Plastein from hydrolysates of porcine hemoglobin and meat using Alcalase and papain

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Plastein from hydrolysates of porcine hemoglobin and meat using Alcalase and papain. / Li, Qian; Fu, Yu; Zhang, Longteng; Otte, Jeanette; Lametsch, René.

In: Food Chemistry, Vol. 320, 126654, 2020.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Li, Q, Fu, Y, Zhang, L, Otte, J & Lametsch, R 2020, 'Plastein from hydrolysates of porcine hemoglobin and meat using Alcalase and papain', Food Chemistry, vol. 320, 126654. https://doi.org/10.1016/j.foodchem.2020.126654

APA

Li, Q., Fu, Y., Zhang, L., Otte, J., & Lametsch, R. (2020). Plastein from hydrolysates of porcine hemoglobin and meat using Alcalase and papain. Food Chemistry, 320, [126654]. https://doi.org/10.1016/j.foodchem.2020.126654

Vancouver

Li Q, Fu Y, Zhang L, Otte J, Lametsch R. Plastein from hydrolysates of porcine hemoglobin and meat using Alcalase and papain. Food Chemistry. 2020;320. 126654. https://doi.org/10.1016/j.foodchem.2020.126654

Author

Li, Qian ; Fu, Yu ; Zhang, Longteng ; Otte, Jeanette ; Lametsch, René. / Plastein from hydrolysates of porcine hemoglobin and meat using Alcalase and papain. In: Food Chemistry. 2020 ; Vol. 320.

Bibtex

@article{bf23339a01634ca1924014827ceba453,
title = "Plastein from hydrolysates of porcine hemoglobin and meat using Alcalase and papain",
abstract = "Plastein is defined as a protease-induced peptide aggregate and has been explored for over a century. This study investigated the effects of Alcalase and papain on plastein formation in protein hydrolysates of porcine hemoglobin and meat by measuring turbidity, particle size distribution, free amino groups and chemical interactions, as well as identifying the soluble peptides remaining in solution by LC–MS/MS. The results showed that Alcalase induced more peptide aggregation than papain in terms of increases in turbidity and particle size. Porcine hemoglobin was better than meat in inducing plastein formation in a short reaction time. Besides, covalent bonds involving peptide bonds and disulfide bonds were not crucial in the plastein reaction, instead a high proportion of hydrophobic interactions dominated the plastein. Not all peptides of both hydrolysates took part in plastein formation, and the regions of sequence that were prone to aggregation were visualized by Peptigram.",
keywords = "Meat, Peptide characterization, Plastein, Porcine hemoglobin",
author = "Qian Li and Yu Fu and Longteng Zhang and Jeanette Otte and Ren{\'e} Lametsch",
year = "2020",
doi = "10.1016/j.foodchem.2020.126654",
language = "English",
volume = "320",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Plastein from hydrolysates of porcine hemoglobin and meat using Alcalase and papain

AU - Li, Qian

AU - Fu, Yu

AU - Zhang, Longteng

AU - Otte, Jeanette

AU - Lametsch, René

PY - 2020

Y1 - 2020

N2 - Plastein is defined as a protease-induced peptide aggregate and has been explored for over a century. This study investigated the effects of Alcalase and papain on plastein formation in protein hydrolysates of porcine hemoglobin and meat by measuring turbidity, particle size distribution, free amino groups and chemical interactions, as well as identifying the soluble peptides remaining in solution by LC–MS/MS. The results showed that Alcalase induced more peptide aggregation than papain in terms of increases in turbidity and particle size. Porcine hemoglobin was better than meat in inducing plastein formation in a short reaction time. Besides, covalent bonds involving peptide bonds and disulfide bonds were not crucial in the plastein reaction, instead a high proportion of hydrophobic interactions dominated the plastein. Not all peptides of both hydrolysates took part in plastein formation, and the regions of sequence that were prone to aggregation were visualized by Peptigram.

AB - Plastein is defined as a protease-induced peptide aggregate and has been explored for over a century. This study investigated the effects of Alcalase and papain on plastein formation in protein hydrolysates of porcine hemoglobin and meat by measuring turbidity, particle size distribution, free amino groups and chemical interactions, as well as identifying the soluble peptides remaining in solution by LC–MS/MS. The results showed that Alcalase induced more peptide aggregation than papain in terms of increases in turbidity and particle size. Porcine hemoglobin was better than meat in inducing plastein formation in a short reaction time. Besides, covalent bonds involving peptide bonds and disulfide bonds were not crucial in the plastein reaction, instead a high proportion of hydrophobic interactions dominated the plastein. Not all peptides of both hydrolysates took part in plastein formation, and the regions of sequence that were prone to aggregation were visualized by Peptigram.

KW - Meat

KW - Peptide characterization

KW - Plastein

KW - Porcine hemoglobin

U2 - 10.1016/j.foodchem.2020.126654

DO - 10.1016/j.foodchem.2020.126654

M3 - Journal article

C2 - 32222661

AN - SCOPUS:85082110809

VL - 320

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

M1 - 126654

ER -

ID: 240147904