Colloids and Interfaces (Dec 2022)

Effect of Enzymatic Hydrolysis on Solubility and Emulsifying Properties of Lupin Proteins (<i>Lupinus luteus</i>)

  • Mauricio Opazo-Navarrete,
  • César Burgos-Díaz,
  • Karla A. Garrido-Miranda,
  • Sergio Acuña-Nelson

DOI
https://doi.org/10.3390/colloids6040082
Journal volume & issue
Vol. 6, no. 4
p. 82

Abstract

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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 Lupinus luteus) proteins can be improved by enzymatic hydrolysis using commercial enzymes.

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