http://link.springer.com/content/pdf/10.1007/BF03223342.pdf

Whey proteins: Super ingredients for functional foods?

Pressure denaturation of proteins

This paper focuses on the resistance of packaging materials to piercing during high pressure thawing and delamination due to residual air. Six different packaging materials were tested, the influence of temperature, different depressurization rates and freezing were studied. Among the packaging materials tested, only one, BB4L®, containing EVA copolymer, was found to be resistant to piercing.

Behaviour of packaging materials during high pressure thawing.: Note

Cavities in the Hydrophobic Core Govern Pressure Unfolding of Proteins

Enzymatic firming of high-pressure frozen strawberry halves by means of exogenous pectinmethylesterase.

High pressure low temperature treatments (HPLT) combine the effects of high pressures with low temperature and freezing effects. The aim of this study is to investigate the impact of HPLT on major milk protein fractions and to identify the potential of this technology for modification of these frequently used proteins. Pressure assisted freezing (PAF, -35 °C) and pressure shift freezing (PSF, -15 °C) were applied from 100-600 MPa to identify the most promising process parameters for protein modification. High pressure treatments at room temperature (HP) were performed as reference values for the impact of pressure. Milk protein dispersions (whey protein isolate WPI; micellar casein MC; 80:20 MC:WPI and 20:80 MC:WPI weight based mixtures) were treated at pH 7.0 and pH 5.8 at a concentration of 2 % (w/w). Colloidal stability, structural changes and modification in techno-functional properties were used as an indicator for protein modification on different molecular levels. HPLT induced specific fibrous flocks in samples with 80 and 100 % MC. These flocks showed a shear thickening effect and represent a promising HPLT specific functional property. Especially PSF treatments induced new secondary structure motifs (β-sheet) from random coils in WPI containing samples. Those structuring effects could not be observed for HP treatments. These changes can be influenced by altering the sample composition or the treatment pH. Furthermore, slight increases in foam stability were detected especially for pure WPI solutions after HPLT as well as after HP treatments, while emulsification properties remained almost unchanged. The results of the present study indicate a specific modification of milk proteins via HPLT treatments which is promising for new food applications.

/pdf/impact-of-hplt-treatments-on-micellar-caseins-and-whey-34cup3y3kl.pdf

Impact of HPLT treatments on micellar caseins and whey proteins

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Impact of HPLT treatments on micellar caseins and whey proteins