ArticleBioMed research international2025
Identification and Characterization of a Protease Producing
Article in BioMed research international, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Biodegradation of hair waste for keratinase production using Bacillus altitudinis VK-1120 and its application in enzymatic dehairing.Biodegradation · 2026Article
- Bio-process development for sustainable, large-scale production of LAB-oligosaccharides as a potential anti-colon-cancer metabolites produced by Lactobacillus acidophilus 20079.Microbial cell factories · 2026Article
- Nitrogen Management in Crop-Soil-Environment Systems: Pathways Toward Sustainable and Climate-Resilient Agriculture.International journal of molecular sciences · 2026Review
- Optimization of protease production by newly isolated Bacillus sp. from the Red Sea using defatted soybean cake.Scientific reports · 2025Article
- Morpho-biochemical and molecular characterization of Bacillus subtilis and Priestia megaterium isolates from eastern Indian farmlands.Molecular biology reports · 2025Article
- Indigenous bacteria as potential agents for trace metal remediation in industrial wastewater.Scientific reports · 2025Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Environmental pollution has been a significant concern for the last few years. The leather industry significantly contributes to the economy but is one of Bangladesh's most prominent polluting industries. It is also responsible for several severe diseases such as cancer, lung diseases, and heart diseases of leather workers because they use bleaching agents and chemicals, and these have numerous adverse effects on human health. The study was aimed at isolating, identifying, and molecularly characterizing bacteria that produce protease enzymes that are highly capable of dehairing goat hide. Several attempts were made to isolate and identify protease-producing bacterial strains from different soil samples of tannery wastes. Initially, a total of four isolates were selected from tannery soil. After the different phenotypic and morphological characterization, one isolate (BS2) showed Gram-positive, rod-shaped, and spore-forming characteristics and could produce novel hair-degrading protease enzymes. The growth profile and protease activity of the bacteria at 37°C were observed; a basal level of extracellular protease increased with time. The enzyme's proteolytic activity was measured, and the unit of enzyme activity of the enzyme sample was 18.1. The ExPASy server (ProtParam) tool was used to estimate the physicochemical characteristics of the proteins and found molecular weight (MW) (7375.94 Da), aliphatic index (71.56), instability index (II, 80.63), Grand Average of Hydropathy (GRAVY) (-0.231), and isoelectric point (11.41). The protein-protein interactions (PPI) networks were generated using the Search Tool for the Retrieval of Interacting Genes (STRING) database and Cytoscape software. The PSIPRED v.4.0 and SAVES v.6.0 programs were used to determine the secondary and three-dimensional assembly of the selected protein. They found alpha helix (16, 25.00%), extended strand (6, 9.38%), beta-turn (5, 7.81%), and random coil (37, 57.81%). DNA isolation and purification were carried out, and the purity ratio was ~2.17 at 260 and 280 nm. Polymerase chain reaction (PCR) for amplifying the 16S rRNA gene was conducted, and the isolate was authentically recognized as
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