Effect of Enzymatic Hydrolysis on Solubility and Emulsifying Properties of Lupin Proteins (Lupinus luteus)

Solubility and emulsifying properties are important functional properties associated with proteins. However, many plant proteins have lower techno-functional properties, which limit their functional performance in many formulations. Therefore, the objective of this study was to investigate the effec...

Full description

Saved in:
Bibliographic Details
Published in:Colloids and interfaces 2022-12, Vol.6 (4), p.82
Main Authors: Opazo-Navarrete, Mauricio, Burgos-Díaz, César, Garrido-Miranda, Karla A., Acuña-Nelson, Sergio
Format: Article
Language:English
Subjects:
Alkaline protease
Analytical chemistry
By products
emulsifying properties
Enzymes
Food
Glycerol
Hydrolysates
Hydrolysis
Ingredients
Laboratories
lupin proteins
Lupins
Molecular weight
Protease
Proteases
protein hydrolysis
Proteins
Proteolysis
Seeds
Solubility
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Solubility and emulsifying properties are important functional properties associated with proteins. However, many plant proteins have lower techno-functional properties, which limit their functional performance in many formulations. Therefore, the objective of this study was to investigate the effect of protein hydrolysis by commercial enzymes to improve their solubility and emulsifying properties. Lupin protein isolate (LPI) was hydrolyzed by 7 commercial proteases using different E/S ratios and hydrolysis times while the solubility and emulsifying properties were evaluated. The results showed that neutral and alkaline proteases are most efficient in hydrolyzing lupin proteins than acidic proteases. Among the proteases, Protamex® (alkaline protease) showed the highest DH values after 5 h of protein hydrolysis. Meanwhile, protein solubility of LPI hydrolysates was significantly higher (p < 0.05) than untreated LPI at all pH analyzed values. Moreover, the emulsifying capacity (EC) of undigested LPI was lower than most of the hydrolysates, except for acidic proteases, while emulsifying stability (ES) was significantly higher (p < 0.05) than most LPI hydrolysates by acidic proteases, except for LPI hydrolyzed with Acid Stable Protease with an E/S ratio of 0.04. In conclusion, the solubility, and emulsifying properties of lupin (Lupinus luteus) proteins can be improved by enzymatic hydrolysis using commercial enzymes.
ISSN:2504-5377
2504-5377
DOI:10.3390/colloids6040082