The use of lipases from animal sources for the synthesis of new biocatalysts is barely studied in the literature. The present work focused on the immobilization of lipases from kid goat's and lamb's epiglottis in different ionic supports. For this, anionic supports (monoaminoethyl-N-aminoethyl-agarose (MANAE) and diethylaminoethyl-agarose (DEAE)) and cationic supports (carboxymethyl-agarose and sulfopropyl-agarose) were used. The immobilization parameters were evaluated, as well as the thermal stability of the immobilized enzymes and their stability at different values of pH. Then, the performance of the biocatalysts was evaluated in hydrolysis reactions for obtaining omega-3 fatty acids from fish oil (eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA)). Values of 100% of recovered activity were obtained for lipase from goats, indicating that it was possible to maintain all the enzymatic activities of the immobilized enzymes on the supports. The immobilized enzymes were more stable in different pH conditions and at a temperature of 50 °C, reaching values of stabilization factor of 12.17 and t of 9.86 h, for lamb lipase immobilized in sulfopropyl agarose. In general, the anionic supports led to lower Km values and the cationic ones to a higher Vmax. Lamb lipase showed the highest selectivity values for EPA/DHA, reaching values of 6.43 using MANAE. Thus, the high potential for using such biocatalysts from animal sources in the food or pharmaceutical industries is observed.
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http://dx.doi.org/10.1007/s12010-024-04942-2 | DOI Listing |
Sci Rep
January 2025
Department of Nanotechnology, Agricultural Biotechnology Research Institute of Iran (ABRII), Agricultural Research Education and Extension Organization (AREEO), P. O. Box: 31535-1897, Karaj, Iran.
Herein, an efficient and feasible approach was developed to oxidize low-cost agricultural waste (quinoa husk, QS) for the synthesis of carboxylated nanocellulose (CNC). The as-prepared rod-like CNCs (average diameter of 10 nm and length of 103 nm) with a high specific surface area (173 m/g) were utilized for the immobilization of a model protease enzyme (PersiProtease1) either physically or via covalent attachment. For chemical immobilization, CNCs were firstly functionalized with N, N'-dicyclohexylcarbodiimide (DCC) to provide DCNCs nanocarrier which could covalently bond to enzyme trough nucleophilic substitution reaction and formation of the amide bond between DCNCs and enzyme.
View Article and Find Full Text PDFAdv Mater
December 2024
MOE International Joint Research Laboratory on Synthetic Biology and Medicines, School of Biology and Biological Engineering, South China University of Technology, Guangzhou, 510006, P. R. China.
The development of novel methods to enhance enzyme-carrier interactions in situ, at a feasible cost, and on a large scale is crucial for improving the stability and durability of current immobilized enzyme systems used in industrial settings. Here, a pioneering approach termed "silica-based inorganic glue" is proposed, which utilizes protein-catalyzed silicification to fix enzyme within porous matrix while preserving enzyme activity. This innovative strategy offers several key benefits, including conformational stabilization of enzymes, improved interactions between enzymes and the matrix, prevention of enzyme leakage, and mitigation of pore blocking.
View Article and Find Full Text PDFCurr Opin Chem Biol
December 2024
Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA; Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA. Electronic address:
Enzymes catalyze molecular reactions with remarkable efficiency and selectivity under mild conditions. Photoactivated enzymes make use of a light-absorbing chromophore to drive chemical transformations, ideally using sunlight as an energy source. The direct attachment of a chromophore to native enzymes is advantageous, as information on the underlying catalytic mechanisms can be obtained.
View Article and Find Full Text PDFJ Am Chem Soc
December 2024
School of Chemical Engineering, The University of Queensland, St Lucia, QLD 4072, Australia.
The development of efficient artificial photosynthesis systems is crucial for sustainable chemical production, as they mimic natural processes to convert solar energy into chemical products, thereby addressing both energy and environmental challenges. The main bottlenecks in current research include fabricating highly selective, stable, and scalable catalysts, as well as effectively harnessing the full spectrum of light, particularly the low-energy, long-wavelength portion. Herein, we report a novel composite photocatalyst system based on lead halide perovskites embedded in functionalized MOF glass.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
School of Chemical Engineering, Yeungnam University, 280 Daehak-ro, Gyeongsan 38541, South Korea; Research Institute of Cell Culture, Yeungnam University, 280 Daehak-ro, Gyeongsan 38541, South Korea. Electronic address:
Meticulous and bespoke fabrication of structural materials with simple yet innovative outlines along with on-demand availability is the imperative aspiration for numerous fields. The alliance between nanotechnology and enzymes has led to the establishment of an inimitable and proficient class of materials. With the advancement in the field of additive manufacturing, the fabrication of some complex biological architects is achievable with similitude to the instinctive microenvironment of the biological tissue.
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