Evaluation of a novel purified and characterized alkaline protease from the extremophile Exiguobacterium alkaliphilum VLP1 as a detergent additive

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Hemsinli A., Gürkök S.

BIOTECHNOLOGY JOURNAL, cilt.19, sa.1, ss.1-10, 2024 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 19 Sayı: 1
  • Basım Tarihi: 2024
  • Doi Numarası: 10.1002/biot.202300441
  • Dergi Adı: BIOTECHNOLOGY JOURNAL
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Compendex, EMBASE, MEDLINE, Veterinary Science Database
  • Sayfa Sayıları: ss.1-10
  • Atatürk Üniversitesi Adresli: Evet

Özet

This study focused on the isolation and identification of a novel alkaline protease-producing strain from Lake Van, the largest soda lake on Earth. The objective was to purify, characterize, and investigate the potential application of protease in the detergent industry. Through a combination of classical and molecular methods, the most potent protease producer was identified as Exiguobacterium alkaliphilum VLP1. The purification process, involving ammonium sulfate precipitation, ultrafiltration, and anion exchange chromatography, resulted in a 45-fold purification with a yield of 6.4% and specific activity of 1169 U mg-1 protein. The enzyme exhibited a molecular weight of 69 kDa, a Km value of 0.4 mm, and a maximal velocity (Vmax ) value of 2000 U mg-1 . The optimum activity was observed at 40°C and potential of hydrogen (pH) 9, while the enzyme also exhibited remarkable stability in the ranges of 30-60°C and pH 9-12. Notably, this study represents the first report of an alkaline protease isolated and characterized from E. alkaliphilum. This study also highlighted the potential of the enzyme as a detergent additive, as it showed compatibility with commercial detergents and effectively removed blood and chocolate stains from fabrics.