Kritika Singh
Banaras Hindu University
32 Papers
10 Citations
Kritika Singh is an academic researcher from Banaras Hindu University. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 7, co-authored 9 publications.
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Papers
α-Amylase from wheat (Triticum aestivum) seeds: Its purification, biochemical attributes and active site studies
Kritika Singh,Arvind M. Kayastha +1 more
TL;DR: Chemical modification studies showed that the enzyme contains histidine and carboxylic residues at its active site for its catalytic activity and possibly conserved areas and hence is suitable for application in starch based industries.
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Functionalized graphene sheets as immobilization matrix for Fenugreek β-amylase: enzyme kinetics and stability studies.
TL;DR: Increase in thermal stability of immobilized enzyme and non-toxic nature of functionalized graphene can be exploited for production of maltose in food and pharmaceutical industries.
Optimal immobilization of α-amylase from wheat (Triticum aestivum) onto DEAE-cellulose using response surface methodology and its characterization
Kritika Singh,Arvind M. Kayastha +1 more
TL;DR: In this paper, the response surface methodology was utilized to seek optimal parameters for immobilization and Box-Behnken design was found worthy with 86% immobilization of wheat α-amylase on DEAE-cellulose matrix under optimal condition.
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α-Amylase immobilization onto functionalized graphene nanosheets as scaffolds: Its characterization, kinetics and potential applications in starch based industries.
TL;DR: In this article, the authors used functionalized graphene sheets as a scaffold for α-amylase immobilization using Response Surface Methodology based on Box-Behnken design, with an overall immobilization efficiency of 85.16%.
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Heat, Acid and Chemically Induced Unfolding Pathways, Conformational Stability and Structure-Function Relationship in Wheat α-Amylase.
TL;DR: Careful examination of biophysical properties of intermediate states populated in urea and GdHCl induced denaturation suggests that α-amylase unfolding undergoes irreversible and non-coincidental cooperative transitions, as opposed to previous reports of two-state unfolding.