Protease inhibitors significantly control physiologically relevant protease activities. Protease inhibitors from marine microbial sources are unique due to their rough living environmental conditions. In the present study, a protein protease inhibitor (PI) was produced from marine Oceanimonas sp. BPMS22. Seven different media were screened for the growth of the bacterium and production of PI. Different carbon and nitrogen sources were screened and optimized for the specific protease inhibitor activity. Three different growth models were checked for the best fit of the bacterial growth. A modified Gompertz model was selected as the best model for the growth of Oceanimonas sp. BPMS22 with the maximum specific growth rate of 0.165 hr and doubling time of 4.2 hr. The production of PI takes place during the non-growing phase of the bacterial growth. A kinetic model for the production of PI during non-growing phase was used for studying various process parameters. From the model, the maximum trypsin inhibitor formation rate of 0.3802 IU per mg of biomass per hour was observed at 49.91 hr.
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http://dx.doi.org/10.1080/10826068.2018.1476878 | DOI Listing |
Front Cell Infect Microbiol
April 2023
Department of Biotechnology, School of Chemical and Biotechnology, SASTRA Deemed to be University, Thanjavur, India.
The sp. -derived protein protease inhibitor (PPI) has been proven to shift macrophages towards an inflammatory state and reduce infection and . The current study explored and validated the mechanistic aspects of the PPI and Toll-like receptor (TLR) interaction.
View Article and Find Full Text PDFInt Immunopharmacol
November 2022
Department of Biotechnology, School of Chemical and Biotechnology, SASTRA Deemed to be University, Thanjavur 613 401, India; Department of Paramedical and Allied Health Sciences, Midnapore City College, Midnapore 721 129, India. Electronic address:
The present study aimed to validate the potential of a novel serine protein protease inhibitor (PPI), purified from marine Oceanimonas sp. BPMS22, induced M2 to M1 repolarization of the macrophages to treat visceral leishmaniasis (VL). Peptide mass fingerprint of the purified trypsin digested PPI peptide was obtained using matrix-assisted laser desorption ionization-time of flight combined with tandem mass spectrometry (MALDI-TOF MS/MS) and the sequence was used to construct a 3D protein model by homology modelling.
View Article and Find Full Text PDFMar Biotechnol (NY)
December 2018
Bioprospecting Laboratory, School of Chemical and Biotechnology, SASTRA Deemed University, Thanjavur, 613 401, India.
Protease inhibitors control major biological protease activities to maintain physiological homeostasis. Marine bacteria isolated from oligotrophic conditions could be taxonomically distinct, metabolically unique, and offers a wide variety of biochemicals. In the present investigation, marine sediments were screened for the potential bacteria that can produce trypsin inhibitors.
View Article and Find Full Text PDFPrep Biochem Biotechnol
January 2019
a Bioprospecting Laboratory, School of Chemical and Biotechnology , SASTRA Deemed University, Thanjavur , India.
Protease inhibitors significantly control physiologically relevant protease activities. Protease inhibitors from marine microbial sources are unique due to their rough living environmental conditions. In the present study, a protein protease inhibitor (PI) was produced from marine Oceanimonas sp.
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