N succ ala ala ala p nitroanilide aaavpn

Elastase assay was performed by using porcine pancreatic elastase (Sigma Aldrich, Saint Quentin Fallavier, France). The elastase activity was determined using N-Succ-Ala-Ala-Ala-p-nitroanilide (AAAVPN; Sigma Aldrich, Saint Quentin Fallavier, France) as a substrate, as described by Wittenauer et al. [34 (link)]. The release of p-nitroaniline at 410 nm using a microplate reader (BioTek ELX800; BioTek Instruments). Triplicated measurements were performed, and the anti-elastase activity was expressed, for each extract, as an inhibition percentage relative to the corresponding control (adding same volume of extraction solvent).

Elastase assay was performed by using porcine pancreatic elastase (Sigma Aldrich) and its activity was determined with spectrophotometer by making use of N-Succ-Ala-Ala-Ala-p-nitroanilide (AAAVPN; Sigma Aldrich) as a substrate and following p-nitroaniline release at 410 nm using a microplate reader (BioTek ELX800; BioTek Instruments) by adopting the method of Wittenauer et al. (2015) [78 (link)]. Triplicated measurements were used and the anti-elastase activity was expressed as a % of inhibition relative to the corresponding control (adding same volume of extraction solvent) for every extract.

For this assay, porcine pancreatic elastase (Sigma Aldrich) was used according to the protocol described by Wittenauer et al. (2015) (link). Here, N-Succ-Ala-Ala-Ala-p-nitroanilide (AAAVPN; Sigma Aldrich) was used as a substrate, and the release of p-nitroaniline was measured at 410 nm using an absorbance microplate reader (BioTek ELX800; BioTek Instruments). All the experiments were performed in triplicate, and the anti-elastase activity was expressed as a percentage of inhibition relative to the control which consisted of the same volume of extraction solvent. Oleanolic acid (10 µM) was used as the specific inhibitor of elastase leading to an inhibition of 47.8 ± 1.4%.