Epicatechin Adducting with 5-Hydroxymethylfurfural as an Inhibitory Mechanism against Acrylamide Formation in Maillard Reactions

2018 ◽  
Vol 66 (47) ◽  
pp. 12536-12543 ◽  
Author(s):  
Yajing Qi ◽  
Hui Zhang ◽  
Hao Zhang ◽  
Gangcheng Wu ◽  
Li Wang ◽  
...  
2009 ◽  
Vol 22 (8) ◽  
pp. 1483-1489 ◽  
Author(s):  
Ka-Wing Cheng ◽  
Xiaohui Zeng ◽  
Yun Sang Tang ◽  
Jia-Jun Wu ◽  
Zhiwei Liu ◽  
...  

2006 ◽  
Vol 71 (1) ◽  
pp. C28-C33 ◽  
Author(s):  
Pernille Baardseth ◽  
Hans Blom ◽  
Grete Skrede ◽  
Liv T. Mydland ◽  
Anders Skrede ◽  
...  

1975 ◽  
Vol 33 (03) ◽  
pp. 573-585 ◽  
Author(s):  
Masahiro Iwamoto

SummaryInteractions between tranexamic acid and protein were studied in respect of the antifibrinolytic actions of tranexamic acid. Tranexamic acid did neither show any interaction with fibrinogen or fibrin, nor was incorporated into cross-linked fibrin structure by the action of factor XIII. On the other hand, tranexamic acid bound to human plasmin with a dissociation constant of 3.5 × 10−5 M, which was very close to the inhibition constant (3.6 × 10−5 M) for this compound in inhibiting plasmin-induced fibrinolysis. The binding site of tranexamic acid on plasmin was not the catalytic site of plasmin, because TLCK-blocked plasmin also showed a similar affinity to tranexamic acid (the dissociation constant, 2.9–4.8 × 10−5 M).In the binding studies with the highly purified plasminogen and TLCK-plasmin preparations which were obtained by affinity chromatography on lysine-substituted Sepharose, the molar binding ratio was shown to be 1.5–1.6 moles tranexamic acid per one mole protein.On the basis of these and other findings, a model for the inhibitory mechanism of tranexamic acid is presented.


2019 ◽  
Vol 25 (3) ◽  
Author(s):  
Mariano Larzábal ◽  
Hector A. Baldoni ◽  
Fernando D. Suvire ◽  
Lucrecia M. Curto ◽  
Gabriela E. Gomez ◽  
...  

Antioxidants ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 993
Author(s):  
Su Lee Kuek ◽  
Azmil Haizam Ahmad Tarmizi ◽  
Raznim Arni Abd Razak ◽  
Selamat Jinap ◽  
Maimunah Sanny

This study aims to evaluate the influence of Vitamin A and E homologues toward acrylamide in equimolar asparagine-glucose model system. Vitamin A homologue as β-carotene (BC) and five Vitamin E homologues, i.e., α-tocopherol (AT), δ-tocopherol (DT), α-tocotrienol (ATT), γ-tocotrienol (GTT), and δ-tocotrienol (DTT), were tested at different concentrations (1 and 10 µmol) and subjected to heating at 160 °C for 20 min before acrylamide quantification. At lower concentrations (1 µmol; 431, 403, 411 ppm, respectively), AT, DT, and GTT significantly increase acrylamide. Except for DT, enhancing concentration to 10 µmol (5370, 4310, 4250, 3970, and 4110 ppm, respectively) caused significant acrylamide formation. From linear regression model, acrylamide concentration demonstrated significant depreciation over concentration increase in AT (Beta = −83.0, R2 = 0.652, p ≤ 0.05) and DT (Beta = −71.6, R2 = 0.930, p ≤ 0.05). This study indicates that different Vitamin A and E homologue concentrations could determine their functionality either as antioxidants or pro-oxidants.


2021 ◽  
pp. 129305
Author(s):  
Matthew Knight ◽  
Simon McWilliam ◽  
Sarah Peck ◽  
Georgios Koutsidis ◽  
Gemma Chope ◽  
...  

2021 ◽  
Vol 350 ◽  
pp. 129060
Author(s):  
Amira Haddarah ◽  
Elissa Naim ◽  
Iman Dankar ◽  
Francesc Sepulcre ◽  
Montserrat Pujolà ◽  
...  

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