High‐intensity ultrasound improves threadfin bream surimi gelation at low NaCl contents

化学 食品科学 扫描电子显微镜 傅里叶变换红外光谱 核化学 材料科学 化学工程 有机化学 工程类 复合材料
作者
Ling Tang,Jirawat Yongsawatdigul
出处
期刊:Journal of Food Science [Wiley]
卷期号:86 (3): 842-851 被引量:24
标识
DOI:10.1111/1750-3841.15637
摘要

Abstract Effects of high‐intensity ultrasound (HIU) treatments on gelation of threadfin bream ( Nemipteru s spp.) surimi at various NaCl contents (0.5, 1, and 2% NaCl) were investigated. Protein extractability at 0.5% NaCl was increased with the ultrasonic intensity ( p < 0.05). At all tested NaCl contents, reactive sulfhydryl group (SH) content and surface hydrophobicity of the surimi pastes were increased after HIU treatments and were accompanied by a decrease in the Ca 2+ ‐ATPase activity and total SH content, indicating a greater extent of unfolding and conformational changes induced by HIU at higher NaCl contents. Textural properties and color of the surimi gels at 0.5% NaCl were improved concomitant to an increase in ultrasonic intensity ( p < 0.05), whereas HIU treatments resulted in inferior gels at 1 and 2% NaCl. Scanning electron microscopy (SEM) revealed that HIU resulted in a more orderly gel network at 0.5% NaCl. Fourier transform infrared (FT‐IR) spectroscopy indicated that the α‐helix content of the surimi gels was decreased as the ultrasonic intensity and NaCl content increased, confirming that structural changes induced by HIU were more profound at higher NaCl contents. The results suggested that HIU technology can be applied to improve only the 0.5% NaCl surimi gel. Practical Application High‐intensity ultrasound (HIU) improved surimi gel containing 0.5% NaCl due to an increase in protein extractability and protein conformational changes. It is likely to lay a theoretical foundation for utilization of HIU technology in production of surimi‐based products at low/reduced salt levels.
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