Enzyme-controlled hygroscopicity and proton dynamics in sea cucumber (Stichopus japonicus) ovum peptide powders

摘要: The enzyme-controlled hygroscopicity of peptide powders during storage at room temperature may have a profound effect on their properties. present study aims to elucidate hygroscopicity, proton dynamics, as well the microstructure sea cucumber ovum peptides (SCOPs) powder produced with different enzymes storage. SCOPs Alcalase exhibited strongest moisture absorption capacity, which was significantly higher than those papain, neutrase, and trypsin (P < .05). This might be attributed greater hydrolysis producing more polar groups. Moreover, dynamic transformations water populations varied greatly among enzymes. Even so, common migration rule that free gradually transformed into immobilized simultaneously converted bound after absorption. induced morphological changes SCOPs, from smooth amorphous structure sizes particle agglomerates. displayed smaller agglomerates trypsin. provides theoretical basis for quality assurance powders, particularly Alcalase.