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Expression and Characterization of Surfactnt-Stable Calcium-Dependent Protease: a Potential Additive for Laundry Detergents

Expression and Characterization of Surfactnt-Stable Calcium-Dependent Protease: a Potential... Extracellular protease SptA from the halophilic archaeon Natrinema sp. J7 was successfully expressed in Bacillus subtilis SCK6 using touchdown two-step PCR and plasmid multimer. Culture optimization was conducted to increase SptA protease activity 132-fold. It was shown that enzyme activity achieved the maximum activity at pH 8.0 and 55°C with casein as the substrate. SptA protease kept high stability and activity against many organic solvents and even maintained 60% activity in the presence of 8% NaCl. Meanwhile, SptA was redefined as a highly Ca2+-dependent subtilisin-like serine protease. Interestingly, SptA protease processed an autodigestion from 45 to 35 kDa in presence of Ca2+. Homology modeling illustrated the three binding sites of Ca2+ and the catalytic triad His231-Asp190-Ser384. In addition, SptA protease exhibited high compatibility with many surfactants and commercial detergents, showing 100% stability in the presence of commercial detergent Comfort. Washing performance analysis demonstrated remarkably high de-staining of the enzyme at 40°C for 20 min with a lower supplementation (500 U/mL). Accordingly, SptA protease could be considered as a promising bio-additive in the detergent industry. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Expression and Characterization of Surfactnt-Stable Calcium-Dependent Protease: a Potential Additive for Laundry Detergents

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References (33)

Publisher
Springer Journals
Copyright
Copyright © Pleiades Publishing, Inc. 2021. ISSN 0003-6838, Applied Biochemistry and Microbiology, 2021, Vol. 57, No. 4, pp. 481–492. © Pleiades Publishing, Inc., 2021.
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1134/s0003683821040165
Publisher site
See Article on Publisher Site

Abstract

Extracellular protease SptA from the halophilic archaeon Natrinema sp. J7 was successfully expressed in Bacillus subtilis SCK6 using touchdown two-step PCR and plasmid multimer. Culture optimization was conducted to increase SptA protease activity 132-fold. It was shown that enzyme activity achieved the maximum activity at pH 8.0 and 55°C with casein as the substrate. SptA protease kept high stability and activity against many organic solvents and even maintained 60% activity in the presence of 8% NaCl. Meanwhile, SptA was redefined as a highly Ca2+-dependent subtilisin-like serine protease. Interestingly, SptA protease processed an autodigestion from 45 to 35 kDa in presence of Ca2+. Homology modeling illustrated the three binding sites of Ca2+ and the catalytic triad His231-Asp190-Ser384. In addition, SptA protease exhibited high compatibility with many surfactants and commercial detergents, showing 100% stability in the presence of commercial detergent Comfort. Washing performance analysis demonstrated remarkably high de-staining of the enzyme at 40°C for 20 min with a lower supplementation (500 U/mL). Accordingly, SptA protease could be considered as a promising bio-additive in the detergent industry.

Journal

Applied Biochemistry and Microbiology – Springer Journals

Published: Jul 27, 2021

Keywords: heterologous expression; Ca2+-dependent; surfactant-stable; homology modeling; detergent formulation

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