Title: In vitro Inhibitory Studies and Effect of Selected Plant Extracts and Cations on Elastase (EC 3.4.21.11) Activity produced by Aspergillus niger and Aspergillus flavus
Abstract:Elastase is a member of the serine protease enzyme family that hydrolytically degrades elastin, a connective tissue component leading to aging and wrinkling of the skin. In this report, we investigate...Elastase is a member of the serine protease enzyme family that hydrolytically degrades elastin, a connective tissue component leading to aging and wrinkling of the skin. In this report, we investigated the in-vitro inhibitory effects of some cations and n-hexane extract of Hibiscus cannabinus , Vernonia amygdalina , Murraya koenigii , and Telfairia occidentalis on the activity of Elastase isolated from Aspergillus flavus and Aspergillus niger . Elastase was extracted, isolated and partially purified from Aspergillus flavus and Aspergillus niger. The data obtained in this study demonstrated that the activity of elastase in Aspergillus flavus was higher compared to that of Aspergillus niger after salting out. The elastase inhibition activities of Hibiscus cannabinus, Vernonia amygdalina, Murraya koenigii, and Telfairia occidentalis reveal that the leaf extract from Murraya koenigii, in Aspergillus flavus had more significant inhibition was obtained compared to that of Aspergillus niger, with inhibitory effect from 40µg/ml. While that of Hibiscus cannabinus showed similar inhibition characteristics to Murraya koenigii. Both Hibiscus cannabinus and Vernonia amygdalina had an effect at 80µg/ml; all the extracts appeared to have more effects on the enzyme obtained from Aspergillus flavus than from the Aspergillus niger. The potential of exploring these plant extract as an anti-aging recipe was discussed. Keywords: Inhibitory studies, Elastase, Aspergillus flavus , Aspergillus niger , Hibiscus cannabinus , Vernonia amygdalina , Murraya koenigii , and Telfairia occidentalisRead More
Publication Year: 2016
Publication Date: 2016-01-01
Language: en
Type: article
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