Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/11422
Title: Purification and biochemical characterization of a novel thermostable serine protease from Geobacillus sp. GS53
Authors: Güracar Baykara, Seden
Sürmeli, Yusuf
Şanlı Mohamed, Gülşah
Keywords: Serine protease
Geobacillus
Thermostability
Surfactant
Issue Date: 2021
Publisher: Springer
Abstract: Proteases account for approximately 60% of the enzyme market in the world, and they are used in various industrial applications including the detergent industry. In this study, production and characterization of a novel serine protease of thermophilic Geobacillus sp. GS53 from Balcova geothermal region, Izmir, Turkey, were performed. The thermostable protease was purified through ammonium sulfate precipitation and anion-exchange chromatography. The results showed that the protease had 137.8 U mg(-1) of specific activity and optimally worked at 55 C-o and pH 8. It was also active in a broad pH (4-10) and temperature (25-75 degrees C) ranges. The protease was highly stable at 85 degrees C and demonstrated relative stability at pH 4, 7, and 10. Also, the enzyme had high stability against organic solvents and surfactants; enzyme relative activity did not decrease below 81% upon preincubation for 10 min. Ca2+, Cu2+, and Zn2+ ions slightly induced protease activity. The protease was highly specific to casein, skim milk, Hammerstein casein, and BSA substrates. These results revealed that the protease might have a potential effect in a variety of industrial fields, especially the detergent industry, because of its high thermostability and stability to surfactants.
URI: https://doi.org/10.1007/s12010-021-03512-0
https://hdl.handle.net/11147/11422
ISSN: 0273-2289
1559-0291
Appears in Collections:Chemistry / Kimya
PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

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