Gelation of single heated vs. double heated whey protein isolate

Glibowski, Paweł; Mleko, S.; Wesołowska–Trojanowska, Marta

doi:10.1016/j.idairyj.2005.10.024

Cited by 18 publications

(11 citation statements)

References 17 publications

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“…Heating at 85 o C resulted in a sharp decrease in "nativelike" lg and lac bands, and a concomitant appearance of both aggregate smears and high molecular mass protein aggregates bands (Fig. 2); this indicates extensive protein aggregation, and consequently aggregation of lg and lac (Glibowski et al, 2006;Schokker et al, 2000). Heating lac is responsible for producing non-native monomeric groups of lac dimers and larger aggregates.…”

Section: Whey Protein Denaturationmentioning

confidence: 98%

“…250 kDa. Molecules with molecular mass above 1000 kDa remained at the top of the wells, and only the molecules up to 250 kDa could enter the resolving gel (Glibowski et al, 2006). The appearance of the large aggregate smear region changed with heating time for both MEF and COV treatments.…”

Section: Whey Protein Denaturationmentioning

confidence: 99%

“…The whey protein bands on the resultant native gels were identified by con-current electrophoresis of lg and lac samples. Some other protein bands (such as BSA) were identified by comparing the results with reported patterns (Glibowski, Mleko, & Wesolowska-Trojanowska, 2006;Havea, Singh, Creamer, & Campanella, 1998). The results of Native-PAGE were quantified with gel densitometry, in attempts to measure the loss of the major native whey proteins.…”

Section: Whey Protein Denaturationmentioning

confidence: 99%

“…(Glibowski et al, 2006;Schokker et al, 2000;Wehbi et al, 2005). In fact, protein large aggregates were at the top of the resolving gel e characterized by a molecular mass of ca.…”

Section: Whey Protein Denaturationmentioning

confidence: 99%

“…2, lanes 9 and 10). This may be a clue to an increase in the overall size (and molecular weight) of the heat-induced protein aggregates and complexes, which probably become trapped on the top of the stacking wells (Cho et al, 2003;Glibowski et al, 2006). Both results from RP-HPLC and Native-PAGE indicate that MEF can preserve higher contents of native proteins during early stages of heating than COV (see Tables 1 and 2), which is in agreement with previous results regarding denaturation kinetics of whey proteins (Pereira et al, 2011).…”

Section: Whey Protein Denaturationmentioning

confidence: 99%

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Influence of moderate electric fields on gelation of whey protein isolate

et al. 2015

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Proteins are one of the food constituents most affected by heating, and some of the changes involve their unfolding, denaturation and gelation. Ohmic heating has often been claimed to improve the quality of foodstuffs due to its uniform heating and (putative) presence of a moderate electric field (MEF). However, this is still subject to discussion, so it is important to determine the effect of ohmic heating and of its MEF upon food constituents. Hence, the aim of this work was to evaluate the effects of MEF on denaturation, aggregation and viscoelastic properties of whey protein isolate (WPI), and compare them with those obtained via conventional heating under identical treatment conditions (up to 30 min at 85 o C). Results have shown that MEF interferes with whey protein unfolding and aggregation pathways at relatively high temperatures. MEF treatments have resulted in WPI solutions possessing more 8 and 10% of native Lactoglobulin and Lactalbumin, respectively, after 30 s of heating at 85 o C, when compared with a conventional heating method. Protein aggregates from MEF-treated WPI solutions presented a maximum increase in size of 78 nm, whereas conventional heating produced an increase of 86 nm. Unlike in conventional heating, aggregation of whey proteins during MEF was not sufficiently strong to form a true elastic gel network, since decreases in both storage and loss modulus were observed following MEF treatment. Our results suggest that MEF may provide a novel method for production of a whey protein matrix with distinctive gel-forming properties.2

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Section: Whey Protein Denaturationmentioning

confidence: 98%

Section: Whey Protein Denaturationmentioning

confidence: 99%

Section: Whey Protein Denaturationmentioning

confidence: 99%

“…(Glibowski et al, 2006;Schokker et al, 2000;Wehbi et al, 2005). In fact, protein large aggregates were at the top of the resolving gel e characterized by a molecular mass of ca.…”

Section: Whey Protein Denaturationmentioning

confidence: 99%