Stability of Barley and Malt Lipid Transfer Protein 1 (LTP1) toward Heating and Reducing Agents: Relationships with the Brewing Process
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文摘
Barley lipid transfer protein (LTP1) is a heat-stable and protease-resistant albumin that concentratesin beer, where it participates in the formation and stability of beer foam. Whereas the barley LTP1does not display any foaming properties, the corresponding beer protein is surface-active. Such animprovement is related to glycation by Maillard reactions on malting, acylation on mashing, andstructural unfolding on brewing. The structural stability of purified barley and glycated malt LTP1toward heating has been analyzed. Whatever the modification, lipid adduction or glycation, barleyLTP1s are highly stable proteins that resisted temperatures up to 100 C. Unfolding of LTP1 occurredonly when heating was conducted in the presence of a reducing agent. In the presence of sodiumsulfite, the lipid-adducted barley and malt LTP1 displayed higher heat stability than the nonadductedprotein. Glycation had no or weak effect on heat-induced unfolding. Finally, it was shown that unfoldingoccurred on wort boiling before fermentation and that the reducing conditions are provided by maltextract.Keywords: Lipid transfer protein 1; protein unfolding; malting; brewing

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