Identification of a Novel Thermostable Alkaline Protease from <i>Bacillus megaterium</i>-TK1 for the Detergent and Leather Industry
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 <i>Bacillus megaterium</i>-TK1 strain from a seawater source. The extracellular thermostable ser...
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MDPI AG
2020-12-01
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| Series: | Biology |
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| Online Access: | https://www.mdpi.com/2079-7737/9/12/472 |
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| author | Tamilvendan Manavalan Arulmani Manavalan Shiyamsundar Ramachandran Klaus Heese |
| author_facet | Tamilvendan Manavalan Arulmani Manavalan Shiyamsundar Ramachandran Klaus Heese |
| author_sort | Tamilvendan Manavalan |
| collection | DOAJ |
| description | 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 <i>Bacillus megaterium</i>-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. |
| first_indexed | 2024-03-10T14:02:19Z |
| format | Article |
| id | doaj.art-bb5c007994bc4d57b2aef36bfa81e520 |
| institution | Directory Open Access Journal |
| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-10T14:02:19Z |
| publishDate | 2020-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biology |
| spelling | doaj.art-bb5c007994bc4d57b2aef36bfa81e5202023-11-21T01:02:33ZengMDPI AGBiology2079-77372020-12-0191247210.3390/biology9120472Identification of a Novel Thermostable Alkaline Protease from <i>Bacillus megaterium</i>-TK1 for the Detergent and Leather IndustryTamilvendan Manavalan0Arulmani Manavalan1Shiyamsundar Ramachandran2Klaus Heese3Centre for Advanced Studies in Botany, University of Madras, Chennai, Tamil Nadu 600 025, IndiaCentre for Advanced Studies in Botany, University of Madras, Chennai, Tamil Nadu 600 025, IndiaDepartment of Biotechnology, Anna University, BIT-Campus, Tiruchirappalli, Tamil Nadu 620 024, IndiaGraduate School of Biomedical Science and Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul 133-791, KoreaAn 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 <i>Bacillus megaterium</i>-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.https://www.mdpi.com/2079-7737/9/12/472<i>Bacillus megaterium</i>detergenthydrolaseproteasethermostable |
| spellingShingle | Tamilvendan Manavalan Arulmani Manavalan Shiyamsundar Ramachandran Klaus Heese Identification of a Novel Thermostable Alkaline Protease from <i>Bacillus megaterium</i>-TK1 for the Detergent and Leather Industry Biology <i>Bacillus megaterium</i> detergent hydrolase protease thermostable |
| title | Identification of a Novel Thermostable Alkaline Protease from <i>Bacillus megaterium</i>-TK1 for the Detergent and Leather Industry |
| title_full | Identification of a Novel Thermostable Alkaline Protease from <i>Bacillus megaterium</i>-TK1 for the Detergent and Leather Industry |
| title_fullStr | Identification of a Novel Thermostable Alkaline Protease from <i>Bacillus megaterium</i>-TK1 for the Detergent and Leather Industry |
| title_full_unstemmed | Identification of a Novel Thermostable Alkaline Protease from <i>Bacillus megaterium</i>-TK1 for the Detergent and Leather Industry |
| title_short | Identification of a Novel Thermostable Alkaline Protease from <i>Bacillus megaterium</i>-TK1 for the Detergent and Leather Industry |
| title_sort | identification of a novel thermostable alkaline protease from i bacillus megaterium i tk1 for the detergent and leather industry |
| topic | <i>Bacillus megaterium</i> detergent hydrolase protease thermostable |
| url | https://www.mdpi.com/2079-7737/9/12/472 |
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