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Alcalase hydrolysis enhances solubility and foaming properties of perilla protein isolate through structural modification
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DOI：10.1007/s00217-026-05241-2.png)
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Abstract
En 中文
The limited functional properties of plant proteins remain a major challenge for their application in food systems. This study investigated the structural and functional modifications of perilla protein isolate (PPI) hydrolysates produced by Alcalase enzyme hydrolysis (EH) at varying degrees of hydrolysis (DH) of 5%, 10%, and 15% to elucidate structure–function relationships. Scanning electron microscopy revealed that PPI morphology changed from a flake-like structure with sharp edges to a smooth edge protrusion with small pores after EH. The particle size of PPI decreased from 33,836 to 522.5 nm along with increased surface charge from − 22.3 to -25.6 mV after EH. The surface hydrophobicity decreased from 8.65 to 0.23 µg CBBG bound as DH% increased. EH results in changes in protein conformation, including fluorescence quenching, increased UV-visible absorption at 280 nm, and free sulfhydryl content. Furthermore, protein molecular flexibility increased after EH, as the α-helix/β-sheet ratio decreased from 0.09 to 0.05. The protein solubility progressively improved with DH, reaching 64% at pH 3 and 86% at pH 7 for 10% DH hydrolysates. Furthermore, foaming capacity increased markedly from 17% in native PPI to 54.8% after 10% DH. In contrast, the water- and oil-holding capacities decreased from 5.5 to 1 g/g and from 4.2 to 2.6 g/g after 15% DH. 5% DH increased the thermal denaturation temperature of PPI from 110.9 to 116.9 °C. These findings suggest that controlled Alcalase hydrolysis effectively enhances the structural adaptability and techno-functional attributes of PPI, particularly solubility and foaming, which are critical for its incorporation into plant-based food formulations as a potential foaming agent.
Keywords:
Enzymatic hydrolysis
Perilla protein isolate
Functional properties
Degree of hydrolysis
Solubility
Foaming capacity and stability
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