Evaluation of a Thermophilic,Psychrostable, and Heavy Metal-Resistant Red Sea Brine Pool Esterase |
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Authors: | Shimaa F. Ahmed Rehab Z. Abdallah Rania Siam |
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Affiliation: | 1.Biology Department, School of Sciences and Engineering, The American University in Cairo, New Cairo 11835, Egypt; (S.F.A.); (R.Z.A.);2.Max Planck institute for Terrestrial Microbiology, 35043 Marburg, Germany;3.University of Medicine and Health Sciences, Basseterre, Saint Kitts and Nevis |
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Abstract: | Lipolytic enzymes catalyze the hydrolysis and synthesis of ester compounds. They are valuable in the pulp, food, and textile industries. This study aims to comprehensively evaluate the extreme properties of a hormone-sensitive lipase (EstATII-TM) isolated from the Red Sea Atlantis II brine pool. EstATII-TM was cloned, expressed, and its biochemical activities were assessed under different conditions. EstATII-TM catalytic properties and resistance to different metal ions were compared to commercial thermophilic esterases under different temperatures. Phylogenetically, EstATII-TM was assigned to the GDSAG motif subfamily of hormone-sensitive lipase. The optimal enzyme activity was evident at a temperature of 30 °C and pH 7–8. The enzyme retained 84.9% of its activity at 0.5 M NaCl. EstATII-TM maintained 93% to 97% activity at −40 and −20 °C, respectively. EstATII-TM activity was significantly enhanced, up to 10-fold, at temperatures ranging from 45 to 65 °C in the presence of 1 mM Cu2+, Cd2+, Ba2+, Mn2+, and Zn2+. EstATII-TM showed superior catalytic activity and resistance-to/enhancement-by metal ions compared to two commercial thermophilic esterases. The Red Sea Atlantis II brine EstATII-TM is characterized by tolerance to high temperatures, stability to hot and cold conditions, as well as toxic heavy metal contamination, making it an ideal candidate for industrial processes. |
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Keywords: | thermophilic psychrostable heavy metals commercial esterases brine pool metagenomics |
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