scholarly journals Protein cross-linking and the Maillard reaction decrease the solubility of milk protein concentrates

2018 ◽  
Vol 6 (5) ◽  
pp. 1196-1203 ◽  
Author(s):  
Fengjiao Fan ◽  
Meng Liu ◽  
Pujie Shi ◽  
Xianbing Xu ◽  
Weihong Lu ◽  
...  
Nephron ◽  
1995 ◽  
Vol 69 (4) ◽  
pp. 438-443 ◽  
Author(s):  
Toshimitsu Niwa ◽  
Naohito Takeda ◽  
Takashi Miyazaki ◽  
Hideo Yoshizumi ◽  
Akira Tatematsu ◽  
...  

2013 ◽  
Vol 31 (2) ◽  
pp. 83-91 ◽  
Author(s):  
Thao T. Le ◽  
John W. Holland ◽  
Bhesh Bhandari ◽  
Paul F. Alewood ◽  
Hilton C. Deeth

1996 ◽  
Vol 271 (32) ◽  
pp. 19338-19345 ◽  
Author(s):  
Ramanakoppa H. Nagaraj ◽  
Irina N. Shipanova ◽  
Frederick M. Faust

2015 ◽  
Vol 96 (10) ◽  
pp. 3500-3507 ◽  
Author(s):  
Jacek Domagała ◽  
Dorota Najgebauer-Lejko ◽  
Ilona Wieteska-Śliwa ◽  
Marek Sady ◽  
Monika Wszołek ◽  
...  

2011 ◽  
Vol 59 (23) ◽  
pp. 12473-12479 ◽  
Author(s):  
Thao T. Le ◽  
Bhesh Bhandari ◽  
John W. Holland ◽  
Hilton C. Deeth

2016 ◽  
Vol 2016 ◽  
pp. 1-6 ◽  
Author(s):  
S. Montha ◽  
P. Suwandittakul ◽  
A. Poonsrisawat ◽  
P. Oungeun ◽  
C. Kongkaew

Maillard reaction in Natural Rubber (NR) latex was investigated by treating fresh NR latex with glutaraldehyde (C5H8O2) in amounts of 0, 50, 100, and 200 mmol/kg of latex. Protein cross-linking in fresh NR latex and solid NR was confirmed by using sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE) and attenuated total reflection infrared (ATR-IR) spectroscopy, respectively. It was found that degree of protein cross-linking in NR increased with increasing C5H8O2concentration. Physical properties of untreated and treated NR substances in terms of gel content, initial Wallace plasticity (P0), plasticity retention index (PRI), Mooney viscosity, and tensile strength were carefully explored. Results clearly showed that the Maillard cross-linking of proteins had remarkable effect on bulk NR properties, that is, solvent resistance, hardness, resistance to oxidation, rheological behavior, and resistance to stretching out.


1994 ◽  
Vol 71 (04) ◽  
pp. 402-415 ◽  
Author(s):  
Daniel Aeschlimann ◽  
Mats Paulsson

1997 ◽  
Vol 77 (05) ◽  
pp. 0959-0963 ◽  
Author(s):  
Lisa Seale ◽  
Sarah Finney ◽  
Roy T Sawyer ◽  
Robert B Wallis

SummaryTridegin is a potent inhibitor of factor Xllla from the leech, Haementeria ghilianii, which inhibits protein cross-linking. It modifies plasmin-mediated fibrin degradation as shown by the absence of D-dimer and approximately halves the time for fibrinolysis. Plasma clots formed in the presence of Tridegin lyse more rapidly when either streptokinase, tissue plasminogen activator or hementin is added 2 h after clot formation. The effect of Tridegin is markedly increased if clots are formed from platelet-rich plasma. Platelet-rich plasma clots are lysed much more slowly by the fibrinolytic enzymes used and if Tridegin is present, the rate of lysis returns almost to that of platelet- free clots. These studies indicate the important role of platelets in conferring resistance to commonly used fibrinolytic enzymes and suggest that protein cross-linking is an important step in this effect. Moreover they indicate that Tridegin, a small polypeptide, may have potential as an adjunct to thrombolytic therapy.


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