Influence of milk protein cross-linking by transglutaminase on the rennet coagulation time and the gel properties

2015 ◽  
Vol 96 (10) ◽  
pp. 3500-3507 ◽  
Author(s):  
Jacek Domagała ◽  
Dorota Najgebauer-Lejko ◽  
Ilona Wieteska-Śliwa ◽  
Marek Sady ◽  
Monika Wszołek ◽  
...  
Keyword(s):  
Milk Protein ◽  
Cross Linking ◽  
Gel Properties ◽  
Coagulation Time ◽  
Rennet Coagulation ◽  
Protein Cross Linking

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 ◽  
...  
Keyword(s):  
Maillard Reaction ◽  
Milk Protein ◽  
Cross Linking ◽  
Protein Concentrates ◽  
Protein Cross Linking

Studies on the heat stability of milk protein: II. Effect of exposing milk to light

1975 ◽  
Vol 42 (1) ◽  
pp. 57-71 ◽  
Author(s):  
A. W. M. Sweetsur ◽  
J. C. D. White
Keyword(s):  
Milk Protein ◽  
Necessary Conditions ◽  
Type A ◽  
Heat Stability ◽  
Coagulation Time ◽  
Stability Curve ◽  
Photo Oxidation ◽  
Rennet Coagulation

SummaryIt was found that the increase in heat stability (coagulation time) that occurs when some milks are stored in light was not caused by changes in pH. These labile milks invariably gave a type A heat-stability curve, had a pH in the range corresponding to the coagulation-time minimum of the curve, and showed the expected abnormal 2-stage type of coagulation. The increase in coagulation time following exposure to light resulted from a delay in the occurrence of the first coagulation, the second coagulation time remaining unaltered. The presence of riboflavin in milk and of O2 in the headspace atmosphere during storage were necessary conditions for milk to be labile. Since light, headspace O2 and riboflavin had similar influences on rennet coagulation time it is suggested that in both instances the causative reaction, as proposed by others to account for the increase in rennet coagulation time of H2O2-treated milk, is stabilization of the heat- and rennin-sensitive methionine-phenylalaninebond in κ-casein by photo-oxidation of the methionine to methionine sulphoxide.

Transglutaminases: Protein Cross-Linking Enzymes in Tissues and Body Fluids

1994 ◽  
Vol 71 (04) ◽  
pp. 402-415 ◽  
Author(s):  
Daniel Aeschlimann ◽  
Mats Paulsson
Keyword(s):  
Body Fluids ◽  
Cross Linking ◽  
Protein Cross Linking

Tridegin, a Novel Peptidic Inhibitor of Factor XIIIa from the Leech, Haementeria ghilianii, Enhances Fibrinolysis In Vitro

1997 ◽  
Vol 77 (05) ◽  
pp. 0959-0963 ◽  
Author(s):  
Lisa Seale ◽  
Sarah Finney ◽  
Roy T Sawyer ◽  
Robert B Wallis
Keyword(s):  
Potent Inhibitor ◽  
Platelet Rich Plasma ◽  
Factor Xiiia ◽  
Cross Linking ◽  
Fibrinolytic Enzymes ◽  
Small Polypeptide ◽  
Tissue Plasminogen ◽  
Protein Cross Linking

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.

scholarly journals Glycan-protein cross-linking mass spectrometry reveals sialic acid-mediated protein networks on cell surfaces

2021 ◽  
Author(s):  
Yixuan Xie ◽  
Siyu Chen ◽  
Qiongyu Li ◽  
Ying Sheng ◽  
Michael R Alvarez ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Sialic Acid ◽  
Membrane Proteins ◽  
Cell Membranes ◽  
Sialic Acids ◽  
Cross Linking ◽  
Protein Networks ◽  
Cell Surfaces ◽  
Protein Cross Linking

A cross-linking method is developed to elucidate the glycan-mediated interactions between membrane proteins through sialic acids. The method provides previously unknown extensive glycomic interactions on cell membranes. The vast majority...

Effect of protein cross-linking aldehydes on nerve activity

1981 ◽  
Vol 89 (2) ◽  
pp. 159-165 ◽  
Author(s):  
D. G. Margineanu ◽  
Eva Katona ◽  
Junona Popa
Keyword(s):  
Cross Linking ◽  
Nerve Activity ◽  
Protein Cross Linking

A Novel Protein Cross-Linking Reaction in Stressed Neutral Protamine Hagedorn Formulations of Insulin

1999 ◽  
Vol 88 (3) ◽  
pp. 331-336 ◽  
Author(s):  
Ronald C. Beavis ◽  
Michael D. Kneirman ◽  
David Sharknas ◽  
Mark A. Heady ◽  
Bruce H. Frank ◽  
...  
Keyword(s):  
Cross Linking ◽  
Neutral Protamine Hagedorn ◽  
Novel Protein ◽  
Protein Cross Linking

scholarly journals Model of the Mediator middle module based on protein cross-linking

2013 ◽  
Vol 41 (20) ◽  
pp. 9266-9273 ◽  
Author(s):  
Laurent Larivière ◽  
Clemens Plaschka ◽  
Martin Seizl ◽  
Evgeniy V. Petrotchenko ◽  
Larissa Wenzeck ◽  
...  
Keyword(s):  
Cross Linking ◽  
Protein Cross Linking

scholarly journals Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II

2014 ◽  
Vol 111 (45) ◽  
pp. 16178-16183 ◽  
Author(s):  
Manjula P. Mummadisetti ◽  
Laurie K. Frankel ◽  
Henry D. Bellamy ◽  
Larry Sallans ◽  
Jost S. Goettert ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Cross Linking ◽  
Higher Plant ◽  
Protein Cross Linking
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