Arvind M. Kayastha

ORCID: 0000-0002-5090-7159
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Research Areas
  • Enzyme Production and Characterization
  • Enzyme Catalysis and Immobilization
  • Phytase and its Applications
  • Electrochemical sensors and biosensors
  • Microbial Applications in Construction Materials
  • Enzyme Structure and Function
  • Protein Hydrolysis and Bioactive Peptides
  • Proteins in Food Systems
  • Microbial Metabolites in Food Biotechnology
  • Graphene and Nanomaterials Applications
  • Biofuel production and bioconversion
  • Microbial Metabolic Engineering and Bioproduction
  • Biochemical Acid Research Studies
  • Protein Interaction Studies and Fluorescence Analysis
  • Biochemical and Molecular Research
  • Food composition and properties
  • Algal biology and biofuel production
  • Cassava research and cyanide
  • Electrochemical Analysis and Applications
  • Metabolism and Genetic Disorders
  • Protein Structure and Dynamics
  • Glycosylation and Glycoproteins Research
  • Carbon and Quantum Dots Applications
  • Natural Antidiabetic Agents Studies
  • Nanoparticles: synthesis and applications

Banaras Hindu University
2015-2024

Ruhr University Bochum
2005

National Institute of Diabetes and Digestive and Kidney Diseases
1991-1994

National Institutes of Health
1991-1994

Shimane University
1991

Kōchi University
1991

Physico-chemical properties reflect the functional and structural characteristics of a protein. The comparative study physicochemical is important to know role protein in exploring its molecular evolution. A number online offline tools are available for calculating physico-chemical single sequence. However, tool not with graphical visualization Multi-FASTA sequences. Hence, we describe development utility MFPPI V.1.0 (a web interface developed JAVA platform) input each FASTA sequence from...

10.6026/97320630012074 article EN cc-by Bioinformation 2016-04-10

In this case study, we analysed the properties of unfolded states and pathways leading to complete denaturation a multimeric chick pea β-galactosidase (CpGAL), as obtained from treatment with guanidium hydrochloride, urea, elevated temperature extreme pH.CpGAL, heterodimeric protein native molecular mass 85 kDa, belongs α+β class protein. The conformational stability thermodynamic parameters CpGAL unfolding in different were estimated interpreted using circular dichroism fluorescence...

10.1371/journal.pone.0050380 article EN cc-by PLoS ONE 2012-11-21

Background β-Galactosidase is a vital enzyme with diverse application in molecular biology and industries. It was covalently attached onto functionalized graphene nano-sheets for various analytical applications based on lactose reduction. Methodology/Principal Findings Response surface methodology Box-Behnken design of experiment used determination optimal immobilization conditions, which resulted 84.2% efficiency. Native immobilized characterized the help transmission scanning electron...

10.1371/journal.pone.0040708 article EN cc-by PLoS ONE 2012-07-18

Urease purified from pigeonpea seeds was immobilized on gelatin beads via cross‐linking with glutaraldehyde. The maximum immobilization (75%) observed at 30 mg/ml gelatin, 0·414 mg of enzyme/bead, 1% (v/v) glutaraldehyde and 4 °C. Beads stored in 50 mM Tris/acetate buffer (pH 7·3) °C showed a half‐life 240 days there practically no leaching enzyme (less than 2%) over period days. These can be reused more times (with 24 h intervals) without much loss activity (i.e. less 11%). urease shift its...

10.1042/ba20010016 article EN Biotechnology and Applied Biochemistry 2001-08-01

The origin of reaction and substrate specificity the control activity by protein-protein interaction are investigated using tryptophan synthase alpha 2 beta complex from Salmonella typhimurium. We have compared some spectroscopic kinetic properties wild type subunit five mutant forms that altered catalytic properties. These enzymes, which were engineered site-directed mutagenesis, single amino acid replacements in either active site or wall a tunnel extends to complex. find complexes...

10.1016/s0021-9258(18)54673-1 article EN cc-by Journal of Biological Chemistry 1991-11-01
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