 44 kDa. It was expressed in Escherichia coli at 37 °C in soluble and insoluble forms when induced with 0.5 mM IPTG. Soluble FAD12 has been purified using Ni2+-Sepharose affinity chromatography with a total protein yield of 0.728 mg/mL. Gas chromatography-mass spectrometry (GC-MS) analysis revealed that desaturase activity of FAD12 could produce linoleic acid from oleic acid at a retention time of 17.6 with a conversion rate of 47%. Characterization of purified FAD12 revealed the optimal temperature of FAD12 was 50 °C with 2 mM preferred substrate concentration of oleic acid. Analysis of circular dichroism (CD) showed FAD12 was made up of 47.3% and 0.9% of alpha-helix and β-sheet secondary structures. The predicted Tm value was 50.2 °C.
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Research Interests: Engineering, Biochemistry, Chemistry, Biology, Heat Treatment, and 15 moreAgricultural Biotechnology, Ion Chromatography, Medicine, Biological Sciences, Biodegradation, Escherichia coli, Affinity chromatography, Enzyme, Fermentation, Microbial Biochemistry and Plant Biotechnology, Biological Macromolecules, Inulin, Corncob, Biochemistry and cell biology, and Genetically Modified Rice
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Meyerozyma guilliermondii strain SO, a newly isolated yeast species from spoilt orange, has been used as a host to express the recombinant proteins using methylotrophic yeast promoters. However, as a novel yeast expression system, the... more
Meyerozyma guilliermondii strain SO, a newly isolated yeast species from spoilt orange, has been used as a host to express the recombinant proteins using methylotrophic yeast promoters. However, as a novel yeast expression system, the vacuolar proteases of this yeast have not been determined, which may have contributed to the low level of heterologous protein secretions. Thus, this study aimed to determine intra- and extracellular proteolytic activity and identify the putative vacuolar proteases using bioinformatics techniques. A clear zone was observed from the nutrient agar skimmed milk screening plate. Proteolytic activity of 117.30 U/ml and 75 U/ml were obtained after 72 h of cultivation for both extracellular and intracellular proteins, respectively. Next, the Hidden Markov model (HMM) was used to detect the presence of the vacuolar proteases (PEP4 and PRB1) from the strain SO proteome. Aspartyl protease (PEP4) with 97.55% identity to Meyerozyma sp. JA9 and a serine protease (P...
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The dynamics and conformational landscape of proteins in organic solvents are events of potential interest in nonaqueous process catalysis. Conformational changes, folding transitions, and stability often correspond to structural... more
The dynamics and conformational landscape of proteins in organic solvents are events of potential interest in nonaqueous process catalysis. Conformational changes, folding transitions, and stability often correspond to structural rearrangements that alter contacts between solvent molecules and amino acid residues. However, in nonaqueous enzymology, organic solvents limit stability and further application of proteins. In the present study, molecular dynamics (MD) of a thermostable Geobacillus zalihae T1 lipase was performed in different chain length polar organic solvents (methanol, ethanol, propanol, butanol, and pentanol) and water mixture systems to a concentration of 50%. On the basis of the MD results, the structural deviations of the backbone atoms elucidated the dynamic effects of water/organic solvent mixtures on the equilibrium state of the protein simulations in decreasing solvent polarity. The results show that the solvent mixture gives rise to deviations in enzyme structu...
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Research Interests: Chemistry, Molecular Dynamics Simulation, Protein Folding, Medicine, Macromolecular X-Ray Crystallography, and 9 moreMolecular Dynamics, Software, High Temperature, Protein Secondary Structure Prediction, Lipase, Molecular Dynamic Simulation, Thermostability, Biochemistry and cell biology, and Geobacillus
Pancreatic lipase inhibitors from natural sources are considered as potential tool for the treatment of obesity. The inhibitory activity of 24 crude extracts of selected Malaysian plants against porcine pancreatic lipase (PPL) was... more
Pancreatic lipase inhibitors from natural sources are considered as potential tool for the treatment of obesity. The inhibitory activity of 24 crude extracts of selected Malaysian plants against porcine pancreatic lipase (PPL) was successfully screened and tested by using in vitro approach. Orthosiphon stamineus, Phyllanthus niruri, Murraya paniculata and Averrhoa bilimbi leaves extracts showed more than 70% inhibitions when incubated with PPL at a final concentration of 500 μg/mL for 15 minutes at 37⁰C. P. niruri crude extract exhibited strongest lipase inhibitory activity, with an IC50 value of 27. 65 μg/mL followed by O. stamineus, M. paniculata and A. bilimbi with IC50 values of 34.74, 41.45 and 55.18 μg/mL, respectively. Inhibition mode study disclosed that O. stamineus and A. bilimbi could act as uncompetitive inhibitor while P. niruri and M. paniculata could act as noncompetitive inhibitor. The results suggested that these four plant extracts may be useful for obesity treatment.
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Research Interests: Biochemistry, Chemistry, Catalysts, Protease, Phytase, and 3 moreActive site, Proteases, and Thermostability
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Due to its thermostability and high pH compatibility, subtilisin is most known for its role as an additive for detergents in which it is categorized as a serine protease according to MEROPS database. Subtilisin is typically isolated from... more
Due to its thermostability and high pH compatibility, subtilisin is most known for its role as an additive for detergents in which it is categorized as a serine protease according to MEROPS database. Subtilisin is typically isolated from various bacterial species of the Bacillus genus such as Bacillus subtilis, B. amyloliquefaciens, B. licheniformis, and various other organisms. It is composed of 268–275 amino acid residues and is initially secreted in the precursor form, preprosubtilisin, which is composed of 29‐residues signal peptide, 77‐residues propeptide, and 275‐residues active subtilisin. Subtilisin is known for the presence of high and low affinity calcium binding sites in its structure. Native subtilisin has general properties of thermostability, tolerance to neutral to high pH, broad specificity, and calcium‐dependent stability, which contribute to the versatility of subtilisin applicability. Through protein engineering and immobilization technologies, many variants of subtilisin have been generated, which increase the applicability of subtilisin in various industries including detergent, food processing and packaging, synthesis of inhibitory peptides, therapeutic, and waste management applications.
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Aquaporins, also known as water channels, are a large family of transmembrane channel proteins present throughout all life domains and are implicated in human disorders. The psychrophilic aquaporin comes to attention because of its... more
Aquaporins, also known as water channels, are a large family of transmembrane channel proteins present throughout all life domains and are implicated in human disorders. The psychrophilic aquaporin comes to attention because of its specialty in adaptive ability to keep on functioning to maintain water homeostasis under low temperatures, which have an optimal temperature for growth at about 15ºC or lower. However, studies regarding aquaporin isolated from psychrophilic Pseudomonas sp. are still scattered. Recently, the genome sequence of an Antarctic Pseudomonas sp. strain AMS3 revealed a gene sequence encoding for a putative aquaporin designated as PAqpZ2_AMS3. In this study, structure analysis and molecular dynamics (MD) simulation of a predicted model of a fully hydrated aquaporin monomer was embedded in a lipid bilayer and was performed at different temperatures for structural flexibility and stability analysis. The MD simulation results revealed that the predicted structure coul...