Demasking kinetics of peptide bond cleavage for whey protein isolate hydrolysed by Bacillus licheniformis protease

2016 ◽  
Vol 133 ◽  
pp. S426-S431 ◽  
Author(s):  
Mikhail M. Vorob’ev ◽  
Claire I. Butré ◽  
Stefano Sforza ◽  
Peter A. Wierenga ◽  
Harry Gruppen
Keyword(s):  
Whey Protein ◽  
Bacillus Licheniformis ◽  
Bond Cleavage ◽  
Peptide Bond ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Peptide Bond Cleavage ◽  
Kinetics Of

Kinetics of Phase Separation of Oat β-Glucan/Whey Protein Isolate Binary Mixtures

2009 ◽  
Vol 4 (3) ◽  
pp. 240-247 ◽  
Author(s):  
Vassilis Kontogiorgos ◽  
Susan M. Tosh ◽  
Peter J. Wood
Keyword(s):  
Phase Separation ◽  
Whey Protein ◽  
Binary Mixtures ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Kinetics Of

Drying and Denaturation Kinetics of Whey Protein Isolate (WPI) During Convective Air Drying Process

2013 ◽  
Vol 31 (13-14) ◽  
pp. 1532-1544 ◽  
Author(s):  
M. Amdadul Haque ◽  
Aditya Putranto ◽  
Peter Aldred ◽  
Jie Chen ◽  
Benu Adhikari
Keyword(s):  
Whey Protein ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Drying Process ◽  
Air Drying ◽  
Denaturation Kinetics ◽  
Kinetics Of

scholarly journals Kringles of substrate plasminogen provide a ‘catalytic switch' in plasminogen to plasmin turnover by Streptokinase

2020 ◽  
Vol 477 (5) ◽  
pp. 953-970
Author(s):  
Vandna Sharma ◽  
Shekhar Kumar ◽  
Girish Sahni
Keyword(s):  
Chemical Transformation ◽  
Active Site ◽  
Catalytic Domain ◽  
Bond Cleavage ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Peptide Bond ◽  
Peptide Bond Cleavage ◽  
Catalytic Processing ◽  
Kinetics Of

To understand the role of substrate plasminogen kringles in its differential catalytic processing by the streptokinase — human plasmin (SK-HPN) activator enzyme, Fluorescence Resonance Energy Transfer (FRET) model was generated between the donor labeled activator enzyme and the acceptor labeled substrate plasminogen (for both kringle rich Lys plasminogen — LysPG, and kringle less microplasminogen — µPG as substrates). Different steps of plasminogen to plasmin catalysis i.e. substrate plasminogen docking to scissile peptide bond cleavage, chemical transformation into proteolytically active product, and the decoupling of the nascent product from the SK-HPN activator enzyme were segregated selectively using (1) FRET signal as a proximity sensor to score the interactions between the substrate and the activator during the cycle of catalysis, (2) active site titration studies and (3) kinetics of peptide bond cleavage in the substrate. Remarkably, active site titration studies and the kinetics of peptide bond cleavage have shown that post docking chemical transformation of the substrate into the product is independent of kringles adjacent to the catalytic domain (CD). Stopped-flow based rapid mixing experiments for kringle rich and kringle less substrate plasminogen derivatives under substrate saturating and single cycle turnover conditions have shown that the presence of kringle domains adjacent to the CD in the macromolecular substrate contributes by selectively speeding up the final step, namely the product release/expulsion step of catalysis by the streptokinase-plasmin(ogen) activator enzyme.

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