A mesophilic bacterium producing a thermostable alkaline lipase was isolated from oil rich soil sample and identified as Acinetobacter sp. EH28. The lipase was partially purified by ammonium sulphate precipitation followed by hydrophobic interaction chromatography with 24.2-fold purification and 57.1U/ml specific activity. The partially purified enzyme exhibited maximum activity at pH 10.0 and at 50 degrees C and was highly stable at 50 degrees C retaining 100% of its activity up to 90min. It was highly stable and retained more than 80% of its initial activity upon exposure to various organic solvents. The EH28 lipase was used for synthesis of the flavor ester ethyl caprylate in organic solvents, thus providing a concept of application of Acinetobacter sp. lipase in non-aqueous catalysis. Reaction parameters best suited for this esterification reaction were 40 degrees C reaction temperature, 1.3:1 ratio of caprylic acid to ethanol and cyclohexane as the medium.
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http://dx.doi.org/10.1016/j.biortech.2009.12.107 | DOI Listing |
Open Vet J
November 2024
Department for Clinical Sciences, University of Sarajevo-Veterinary Faculty, Sarajevo, Bosnia and Herzegovina.
Background: Age-related changes in physiological parameters are crucial in understanding the health and performance of working dogs, particularly those in demanding roles such as military and law enforcement. However, limited research exists on how aging affects the hematological and biochemical health of these dogs.
Aim: This study aims to characterize age-related variations in hematological and biochemical parameters in working Belgian Shepherd dogs to provide insights that could inform health management strategies for these animals.
Int J Biol Macromol
December 2024
College of Marine Sciences, South China Agricultural University, Guangzhou 510642, China. Electronic address:
This study aimed to investigate the effects of B. subtilis HGcc-1 supplementation on the growth performance, immunity response, antioxidant capacity, intestinal microbiota and heat stress resistance of Litopenaeus vannamei. The results showed that B.
View Article and Find Full Text PDFBioprocess Biosyst Eng
December 2024
School of Biosciences and Technology, Vellore Institute of Technology, Vellore, 632014, Tamil Nadu, India.
Lipases are one of the ubiquitous enzymes that belong to the hydrolases family and have a wide variety of applications. Cold-active lipases are of major attraction as they can act in lower temperatures and low water conditions because of their inherent greater flexibility. One of the novel applications of lipase is the enrichment of ω-3 polyunsaturated fatty acids (PUFA) in plant and fish oils.
View Article and Find Full Text PDFFoods
November 2024
Department of Chemistry, Institute of Food Sciences, Warsaw University of Life Sciences-SGGW, Nowoursynowska 159c, 02-776 Warsaw, Poland.
Enzyme immobilization is a crucial method in biotechnology and organic chemistry that significantly improves the stability, reusability, and overall effectiveness of enzymes across various applications. Lipases are one of the most frequently applied enzymes in food. The current study investigated the potential of utilizing selected agri-food and waste materials-buckwheat husks, pea hulls, loofah sponges, and yerba mate waste-as carriers for the immobilization of Sustine 121 lipase and yeast biomass as whole-cell biocatalyst and lipase sources.
View Article and Find Full Text PDFEcotoxicol Environ Saf
December 2024
College of Fisheries, Guangdong Ocean University, Zhanjiang 524088, PR China. Electronic address:
In the context of global warming, heat stress poses a threat to aquatic organisms. In the present study, a comprehensive analysis in hepatopancreas from Procambarus clarkii was conducted to examine the histology, physiological changes, and transcriptome alterations after exposed at 32 and 37 ℃ for 24 and 72 h, respectively, with 26 ℃ as the control group. The results demonstrated that the survival rate of P.
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