Article3 Biotech2016
Organic solvent tolerant metallo protease of novel isolate Serratia marcescens PPB-26: production and characterization.
Article in 3 Biotech, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- Cloning, Expression, and Characterization of a Metalloprotease from Thermophilic BacteriumBiology · 2024Article
- Purification and Characterization of a DegP-Type Protease from the Marine BacteriumMicroorganisms · 2023Article
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteases are a class of enzymes that catalyze hydrolysis of peptide bonds of proteins. In this study, 221 proteolytic bacterial isolates were obtained by enrichment culture method from soils of various regions of Himachal Pradesh, India. From these a hyper producer of protease was screened and identified by morphological and physiological testing and by 16S rDNA sequence as Serratia marcescens PPB-26. Statistical optimization of physiochemical parameters enhanced the protease production by 75 %. Protease of S. marcescens PPB-26 was classified as a metalloprotease. It showed optimal activity at 30 °C, pH 7.5 (0.15 M Tris-HCl buffer) and with 0.8 % substrate concentration. It had K
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Registered trials
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