Foaming and Structural Studies on the Acidic Subunit of Amaranth 11S Globulin Modified with Antihypertensive Peptides as a Function of pH and Ionic Strength.

Autor: Aguilar-Farrera D; Centro de Investigación en Biotecnología Aplicada, Instituto Politécnico Nacional, Carretera Estatal Tecuexcomac-Tepetitla Km 1.5, Tepetitla 90700, Mexico., Morales-Camacho JI; Departamento de Ingeniería Química, Alimentos y Ambiental, Universidad de las Américas Puebla, Sta. Catarina Mártir, San Andrés Cholula 72810, Mexico., Espinosa-Hernández E; Centro de Investigación en Biotecnología Aplicada, Instituto Politécnico Nacional, Carretera Estatal Tecuexcomac-Tepetitla Km 1.5, Tepetitla 90700, Mexico.; Departamento de Ingeniería Química, Alimentos y Ambiental, Universidad de las Américas Puebla, Sta. Catarina Mártir, San Andrés Cholula 72810, Mexico., Benítez-Cardoza CG; Laboratorio de Investigación Bioquímica, ENMyH-IPN, Instituto Politécnico Nacional, Mexico City 07320, Mexico., Jara-Romero GJ; Centro de Investigación en Biotecnología Aplicada, Instituto Politécnico Nacional, Carretera Estatal Tecuexcomac-Tepetitla Km 1.5, Tepetitla 90700, Mexico., Luna-Suárez S; Centro de Investigación en Biotecnología Aplicada, Instituto Politécnico Nacional, Carretera Estatal Tecuexcomac-Tepetitla Km 1.5, Tepetitla 90700, Mexico.
Jazyk: angličtina
Zdroj: Molecules (Basel, Switzerland) [Molecules] 2022 May 31; Vol. 27 (11). Date of Electronic Publication: 2022 May 31.
DOI: 10.3390/molecules27113538
Abstrakt: Some studies aimed at revealing the relationship between protein structure and their functional properties. However, the majority of these reports have been carried out using protein isolates. There are limited reports on the possible relationship between the functional properties and the structure of a purified protein. In this work the amaranth 11S globulin acidic subunit (AAC) and five mutations of the same protein that were modified in their variable regions with antihypertensive peptides (VYVYVYVY and RIPP), were analyzed at two ionic strength (2.9 and 17.6 g/L NaCl) and pH (3.0-7.0). Results revealed better solubility for the proteins mutated at the terminal ends (AACM.1 and AACM.4) and lower solubility for the protein inserted with RIPP peptide. Spectroscopy studies revealed an increase of β-sheet structure at high salt concentration for all proteins. It was also observed that salt concentration acted as a modulator, which allowed a better foam features for all modified proteins limiting movement of side chains and reducing red-shifted displacement of λmax. All proteins showed foam capacity ranging from 76 to 93% although foam stability was twofold better for modified proteins than for AAC at high salt concentration. This study allowed better understanding about the structural changes that influence the foaming properties of engineered proteins.
Databáze: MEDLINE
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