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超声辅助美拉德反应对牡蛎蛋白酶解产物功能特性和风味特性的影响。

Effect of ultrasound-assisted Maillard reaction on functional properties and flavor characteristics of Oyster protein enzymatic hydrolysates.

机构信息

College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China; College of Food Science and Engineering, Guangdong Ocean University, Yangjiang 529500, China; Branch of Chemistry and Chemical Engineering Guangdong Laboratory (Hanjiang Laboratory), Chaozhou 521000, China; Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Zhanjiang 524088, China.

College of Food Science and Engineering, Guangdong Ocean University, Yangjiang 529500, China; Branch of Chemistry and Chemical Engineering Guangdong Laboratory (Hanjiang Laboratory), Chaozhou 521000, China; Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Zhanjiang 524088, China.

出版信息

Ultrason Sonochem. 2024 Dec;111:107113. doi: 10.1016/j.ultsonch.2024.107113. Epub 2024 Oct 16.

DOI:10.1016/j.ultsonch.2024.107113
PMID:39442458
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11532777/
Abstract

To address the delamination phenomenon during storage and flavor characteristics of Oyster protein hydrolysates (OPH). In this study, xylo-oligosaccharides (XOS) were selected to covalently graft with OPH through ultrasound-assisted Maillard reaction, and the effect of ultrasound-assisted Maillard reaction on the structure, functional properties, and flavor characteristics of OPH were investigated. The results revealed that the ultrasound treatment led to a 1.46-fold increase in the degree of grafting compared with the conventional wet-heat Maillard reaction methods. Structural analyses at various levels indicated substantial alterations in the OPH structure following the ultrasound-assisted Maillard reaction. More ordered α-helical secondary structures were shifting to random coiling, the tertiary structure showed more stretching changes, and the surface structure was characterized by loose and porous features. Compared with OPH, the solubility of the ultrasound-assisted Maillard reaction products (OPH-U-M) increased from 54.67% to 70.14%, leading to a notable enhancement in storage stability. Flavor profile analysis demonstrated a decrease in unsaturated aldehydes and ketones presenting fishy and bitter aromas, while an increase in presenting meat aroma compounds was observed in OPH-U-M. Furthermore, OPH-U-M exhibited superior antioxidant properties with DPPH and ABTS radical scavenging abilities enhancing 46.05% and 42.09% in comparison with OPH, respectively. The results demonstrated that covalently binding with XOS under ultrasonication pretreatment endowed OPH with superior functional properties (including solubility, storage stability, and antioxidant activity), and the improvement of flavor profile. This study can provide theoretical guidance and practical implications for promoting the processing applications of oyster protein.

摘要

为了解决牡蛎蛋白水解物(OPH)在储存过程中的分层现象和风味特征。在这项研究中,木二糖(XOS)被选择通过超声辅助美拉德反应与 OPH 共价接枝,并研究了超声辅助美拉德反应对 OPH 的结构、功能特性和风味特征的影响。结果表明,与传统的湿热美拉德反应方法相比,超声处理导致接枝程度增加了 1.46 倍。在各个层次的结构分析表明,超声辅助美拉德反应后 OPH 的结构发生了显著变化。更多有序的α-螺旋二级结构向无规卷曲转变,三级结构显示出更多的拉伸变化,表面结构具有疏松多孔的特征。与 OPH 相比,超声辅助美拉德反应产物(OPH-U-M)的溶解度从 54.67%增加到 70.14%,从而显著提高了储存稳定性。风味分析表明,不饱和醛酮的含量降低,呈现出鱼腥味和苦味的香气,而呈现出肉香的化合物在 OPH-U-M 中增加。此外,与 OPH 相比,OPH-U-M 具有更好的抗氧化性能,DPPH 和 ABTS 自由基清除能力分别提高了 46.05%和 42.09%。结果表明,在超声预处理下与 XOS 共价结合,赋予 OPH 更好的功能特性(包括溶解度、储存稳定性和抗氧化活性),并改善了风味特征。本研究可为促进牡蛎蛋白的加工应用提供理论指导和实际意义。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/2aa72cd9d67a/gr10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/e1d1225b5e3e/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/71a5dc57e494/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/5c524bb8ab43/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/f1c8d4bcdfec/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/a7d9151bec9f/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/56025c52b9f0/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/6fb72d34e202/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/719682bda8cd/gr8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/cdd1519e8ed9/gr9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/2aa72cd9d67a/gr10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/e1d1225b5e3e/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/71a5dc57e494/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/5c524bb8ab43/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/f1c8d4bcdfec/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/a7d9151bec9f/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/56025c52b9f0/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/6fb72d34e202/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/719682bda8cd/gr8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/cdd1519e8ed9/gr9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c6f0/11532777/2aa72cd9d67a/gr10.jpg

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