Enhanced Heat-induced Gelation of<i>β</i>-Lactoglobulin by<i>α</i>-Lactalbumin

Matsudomi, Naotoshi; Oshita, Toru; Sasaki, Eiji; Kobayashi, Kunihiko

doi:10.1271/bbb.56.1697

Cited by 65 publications

(51 citation statements)

References 5 publications

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“…Meanwhile, the elution time of the aggregate peak gradually decreased, indicating growth of aggregate MW with heat time. Previous work (Ju et al, 1997;Matsudomi et al, 1992), however, did not show any change in the elution time of the aggregate peak. This might be due to the small elution particle size [(5-150) × 10 3 or (10-500) × 10 3 MW] of previous SE-HPLC columns, whereas this research used a column capable of detecting a much higher range of particle size [(20-10000) × 10 3 MW].…”

Section: Effect Of Protein Concentration Gel Hardnesscontrasting

confidence: 53%

Effects of Preheating on Properties of Aggregates and of Cold-Set Gels of Whey Protein Isolate

Kilara

1998

J. Agric. Food Chem.

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Various concentrations (1-9%) of whey protein (WP) isolate solutions were heat-denatured at 80°C for 30 min. Size exclusion HPLC and dynamic light scattering revealed formation of soluble aggregates in 3-9% denatured WP solution. Size and content of the aggregates increased with increases in preheated WP concentration. The 4-9% denatured WP solutions were diluted to 3% WP with distilled water. Upon addition of CaCl 2 (20 mM) or glucono-δ-lactone (0.6%, w/v), all 3% denatured WP solutions formed gels at 37°C. Hardness of the gels (3% WP) remarkably increased with WP concentration during preheating or with the aggregate size and content. The HPLC elution profiles showed that prolonging the heating (80°C) time (2-30 min) for 8% WP solution also gradually increases aggregate size and concentration, which then led to increases in hardness of cold-set gels. The results may guide companies in how to manipulate aggregate size and content during developing WP products with capacity for cold gelation.

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Section: Effect Of Protein Concentration Gel Hardnesscontrasting

confidence: 53%

Effects of Preheating on Properties of Aggregates and of Cold-Set Gels of Whey Protein Isolate

Kilara

1998

J. Agric. Food Chem.

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“…Therefore, the presence of b-lg together with a-la in the system, combined with high temperature, allows the incorporation of a-la in the aggregates. Indeed, the presence of b-lg, containing a free thiol group, may lead to the formation of intermolecular disulphide bonds and to co-aggregation with a-la (Calvo et al, 1993;Elfagm & Wheelock, 1978;Matsudomi, Oshita, Sasaki, & Kobayashi, 1992). At 60 1C, peptides may interact with b-lg linked with a-la via disulphide bonds.…”

Section: Protein-peptide Interactionsmentioning

confidence: 99%

Peptide–peptide and protein–peptide interactions in mixtures of whey protein isolate and whey protein isolate hydrolysates

Creusot

Gruppen

Koningsveld

et al. 2006

International Dairy Journal

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“…After WP or beta-lactoglobulin (␤-Lg) solution was heat-denatured, soluble aggregates were detected with size-exclusion (SE) HPLC (Ju et al, 1997;Matsudomi et al, 1992), SDS-PAGE (Laligant et al, 1991) and electron microscopy . The percentage of native WP converted to soluble aggregates depended on the amount of heat.…”

Section: Introductionmentioning

confidence: 99%

Textural Properties of Cold‐set Gels Induced from Heat‐denatured Whey Protein Isolates

Kilara

1998

Journal of Food Science

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A 9% whey protein (WP) isolate solution at pH 7.0 was heat‐denatured at 80°C for 30 min. Size‐exclusion HPLC showed that native WP formed soluble aggregates after heat‐treatment. Additions of CaCl2 (10–40 mM), NaCl (50–400 mM) or glucono‐delta‐lactone (GDL, 0.4–2.0%, w/v) or hydrolysis by a protease from Bacillus licheniformis caused gelation of the denatured solution at 45°C. Textural parameters, hardness, adhesiveness, and cohesiveness of the gels so formed changed markedly with concentration of added salts or pH by added GDL. Maximum gel hardness occurred at 200 mM NaCl or pH 4.7. Increasing CaCl2 concentration continuously increased gel hardness. Generally, GDL‐induced gels were harder than salt‐induced gels, and much harder than the protease‐induced gel.

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Enhanced Heat-induced Gelation ofβ-Lactoglobulin byα-Lactalbumin

Cited by 65 publications

References 5 publications

Effects of Preheating on Properties of Aggregates and of Cold-Set Gels of Whey Protein Isolate

Effects of Preheating on Properties of Aggregates and of Cold-Set Gels of Whey Protein Isolate

Peptide–peptide and protein–peptide interactions in mixtures of whey protein isolate and whey protein isolate hydrolysates

Textural Properties of Cold‐set Gels Induced from Heat‐denatured Whey Protein Isolates

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