alexa Effects of the Two Extracted Agglutinins from Rhizoctonia Solani Kühn (Cantharellales: Ceratobasidiaceae) on Digestive Α-amylase of Pieris Brassicae L. (Lepidoptera: Pieridae)
ISSN: 2155-9600

Journal of Nutrition & Food Sciences
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Research Article

Effects of the Two Extracted Agglutinins from Rhizoctonia Solani Kühn (Cantharellales: Ceratobasidiaceae) on Digestive Α-amylase of Pieris Brassicae L. (Lepidoptera: Pieridae)

Zeynab Alborzi1, Arash Zibaee1*, Samar Ramzi2 and Jalal Jalali Sendi1

1Department of Plant Protection, Faculty of Agricultural Science, University of Guilan, Rasht, Iran

2Department of Plant Protection, Tea Research Institute of Iran, Lahijan, 77555-44159, Iran

Corresponding Author:
Arash Zibaee
Department of Plant Protection
Faculty of Agricultural Science
University of Guilan
Rasht, Iran
Tel: 416351314
E-mail: [email protected]; [email protected]

Received date: May 21, 2016; Accepted date: June 17, 2016; Published date: June 23, 2016

Citation: Alborzi Z, Zibaee A, Ramzi S, Jalali Sendi J (2016) Effects of the Two Extracted Agglutinins from Rhizoctonia Solani Kühn (Cantharellales: Ceratobasidiaceae) on Digestive Α-amylase of Pieris Brassicae L. (Lepidoptera: Pieridae). J Nutr Food Sci 6:526. doi: 10.4172/2155-9600.1000526

Copyright: © 2016 Alborzi Z, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Two galactose specific lectins, RSAI and RSAII, were purified from sclerotia of Rhizoctonia solani Kühn and their inhibitory effects were assessed on digestive α-amylase of Pieris brassicae Linnaeus. Results revealed molecular weight of 16 and 15.7 kDa and IC50 inhibitory concentration of 0.87 and 1.68 mg/ml for RSAI and RSAII, respectively. In native-PAGE experiment, both RSAs provoked disappearance of A2 band of the enzyme and decreased sharpness of A1 band. Determination of α-amylase kinetic parameters using Lineweaver-Burk analysis revealed that compared to the control, both lectins reduced Vmax while Km was increased only in the presence of RSAII. Therefore, kinetic parameters indicated non-competitive and mixed inhibitions for RSAI and RSAII, respectively. Moreover, RSAI and RSAII showed the highest inhibition within pH and temperature range optimal for enzyme activity in the control group, i.e., at pH values of 9 (RSAI) and 11 (RSAII) and temperature of 30°C. Incubation of RSAs at 50, 60 and 70°C showed high stability of RSAII while RSAI lost inhibitory potential at 70°C. Results of the current study clearly indicate negative in vitro effects of RSAs on digestive α-amylase of P. brassicae.

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