2010
DOI: 10.1016/j.soilbio.2009.11.015
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A modified method based on p-nitrophenol assay to quantify hydrolysis activities of lipases in litters

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Cited by 18 publications
(13 citation statements)
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“…Thus, we were able to more accurately determine the interactions between substrates (i.e. both water and p-nitrophenyl laurate), enzymes and the vegetal matrix which drive enzyme activity rates under low water content conditions (Farnet et al, 2010;Goujard et al, 2009). We did not compare lipase activities in the two types of litters quantitatively, since variations in the chemical composition of litter are known to shape microbial community structure and in turn the amount of extracellular enzymes produced (Fioretto et al, 2009;Papa et al, 2008).…”
Section: Discussionmentioning
confidence: 99%
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“…Thus, we were able to more accurately determine the interactions between substrates (i.e. both water and p-nitrophenyl laurate), enzymes and the vegetal matrix which drive enzyme activity rates under low water content conditions (Farnet et al, 2010;Goujard et al, 2009). We did not compare lipase activities in the two types of litters quantitatively, since variations in the chemical composition of litter are known to shape microbial community structure and in turn the amount of extracellular enzymes produced (Fioretto et al, 2009;Papa et al, 2008).…”
Section: Discussionmentioning
confidence: 99%
“…Enzyme activities were measured from litters for different a w values as described by Farnet et al (2010). This assay was adapted for litters from the method of Pencreac'h and Baratti (1996) using methyl t-butyl ether as the organic solvent of the reaction mixture.…”
Section: Lipase Hydrolytic Activitiesmentioning
confidence: 99%
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“…Lipase activity was measured in accordance with Farnet et al . () with p ‐nitrophenyl ( p NP) laurate as substrate. Protease activity was determined using the method of Ladd & Butler ().…”
Section: Methodsmentioning
confidence: 99%
“…Lipase, urease and protease activities were measured directly in the soil. The hydrolysis activity of lipases was measured according to Farnet et al (2010b) using p-nitrophenyl laurate as substrate dissolved in an organic solvent. The release of p-nitrophenol was measured at 412 nm after 2 h-incubation at 30 C. The urease activity was measured using the method of Kandeler and Gerber (1988) based on the determination of NH þ 4 after enzyme action on urea at 37 C for 2 h. Protease activity was determined using 1 g of dry soil equivalent in a 2% casein solution in tris(hydroxymethyl) aminomethane buffer (50 mM, pH 8.1) incubated for 3 h at 50 C. After incubation, the reaction was stopped using trichloroacetic acid (TCA) 15% and the mixture was centrifuged for 10 min at 10 000 rpm.…”
Section: Enzymatic Activitiesmentioning
confidence: 99%