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Article

Identification of a Novel Thermostable Alkaline Protease from Bacillus megaterium-TK1 for the Detergent and Leather Industry

by
Tamilvendan Manavalan
1,*,
Arulmani Manavalan
1,
Shiyamsundar Ramachandran
2 and
Klaus Heese
3,*
1
Centre for Advanced Studies in Botany, University of Madras, Chennai, Tamil Nadu 600 025, India
2
Department of Biotechnology, Anna University, BIT-Campus, Tiruchirappalli, Tamil Nadu 620 024, India
3
Graduate School of Biomedical Science and Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul 133-791, Korea
*
Authors to whom correspondence should be addressed.
Biology 2020, 9(12), 472; https://doi.org/10.3390/biology9120472
Submission received: 15 November 2020 / Revised: 11 December 2020 / Accepted: 14 December 2020 / Published: 16 December 2020
(This article belongs to the Section Microbiology)

Simple Summary

In the current investigation, we describe the characteristic features of a novel Bacillus megaterium bacterium-derived protease with excellent thermostable enzyme activity under stringent alkaline conditions. The protease is highly compatible with various detergents and thus appears to be an eco-friendly additive for a variety of industrial applications.

Abstract

An increased need by the green industry for enzymes that can be exploited for eco-friendly industrial applications led us to isolate and identify a unique protease obtained from a proteolytic Bacillus megaterium-TK1 strain from a seawater source. The extracellular thermostable serine protease was processed by multiple chromatography steps. The isolated protease displayed a relative molecular weight (MW) of 33 kDa (confirmed by zymography), optimal enzyme performance at pH 8.0, and maximum enzyme performance at 70 °C with 100% substrate specificity towards casein. The proteolytic action was blocked by phenylmethylsulfonyl fluoride (PMSF), a serine hydrolase inactivator. Protease performance was augmented by several bivalent metal cations. The protease tolerance was studied under stringent conditions with different industrial dispersants and found to be stable with Surf Excel, Tide, or Rin detergents. Moreover, this protease could clean blood-stained fabrics and showed dehairing activity for cow skin with significantly reduced pollution loads. Our results suggest that this serine protease is a promising additive for various eco-friendly usages in both the detergent and leather industries.
Keywords: Bacillus megaterium; detergent; hydrolase; protease; thermostable Bacillus megaterium; detergent; hydrolase; protease; thermostable
Graphical Abstract

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MDPI and ACS Style

Manavalan, T.; Manavalan, A.; Ramachandran, S.; Heese, K. Identification of a Novel Thermostable Alkaline Protease from Bacillus megaterium-TK1 for the Detergent and Leather Industry. Biology 2020, 9, 472. https://doi.org/10.3390/biology9120472

AMA Style

Manavalan T, Manavalan A, Ramachandran S, Heese K. Identification of a Novel Thermostable Alkaline Protease from Bacillus megaterium-TK1 for the Detergent and Leather Industry. Biology. 2020; 9(12):472. https://doi.org/10.3390/biology9120472

Chicago/Turabian Style

Manavalan, Tamilvendan, Arulmani Manavalan, Shiyamsundar Ramachandran, and Klaus Heese. 2020. "Identification of a Novel Thermostable Alkaline Protease from Bacillus megaterium-TK1 for the Detergent and Leather Industry" Biology 9, no. 12: 472. https://doi.org/10.3390/biology9120472

APA Style

Manavalan, T., Manavalan, A., Ramachandran, S., & Heese, K. (2020). Identification of a Novel Thermostable Alkaline Protease from Bacillus megaterium-TK1 for the Detergent and Leather Industry. Biology, 9(12), 472. https://doi.org/10.3390/biology9120472

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