Richa Sharma
University of Delhi
23 Papers
22 Citations
Richa Sharma is an academic researcher from University of Delhi. The author has contributed to research in topics: Keratinase & Chemistry. The author has an hindex of 10, co-authored 23 publications.
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Papers
Revisiting microbial keratinases: next generation proteases for sustainable biotechnology.
TL;DR: A comprehensive review on microbial keratinases is presented giving an account of chronological progress of research along with the major milestones, and major focus has been on the key characteristics of keratinase, such as substrate specificity, keratin degradation mechanisms, molecular properties, and their role in prion decontamination along with other pharmaceutical applications.
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Psychobiotics: The Next-Generation Probiotics for the Brain
TL;DR: A review of psychobiotic products can be found in this paper, where the authors highlight the scope and advancements made in the field, enlisting numerous commercial psychobiotics products that have flooded the market.
91
Swapping of pro-sequences between keratinases of Bacillus licheniformis and Bacillus pumilus: Altered substrate specificity and thermostability
TL;DR: Pro-sequence mediated conformational changes were also observed in trans and were almost similar to the features acquired by the chimeras constructed in cis by swapping the pro-sequence region.
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Substrate specificity characterization of a thermostable keratinase from Pseudomonas aeruginosa KS-1
Richa Sharma,Rani Gupta +1 more
TL;DR: A feather-degrading strain of Pseudomonas aeruginosa KS-1 was used in the present study and its crude cell-free fermentation broth completely degraded chicken feather within 12 h, in the absence of disulphide reductase activity.
27
Cloning and characterization of a thermostable detergent-compatible recombinant keratinase from Bacillus pumilus KS12
TL;DR: Functional expression of a keratinase from a potential feather‐degrading bacterium, Bacillus pumilus KS12, was achieved in Escherichia coli using pEZZ18 vector and the enzyme was identified as a serine hydrolase as it was completely inhibited by 10 mM phenylmethylsulfonyl fluoride.
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