Comparison of the gel-forming ability and gel properties of α-lactalbumin, lysozyme and myoglobin in the presence of β-lactoglobulin under high pressure

2013 ◽  
Vol 33 (2) ◽  
pp. 415-424 ◽  
Author(s):  
Jin-Song He ◽  
Tai-Hua Mu ◽  
Xishan Guo ◽  
Songming Zhu ◽  
Norihiro Azuma ◽  
...  
Keyword(s):  
High Pressure ◽  
Gel Properties ◽  
Gel Forming Ability ◽  
Β Lactoglobulin

Effects of high pressure homogenization on the solubility, foaming, and gel properties of soy 11S globulin

2021 ◽  
pp. 107261
Author(s):  
Zhuang-Li Kang ◽  
Rong Bai ◽  
Fei Lu ◽  
Tao Zhang ◽  
Zai-Shang Gao ◽  
...  
Keyword(s):  
High Pressure ◽  
High Pressure Homogenization ◽  
Gel Properties ◽  
11S Globulin

Effect of high pressure homogenization on the structure and the interfacial and emulsifying properties of β-lactoglobulin

2018 ◽  
Vol 537 (1-2) ◽  
pp. 111-121 ◽  
Author(s):  
Ali Ali ◽  
Isabelle Le Potier ◽  
Nicolas Huang ◽  
Véronique Rosilio ◽  
Monique Cheron ◽  
...  
Keyword(s):  
High Pressure ◽  
High Pressure Homogenization ◽  
Emulsifying Properties ◽  
Β Lactoglobulin

β-Lactoglobulin Molten Globule Induced by High Pressure

2001 ◽  
Vol 49 (7) ◽  
pp. 3236-3243 ◽  
Author(s):  
Jian Yang ◽  
A. Keith Dunker ◽  
Joseph R. Powers ◽  
Stephanie Clark ◽  
Barry G. Swanson
Keyword(s):  
High Pressure ◽  
Molten Globule ◽  
Β Lactoglobulin

Microbial transglutaminase crosslinks β-casein and β-lactoglobulin to heterologous oligomers under high pressure

2003 ◽  
Vol 216 (1) ◽  
pp. 15-17 ◽  
Author(s):  
Sabine Lauber ◽  
Ingolf Krause ◽  
Henning Klostermeyer ◽  
Thomas Henle
Keyword(s):  
High Pressure ◽  
Microbial Transglutaminase ◽  
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.

Effects of heat treatment and high pressure on the subsequent lactosylation of β-lactoglobulin

2006 ◽  
Vol 99 (4) ◽  
pp. 651-655 ◽  
Author(s):  
M RADAMENDOZA ◽  
M VILLAMIEL ◽  
E MOLINA ◽  
A OLANO
Keyword(s):  
Heat Treatment ◽  
High Pressure ◽  
Β Lactoglobulin
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