Enzyme-controlled hygroscopicity and proton dynamics in sea cucumber (Stichopus japonicus) ovum peptide powders. (October 2018)

• Record Type: Journal Article
• Authors: Wang, Ke; Sun, Na; Li, Dongmei; Cheng, Sheng; Song, Liang; Lin, Songyi
• Is Part Of: Food research international. Volume 112(2018)
• Page Start: 241
• Page End: 249
• Publication Date: 2018-10
• Subjects: SCOPs Sea cucumber ovum peptides -- ANOVA Analysis of variance -- SD Standard deviation -- RH Relative humidity -- DVS Dynamic vapor sorption -- EMC Equilibrium moisture content -- LF-NMR Low field-nuclear magnetic resonance -- CPMG Carr–Purcell–Meiboom–Gill -- SW Spectral width -- NS Scan repetitions -- NECH Echo count -- TW Waiting time -- FTIR Fourier transform infrared -- SEM Scanning electron microscopy; Sea cucumber ovum peptide -- Hygroscopicity -- Proton dynamics -- Morphological changes -- Enzyme; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2018.06.040
• Languages: English
• ISSNs: 0963-9969

Abstract

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