AI Article Synopsis

  • Two types of nuclei—homogeneous and secondary—play a role in fibril formation in whey protein concentrate (WPC), affecting how quickly and effectively amyloid fibrils form.
  • Thioflavin T fluorescence analysis showed that both types of nuclei speed up WPC fibrillation, with homogeneous nuclei resulting in more fibrils compared to secondary nuclei, which accelerated the aggregation process.
  • Although secondary nuclei led to faster aggregation rates initially and shorter gelation times for WPC, the final gel from homogeneous nuclei had a denser structure, providing better water retention.

Article Abstract

Two types of special structures, homogeneous and secondary nuclei, form during fibril formation. The structural and functional properties of amyloid fibrils in whey protein concentrate (WPC) with different ratios of added homogeneous nuclei to secondary nuclei were investigated. Thioflavin T fluorescence analysis and kinetic equations indicated that two types of nuclei could accelerate WPC fibrillation compared with WPC self-assembling into amyloid fibrils, thereby reducing the lag time and increasing the number of fibrils. However, there were considerable differences in the nucleation-inducing capability of WPC fibrillation between homogeneous and secondary nuclei. The number of fibrils formed by adding homogeneous nuclei was higher than that obtained with secondary nuclei, the increase in the Th T fluorescence intensity induced by homogeneous nuclei was 1.83-fold much than secondary nuclei. Meanwhile, secondary nuclei yielded a 2.71-fold faster aggregation rate of WPC than homogeneous nuclei, particularly during the first hour of thermal treatment (protein mass ratio of nuclei to WPC 1:1). The gelation time of WPC after secondary nuclei addition was shorter, from 10 h (WPC (2.0/6.5)) to 4 h (WPC + HN) to 2 h (WPC + SN); however, the gel microstructure of WPC after the addition of homogeneous nuclei was denser, yielding a preferred water holding capacity.

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http://dx.doi.org/10.1016/j.foodres.2018.05.073DOI Listing

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