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Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases

Optimization of the enzymolysis process for preparing peanut protein hydrolysates using alcalase and trypsin was performed by employing the central composite design (CCD) of response surface methodology (RSM). The independent variables were solid-to-liquid ratio (S/L), enzyme-to-substrate ratio (E/S...

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Autores principales: AL-Bukhaiti, Wedad Q., Al-Dalali, Sam, Noman, Anwar, Qiu, Silin, Abed, Sherif M., Qiu, Sheng-Xiang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9602261/
https://www.ncbi.nlm.nih.gov/pubmed/37431052
http://dx.doi.org/10.3390/foods11203303
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author AL-Bukhaiti, Wedad Q.
Al-Dalali, Sam
Noman, Anwar
Qiu, Silin
Abed, Sherif M.
Qiu, Sheng-Xiang
author_facet AL-Bukhaiti, Wedad Q.
Al-Dalali, Sam
Noman, Anwar
Qiu, Silin
Abed, Sherif M.
Qiu, Sheng-Xiang
author_sort AL-Bukhaiti, Wedad Q.
collection PubMed
description Optimization of the enzymolysis process for preparing peanut protein hydrolysates using alcalase and trypsin was performed by employing the central composite design (CCD) of response surface methodology (RSM). The independent variables were solid-to-liquid ratio (S/L), enzyme-to-substrate ratio (E/S), pH, and reaction temperature, while the response variables were degree of hydrolysate (DH), α-amylase, and α-glucosidase inhibitory activity. The highest DH (22.84% and 14.63%), α-amylase inhibition (56.78% and 40.80%), and α-glucosidase inhibition (86.37% and 86.51%) were obtained under optimal conditions, which were S/L of 1:26.22 and 1:30 w/v, E/S of 6% and 5.67%, pH of 8.41 and 8.56, and temperature of 56.18 °C and 58.75 °C at 3 h using alcalase (AH) and trypsin (TH), respectively. Molecular weight distributions of peanut protein hydrolysates were characterized by SDS-PAGE, which were mostly ˂10 kDa for both hydrolysates. Lyophilized AH and TH had IC(50) values of 6.77 and 5.86 mg/mL for α-amylase inhibitory activity, and 6.28 and 5.64 mg/mL for α-glucosidase inhibitory activity. The IC(50) of AH and TH against DPPH radical was achieved at 4.10 and 3.20 mg/mL and against ABTS radical at 2.71 and 2.32 mg/mL, respectively. The obtained hydrolysates with antidiabetic activity could be utilized as natural alternatives to synthetic antidiabetics, particularly in food and pharmaceutical products.
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spelling pubmed-96022612022-10-27 Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases AL-Bukhaiti, Wedad Q. Al-Dalali, Sam Noman, Anwar Qiu, Silin Abed, Sherif M. Qiu, Sheng-Xiang Foods Article Optimization of the enzymolysis process for preparing peanut protein hydrolysates using alcalase and trypsin was performed by employing the central composite design (CCD) of response surface methodology (RSM). The independent variables were solid-to-liquid ratio (S/L), enzyme-to-substrate ratio (E/S), pH, and reaction temperature, while the response variables were degree of hydrolysate (DH), α-amylase, and α-glucosidase inhibitory activity. The highest DH (22.84% and 14.63%), α-amylase inhibition (56.78% and 40.80%), and α-glucosidase inhibition (86.37% and 86.51%) were obtained under optimal conditions, which were S/L of 1:26.22 and 1:30 w/v, E/S of 6% and 5.67%, pH of 8.41 and 8.56, and temperature of 56.18 °C and 58.75 °C at 3 h using alcalase (AH) and trypsin (TH), respectively. Molecular weight distributions of peanut protein hydrolysates were characterized by SDS-PAGE, which were mostly ˂10 kDa for both hydrolysates. Lyophilized AH and TH had IC(50) values of 6.77 and 5.86 mg/mL for α-amylase inhibitory activity, and 6.28 and 5.64 mg/mL for α-glucosidase inhibitory activity. The IC(50) of AH and TH against DPPH radical was achieved at 4.10 and 3.20 mg/mL and against ABTS radical at 2.71 and 2.32 mg/mL, respectively. The obtained hydrolysates with antidiabetic activity could be utilized as natural alternatives to synthetic antidiabetics, particularly in food and pharmaceutical products. MDPI 2022-10-21 /pmc/articles/PMC9602261/ /pubmed/37431052 http://dx.doi.org/10.3390/foods11203303 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
AL-Bukhaiti, Wedad Q.
Al-Dalali, Sam
Noman, Anwar
Qiu, Silin
Abed, Sherif M.
Qiu, Sheng-Xiang
Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases
title Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases
title_full Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases
title_fullStr Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases
title_full_unstemmed Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases
title_short Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases
title_sort response surface modeling and optimization of enzymolysis parameters for the in vitro antidiabetic activities of peanut protein hydrolysates prepared using two proteases
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9602261/
https://www.ncbi.nlm.nih.gov/pubmed/37431052
http://dx.doi.org/10.3390/foods11203303
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