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http://dx.doi.org/10.1016/j.biortech.2024.130382 | DOI Listing |
Appl Biochem Biotechnol
January 2025
Unidad de Biotecnología Industrial, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C, 45019, Zapopan, Jal, Mexico.
Lipases from the basidiomycete fungus Ustilago maydis are promising but underexplored biocatalysts due to their high homology with Candida antarctica lipases. This study provides a comprehensive characterization of a recombinant CALB-like lipase from U. maydis, expressed in Pichia pastoris (rUMLB), and compares its properties with those of the well-studied recombinant lipase B from C.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Department of Agricultural and Environmental Biotechnology, São Paulo State University (UNESP), School of Agricultural and Veterinarian Sciences, Jaboticabal, São Paulo, Brazil; Institute of Bioenergy Research (IPBEN), Jaboticabal, São Paulo, Brazil. Electronic address:
This study characterized a novel bacterial lipase with high biotechnological potential, focusing on industrial and environmental applications. Bacterial isolates were screened using olive oil as a substrate, and the strain with the highest hydrolytic halo was identified as Burkholderia sp. via 16S rRNA analysis.
View Article and Find Full Text PDFBioorg Chem
January 2025
Department of Bioengineering, Gebze Technical University, 41400, Gebze, Kocaeli, Türkiye; BAUZYME Biotechnology Co., Gebze Technical University Technopark, 41400, Gebze, Kocaeli, Türkiye. Electronic address:
α-Amylases, constituting a significant share of the enzyme market, are mainly synthesized by the genus Bacillus. Enzymes tailored for specific industrial applications are needed to meet the growing demand across a range of industries, and thus finding new amylases and optimizing the ones that already exist are extremely important. This study reports the successful expression, characterization and immobilization of P.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
College of Life Science, Northwest A&F University, Yangling 712100, China. Electronic address:
Amycolatopsis sp. BJA-103 was isolated for its exceptional feather-degradation capability, leading to the purification, cloning, and heterologous expression of the keratinase enzyme, KER0199. Sequence analysis places KER0199 within the S8 protease family, revealing <60 % sequence similarity to known proteases.
View Article and Find Full Text PDFVaccines (Basel)
December 2024
Laboratory of Molecular Studies and Experimental Therapy-LEMTE, Department of Genetics, Federal University of Pernambuco, Recife 50670-901, Brazil.
Background/objectives: DNA vaccines are rapidly produced and adaptable to different pathogens, but they face considerable challenges regarding stability and delivery to the cellular target. Thus, effective delivery methods are essential for the success of these vaccines. Here, we evaluated the efficacy of capsules derived from the cell wall of the yeast as a delivery system for DNA vaccines.
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