Biochemical and structural characterization of a detergent-stable serine alkaline protease from seawater haloalkaliphilic bacteria |
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| Institution: | 1. Department of Biochemical and Pharmaceutical Technology, University of São Paulo, São Paulo, SP, 05508-000, Brazil;2. Department of Civil, Chemical and Environmental Engineering, Pole of Chemical Engineering, Genoa University, via Opera Pia 15, 16145 Genoa, Italy;3. Laboratory of Enzymology, Department of Cellular Biology, University of Brasilia, Campus Darcy Ribeiro, Asa Norte, Brasilia, DF, 70910900, Brazil;4. Department of Pharmaceutical Sciences, School of Health Sciences, University of Brasilia, Campus Darcy Ribeiro, Asa Norte, Brasilia, DF, 70910900, Brazil;1. Laboratory of Microbial Biotechnology and Engineering Enzymes (LMBEE), Centre of Biotechnology of Sfax (CBS), University of Sfax, Road of Sidi Mansour Km 6, PO Box 1177, Sfax 3018, Tunisia;2. Laboratory of Natural Products Chemistry and Biomolecules (LNPCB), University of Blida 1, Road of Soumaâ, PO Box 270, 09000 Blida, Algeria;3. National Centre for Research and Development of Fisheries and Aquaculture (CNRDPA) 11, Bd Amirouche PO Box 67, Bou Ismaïl, 42415 Tipaza, Algeria;1. Department of Microbiology, Panjab University, Chandigarh, 160014, India;2. Department of Industrial Microbiology, Guru Nanak Khalsa College, Yamunanagar, Haryana, India;1. Department of Biotechnology, Babasaheb Bhimrao Ambedkar University, Vidya Vihar, Luckhnow 226025, Uttar Pradesh, India;2. Amity Institute of Organic Agriculture, Amity University Uttar Pradesh ( AUUP), Noida 201303, Uttar Pradesh, India |
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| Abstract: | An extracellular protease from a newly isolated seawater haloalkaliphilic bacterium, haloalkaliphilic bacteria Ve2-20-91 HM047794], was purified and characterized. The enzyme is a monomer with a 37.2 kDa estimated molecular weight. It catalyzed reactions in the pH range 8–11 and performed optimally at pH 10. While maximal activity occurred at 50 °C, the temperature profile shifted from 50 to 80 °C in 1–3 M NaCl. The enzyme's thermal stability was probed using circular dichroism (CD) spectroscopy with NaCl at 50 and 70 °C. The changes in the enzyme's secondary structure were also analyzed using Fourier transform infrared spectroscopy (FTIR). The N-terminal amino acid sequence GKDGPPGLCGFFGCI exhibited low homology with other bacterial proteases, which highlights the enzyme's novelty. The enzyme was labile in anionic surfactant (1% w/v SDS) but showed stability in non-ionic surfactants (Tween 20, Tween 80 and Triton X-100 all 1% v/v), commercial detergents, and oxidizing and reducing agents. The enzyme's excellent stability in commercial detergents highlights its potential as a detergent additive. |
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| Keywords: | Alkaline protease Detergent stability Haloalkaliphilic bacteria N-terminal sequence CD spectroscopy FTIR |
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