ArticleMolecules (Basel, Switzerland)2016
High Milk-Clotting Activity Expressed by the Newly Isolated Paenibacillus spp. Strain BD3526.
Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 33 citations in OpenAlex.
- Partitioning purification, biochemical characterization, and milk coagulation efficiency of protease from a newly Streptomyces sp. isolate.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Potential of the Liquid Fermentation of Fishery Waste byPolymers · 2022Article
- Proteases Production and Chitin Preparation from the Liquid Fermentation of Chitinous Fishery By-Products byMarine drugs · 2021Article
- Isolation and Characterization of a New Fusaricidin-Type Antibiotic Produced by Paenibacillus bovis sp. nov BD3526.Current microbiology · 2020Article
- Microbial Conversion of Shrimp Heads to Proteases and Chitin as an Effective Dye Adsorbent.Polymers · 2020Article
- Single-Cell Transcriptomics Reveals That Metabolites Produced byFrontiers in microbiology · 2020Article
- Characteristics of proteolytic microorganisms and their effects on proteolysis in total mixed ration silages of soybean curd residue.Asian-Australasian journal of animal sciences · 2020Article
- Production, purification and characterization of a milk clotting enzyme fromFood science and biotechnology · 2019Article
- Catalytic, kinetic and thermodynamic properties of free and immobilized caseinase on mica glass-ceramics.Heliyon · 2019Article
- Article
- Fermentation Products ofFrontiers in microbiology · 2018Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Paenibacillus spp. BD3526, a bacterium exhibiting a protein hydrolysis circle surrounded with an obvious precipitation zone on skim milk agar, was isolated from raw yak (Bos grunniens) milk collected in Tibet, China. Phylogenetic analysis based on 16S rRNA and whole genome sequence comparison indicated the isolate belong to the genus Paenibacillus. The strain BD3526 demonstrated strong ability to produce protease with milk clotting activity (MCA) in wheat bran broth. The protease with MCA was predominantly accumulated during the late-exponential phase of growth. The proteolytic activity (PA) of the BD3526 protease was 1.33-fold higher than that of the commercial R. miehei coagulant. A maximum MCA (6470 ± 281 SU mL(-1)) of the strain BD3526 was reached under optimal cultivation conditions. The protease with MCA was precipitated from the cultivated supernatant of wheat bran broth with ammonium sulfate and purified by anion-exchange chromatography. The molecular weight of the protease with MCA was determined as 35 kDa by sodium dodecyl sulfate-polyacrylamide gels electrophoresis (SDS-PAGE) and gelatin zymography. The cleavage site of the BD3526 protease with MCA in κ-casein was located at the Met106-Ala107 bond, as determined by mass spectrometry analysis.
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