Impact of UV-C pretreatment on β-lactoglobulin hydrolysis by trypsin: Production and bioavailability of bioactive peptides

Cavalcante, Keila  N.; Feitor, Jéssica Freire; Morais, Sinara T.B.; Nassu, R. T.; Ahrné, Lı́lia; Cardoso, Daniel

doi:10.1016/j.idairyj.2023.105650

Cited by 1 publication

(1 citation statement)

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“…However, trypsin, a member of the serine protease family similar to plasmin, exhibited a different binding mode with β-Lg. Cavalcante et al 34 reported that thermal treatment of β-Lg did not promote its interaction with trypsin. Based on the increased inhibition of plasmin activity by denatured β-Lg, it can be inferred that denatured β-Lg might enhance hydrogen bonding and hydrophobic interactions with the active site of plasmin.…”

Section: Binding Energy Between β-Lg and Plasminmentioning

confidence: 99%

Exploration of Novel Plasmin Inhibitor from β-Lactoglobulin for Enhancing the Storage Stability of UHT Milk

Zhang,

Liu,

Cao

et al. 2024

J. Agric. Food Chem.

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Plasmin-induced protein hydrolysis significantly compromises the stability of ultrahigh-temperature (UHT) milk. β-Lactoglobulin (β-Lg) was observed to inhibit plasmin activity, suggesting that there were active sites as plasmin inhibitors in β-Lg. Herein, plasmin inhibitory peptides were explored from β-Lg using experimental and computational techniques. The results revealed that increased denaturation of β-Lg enhanced its affinity for plasmin, leading to a stronger inhibition of plasmin activity. Molecular dynamics simulations indicated that electrostatic and van der Waals forces were the primary binding forces in the β-Lg/plasmin complex. Denatured β-Lg increased hydrogen bonding and reduced the binding energy with plasmin. The sites of plasmin bound to β-Lg were His624, Asp667, and Ser762. Four plasmin inhibitory peptides, QTMKGLDI, EKTKIPAV, TDYKKYLL, and CLVRTPEV, were identified from β-Lg based on binding sites. These peptides effectively inhibited plasmin activity and enhanced the UHT milk stability. This study provided new insights into the development of novel plasmin inhibitors to improve the stability of UHT milk.

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Section: Binding Energy Between β-Lg and Plasminmentioning

confidence: 99%