Role of ovomucoid in the gelation of a β-lactoglobulin-ovomucoid mixture

Yuno‐Ohta, Naoko; Kato, T.; Ashizawa, Shiho; Kimura, Yoko; Maruyama, Nami; Nishizu, Takahisa

doi:10.1007/s00396-016-3864-0

Cited by 10 publications

(5 citation statements)

References 19 publications

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“…Heating milk at an elevated temperature (>70 8C) causes denaturation of whey protein, which in turn produces complexes with j-casein at the surface of casein micelles via disulfide bond formation or hydrophobic interactions (Lucey, Tamehana, Singh, & Munro, 1998a). b-Lactoglobulin is one of the major globular proteins in whey protein; it contains two disulfide bridges and one free cysteine which becomes exposed at high temperature (Alting, Hamer, de Kruif, & Visschers, 2000;Yuno-Ohta et al, 2016). Denatured b-lactoglobulin initiates the thiol disulfide (SH-SS) interchange reaction with casein micelles and formation of covalent bonds, a process that contributes to the strength of yogurt gel.…”

Section: Practical Applicationsmentioning

confidence: 99%

Physical, rheological, and microstructural properties of whey protein enriched yogurt influenced by heating the milk at different pH values

Mahomud

Katsuno

Zhang

et al. 2017

J Food Process Preserv

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Here, we investigate the effects of pH adjustment before heating milk on the textural properties of whey protein enriched yogurt. Whey protein enriched skim milk was adjusted to pH of 6.3, 6.7, and 7.1 followed by heating at 85 °C for 30 min. Yogurts prepared from milk heated at pH 6.7 showed remarkably higher G′ (storage modulus) values, water holding capacity and firmness compared to those prepared from unheated milk, or milk heated at pH 6.3 or 7.1. A relatively more compact protein network was observed in the yogurt made from milk heated at pH 6.7. Heating milk at pH 6.7 formed both whey protein‐associated casein micelles (WPA‐CM) and soluble whey protein/κ‐casein complexes (SWP‐CC), resulting in the presence of numerous aggregating particles, which was responsible for the firmer yogurt gel. Heating milk at pH 7.1 (mostly SWP‐CC) resulted in higher yogurt firmness than heating at pH 6.3 (mostly WPA‐CM). Practical applications Whey protein fortification and heating milk improve yogurt texture. However, different pH values of the milk before heating and whey protein fortification affect the properties of the yogurt. Variation of milk pH before heat treatment affects the degree of association between denatured whey proteins and casein micelles. As a result, inconsistencies occur in yogurt gel texture. This study showed that yogurt made from milk heated at pH 6.7 had increased firmness and water holding capacity compared with that when the milk was heated at pH 6.3 or 7.1. The pH of milk naturally changes slightly throughout the year, which in turn might affect yogurt firmness. Therefore, milk pH is an important parameter which needs to be adjusted to produce uniform quality yogurt to obtain a well‐accepted commercial product.

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Section: Practical Applicationsmentioning

confidence: 99%

Physical, rheological, and microstructural properties of whey protein enriched yogurt influenced by heating the milk at different pH values

Mahomud

Katsuno

Zhang

et al. 2017

J Food Process Preserv

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“…It is involved in the early stages of EW gelation, together with ovomucin and LYS [ 7 ]. OM is a heat-stable glycoprotein (28 kDa), with the heat stability arising from the high carbohydrate content (around 25–30% of OM) [ 8 ]. Ovomucin confers gel-like properties and is composed of two subunits with MWs of 5.5–8.3 × 10 3 , including alpha-ovomucin (MUC5B) and beta-ovomucin (MUC6).…”

Section: Gelation Of Ew Proteinsmentioning

confidence: 99%

Chicken Egg White Gels: Fabrication, Modification, and Applications in Foods and Oral Nutraceutical Delivery

Li,

Wang,

Chang

et al. 2024

Foods

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Chicken egg white (EW) proteins possess various useful techno-functionalities, including foaming, gelling or coagulating, and emulsifying. The gelling property is one of the most important functionalities of EW proteins, affecting their versatile applications in the food and pharmaceutical industries. However, it is challenging to develop high-quality gelled foods and innovative nutraceutical supplements using native EW and its proteins. This review describes the gelling properties of EW proteins. It discusses the development and action mechanism of the physical, chemical, and biological methods and exogenous substances used in the modification of EW gels. Two main applications of EW gels, i.e., gelling agents in foods and gel-type carriers for nutraceutical delivery, are systematically summarized and discussed. In addition, the research and technological gaps between modified EW gels and their applications are highlighted. By reviewing the new modification strategies and application trends of EW gels, this paper provides insights into the development of EW gel-derived products with new and functional features.

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“…Then, each gel sample was followed by chemical fixation using 0.5% osmium tetroxide in 0.1 M sodium phosphate buffer (pH 7), and then conductive staining was performed using 0.5% (w/v) filtered tannic acid. This double-fixation method followed by conductive treatment with 0.5% tannic acid was repeated according to methods by Yuno-Ohta et al [11] to prevent solubilization of gels and ensure fixation. Gels were then dehydrated in a series of ethanol solutions of increasing concentration (50, 70, 80, 90, 95 and 100% and again 100%, v/v).…”

Section: E Semmentioning

confidence: 99%

Characterization of the gelation and resulting network of a mixed-protein gel derived from sodium caseinate and ovalbumin in the presence of glucono-δ-lactone

Yuno‐Ohta

Shimonomura

Hoshi

et al. 2021

Colloids and Surfaces B: Biointerfaces

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We investigated mixed-protein gels made from sodium caseinate and ovalbumin at different ratios with use of the acidification agent glucono-δ-lactone. Dynamic viscoelastic measurements revealed that increasing the ovalbumin content decreased the mechanical properties of the gel but accelerated onset time of the phase transition. Ultrasound spectroscopy during gelation revealed that the relative velocity gradually decreased, whereas the ultrasonic attenuation increased during the whole acidification process until gelation was complete, although these changes were much smaller than those observed with heat-induced gelation. Confocal laser scanning microscopy along with scanning electron microscopy revealed that although uniform mixing of sodium caseinate and ovalbumin was observed, sodium caseinate is likely to mainly lead formation of the gel network, and the porosity of the resulting gel network depends on the ratio of these two components. The results demonstrate that confocal laser scanning microscopy is a useful tool for analyzing both the networks within mixed-protein gels and the contribution of each protein to the network and gelation.

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Role of ovomucoid in the gelation of a β-lactoglobulin-ovomucoid mixture

Cited by 10 publications

References 19 publications

Physical, rheological, and microstructural properties of whey protein enriched yogurt influenced by heating the milk at different pH values

Physical, rheological, and microstructural properties of whey protein enriched yogurt influenced by heating the milk at different pH values

Chicken Egg White Gels: Fabrication, Modification, and Applications in Foods and Oral Nutraceutical Delivery

Characterization of the gelation and resulting network of a mixed-protein gel derived from sodium caseinate and ovalbumin in the presence of glucono-δ-lactone

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