Interfacial film formation and film stability of high hydrostatic pressure-treated β-lactoglobulin

2021 ◽  
pp. 106746
Author(s):  
Helena Kieserling ◽  
Ingalisa M. Alsmeier ◽  
Anja Steffen-Heins ◽  
Julia K. Keppler ◽  
Robert Sevenich ◽  
...  
Keyword(s):  
Hydrostatic Pressure ◽  
High Hydrostatic Pressure ◽  
Film Formation ◽  
Film Stability ◽  
Interfacial Film ◽  
Β Lactoglobulin

Conformational state and charge determine the interfacial film formation and film stability of β-lactoglobulin

2021 ◽  
Vol 114 ◽  
pp. 106561
Author(s):  
Helena Kieserling ◽  
Annika Pankow ◽  
Julia K. Keppler ◽  
Anja M. Wagemans ◽  
Stephan Drusch
Keyword(s):  
Film Formation ◽  
Conformational State ◽  
Film Stability ◽  
Interfacial Film ◽  
Β Lactoglobulin

The impact of high hydrostatic pressure on structure and dynamics of β-lactoglobulin

2013 ◽  
Vol 1830 (10) ◽  
pp. 4974-4980 ◽  
Author(s):  
Daniela Russo ◽  
Maria Grazia Ortore ◽  
Francesco Spinozzi ◽  
Paolo Mariani ◽  
Camille Loupiac ◽  
...  
Keyword(s):  
Hydrostatic Pressure ◽  
High Hydrostatic Pressure ◽  
Structure And Dynamics ◽  
The Impact ◽  
Β Lactoglobulin

Effect of high hydrostatic pressure on the enzymic hydrolysis of β-lactoglobulin B by trypsin, thermolysin and pepsin

1996 ◽  
Vol 63 (1) ◽  
pp. 111-118 ◽  
Author(s):  
Henrik Stapelfeldt ◽  
Per Hjort Petersen ◽  
Kristian Rotvig Kristiansen ◽  
Karsten Bruun Qvist ◽  
Leif H. Skibsted
Keyword(s):  
High Pressure ◽  
Hydrostatic Pressure ◽  
High Hydrostatic Pressure ◽  
Pressure Effect ◽  
Ambient Pressure ◽  
Apparent Volume ◽  
Enzymic Hydrolysis ◽  
Ambient Conditions ◽  
Β Lactoglobulin ◽  
Hydrolysis Of

SummaryHydrolysis of β-lactoglobulin B (β-lg B) by pepsin, a process slow at ambient conditions, is facilitated at a moderately high hydrostatic pressure such as 300 MPa, corresponding to an apparent volume of activation ΔV# = −63 ml mol−1 at pH 2·5, 30 °C and Γ/2=0·16. Digestion of β-lg by trypsin and thermolysin is likewise enhanced by pressure, and the pressure effect has been traced to pressure denaturation of β-lg B, which by high-pressure fluorescence spectroscopy has been shown to have a large negative volume of reaction, ΔV° = −98 ml mol−1, at pH 6·7, 30 °C and Γ/2 = 0·16. Pressure denaturation is only slowly reversed following release of pressure and the enhanced digestibility is maintained at ambient pressure for several hours.

scholarly journals Production of highly purified fractions of α-lactalbumin and β-lactoglobulin from cheese whey using high hydrostatic pressure

2020 ◽  
Vol 103 (9) ◽  
pp. 7939-7950 ◽  
Author(s):  
Alice Marciniak ◽  
Shyam Suwal ◽  
Serine Touhami ◽  
Julien Chamberland ◽  
Yves Pouliot ◽  
...  
Keyword(s):  
Hydrostatic Pressure ◽  
High Hydrostatic Pressure ◽  
Cheese Whey ◽  
Β Lactoglobulin

Hydrolysis of β-lactoglobulin by thermolysin and pepsin under high hydrostatic pressure

Biopolymers ◽  
1995 ◽  
Vol 35 (5) ◽  
pp. 475-483 ◽  
Author(s):  
Eric Dufour ◽  
Guy Hervé ◽  
Tomasz Haertle
Keyword(s):  
Hydrostatic Pressure ◽  
High Hydrostatic Pressure ◽  
Β Lactoglobulin ◽  
Hydrolysis Of

scholarly journals In vivo methods for testing allergenicity show that high hydrostatic pressure hydrolysates of β-lactoglobulin are immunologically inert

2012 ◽  
Vol 95 (2) ◽  
pp. 541-548 ◽  
Author(s):  
I. López-Expósito ◽  
R. Chicón ◽  
J. Belloque ◽  
R. López-Fandiño ◽  
M.C. Berin
Keyword(s):  
Hydrostatic Pressure ◽  
High Hydrostatic Pressure ◽  
Β Lactoglobulin
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