Journal Articles

Permanent URI for this collectionhttps://mro.massey.ac.nz/handle/10179/7915

Browse

Subject: search.filters.subject.β-lactoglobulin

Search Results

Now showing 1 - 2 of 2
  • Thumbnail Image
    Item
    Heat-induced interactions of hemp protein particles formed by microfluidisation with β-lactoglobulin
    (Elsevier Ltd, 2024-07-01) Ma S; Acevedo-Fani A; Ye A; Singh H
    This study explored the effect of microfluidization on the dispersibility of hempseed protein (HP) and the interactions of microfluidised HP particles with β-lactoglobulin (β-lg) after heat treatment. Microfluidization increased the dispersible protein fraction from 10% (non-microfluidised) to a maximum of 58% (200 MPa, 6 passes) in HP dispersions. Dispersible HP particles were within the micro-sized range (d4,3 ≤ 2 μm) after microfluidization. Heat treatment (95 °C, 10–60 min) of HP particles with β-lactoglobulin (β-lg) induced protein association by sulphydryl-disulphide exchange reactions; β-lg association with HP particles initiated within the first 20 min. Additionally, the particle size (d4,3) values of co-heated HP particles with β-lg were significantly smaller than those found in HP particle dispersions heated alone, results that were in line with microscopy analysis. This suggests that β-lg could have restricted HP particle aggregation. In conclusion, combining microfluidization and heat treatment could offer a venue to modify the physical properties of plant/milk protein mixtures.
  • Thumbnail Image
    Item
    In vitro gastric digestion of heat-induced aggregates of β-lg
    (Elsevier Inc., 2012) Loveday, SM; Singh, Harjinder; Ye, Aiqian; Peram, Malleswara R.
    An in vitro gastric digestion of heat-induced aggregates of β-lactoglobulin (β-lg) in simulated gastric fluid was investigated using sodium dodecyl sulfate-PAGE under nonreducing and reducing conditions, native-PAGE, 2-dimensional electrophoresis, and size exclusion chromatography. Heating at 90ºC significantly increased the digestibility of β-lg, with a high initial digestion rate followed by a relatively constant rate of digestion at a high enzyme:substrate (E:S) ratio of 3:1. At a low E:S ratio (1:6), the rate of digestion of β-lg was slower, and intermediate and low molecular weight species could be seen. The high molecular weight nonnative aggregates (pentamers, tetramers, trimers, etc.) were digested relatively rapidly, whereas some of the nonnative dimers were resistant to digestion and others were digested rapidly. The intermediate molecular weight species (21 to 23 kDa) were digested slowly. These results indicated that the digestibility of nonnative β-lg aggregates varied significantly depending on the E:S ratio and the types of aggregate. Further investigation is necessary to identify and characterize slowly digested dimers and intermediate molecular weight species.