Optimizing and purifying extracellular cold- active lipase from Talaromyces pinophilus AUMC 308 for potential use in industrial detergents
Omar, A., Zohri, A., Abdel-Malek, A., Al-Bedak, O. (2025). Optimizing and purifying extracellular cold- active lipase from Talaromyces pinophilus AUMC 308 for potential use in industrial detergents. EKB Journal Management System, 54(2), 329-357. doi: 10.21608/aunj.2025.347975.1113
Asmaa M.A. Omar; Abdel-Nasser A. Zohri; Ahmed Y. Abdel-Malek; Osama Abdel-Hafeez Mohamed Al-Bedak. "Optimizing and purifying extracellular cold- active lipase from Talaromyces pinophilus AUMC 308 for potential use in industrial detergents". EKB Journal Management System, 54, 2, 2025, 329-357. doi: 10.21608/aunj.2025.347975.1113
Omar, A., Zohri, A., Abdel-Malek, A., Al-Bedak, O. (2025). 'Optimizing and purifying extracellular cold- active lipase from Talaromyces pinophilus AUMC 308 for potential use in industrial detergents', EKB Journal Management System, 54(2), pp. 329-357. doi: 10.21608/aunj.2025.347975.1113
Omar, A., Zohri, A., Abdel-Malek, A., Al-Bedak, O. Optimizing and purifying extracellular cold- active lipase from Talaromyces pinophilus AUMC 308 for potential use in industrial detergents. EKB Journal Management System, 2025; 54(2): 329-357. doi: 10.21608/aunj.2025.347975.1113

Optimizing and purifying extracellular cold- active lipase from Talaromyces pinophilus AUMC 308 for potential use in industrial detergents

Assiut University Journal of Multidisciplinary Scientific Research
Volume 54, Issue 2, May 2025, Page 329-357  XML PDF (631.32 K)
Document Type: Novel Research Articles
DOI: 10.21608/aunj.2025.347975.1113
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Authors
Asmaa M.A. Omar email orcid 1; Abdel-Nasser A. Zohriorcid 2; Ahmed Y. Abdel-Malekorcid 1; Osama Abdel-Hafeez Mohamed Al-Bedakorcid 3
1Department of Botany and Microbiology, Faculty of Science, Assiut University, Assiut, Egypt
2Department of Botany and Microbiology, Faculty of Science, Assiut University, Assiut 71516, Egypt
3Assiut University Mycological Centre
Abstract
In this study, a strain of Talaromyces pinophilus AUMC 308 was used. The 15th days of fermentation at pH 6.0, 15°C with ammonium chloride as the nitrogen source were shown to be the optimal settings for the synthesis of the enzyme. This enzyme was purified 3.57 times using diethylaminoethyl cellulose (DEAE cellulose) then use column chromatography (Sephadex G-75), yielding 189.35 U.mg-1 protein as specific activity with 14.5% yield. The purified cold active lipase exhibited pH stability within a pH range of 4-7, with an optimum pH of 6 yielding 196.08 U.mg-1 as specific activity. The molecular weight of the purified cold active lipase was 30-60 KDa, according to the SDS PAGE. Also, the enzyme exhibits a broad temperature tolerance within 5 – 20ºC with an optimal temperature for specific enzyme activity was 15ºC, yielding 196.08 U.mg-1. Cu2+ ions had the greatest activation impact (126%) when added, followed by Mn2+ (121.75%), Zn2+ (119.5%), Fe2+ (115.22%), Ni2+ (110.83%), and Ca2+ (110.8%). The Km and Vmax for purified enzyme were 25. 16 mg.mL-1, 312.5 µmol.min-1, respectively. The purified lipase showed the most specific activity (262.25 U.mg-1) on Tween 20, followed by olive, sunflower, corn, sesame oils and Tween 80 which displayed 257.35, 237.75, 235.29, 232.84, and 196.08 U.mg-1, respectively.
Keywords
Enzymes; Purification; Sephadex G-75; Cold-active lipases; Penicillium Talaromyces
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