Effect of heat treatment on the binding of selected flavor compounds to myofibrillar proteins

Abstract

BACKGROUND The influence of heat‐induced structural modifications of grass carp myofibrillar protein (MP) on its ability to bind to selected aldehydes (hexanal, heptanal, octanal and nonanal) was investigated. The interactions of MP and flavor compounds were investigated using HS‐GC‐MS, intrinsic fluorescence spectra, Raman spectra, SDS‐PAGE, turbidity, total sulfhydryl content and surface hydrophobicity. RESULTS The ability to bind to aldehydes was strongly influenced by changes in the structure and surface of proteins during the heating process (0–30 min). During the first 0–10 min of heating, the flavor‐binding ability increased, which is likely attributable to increased surface hydrophobicity and total sulfhydryl content, and to the unfolding of secondary structures of MP by exposure to reactive amino acids, sulfhydryl groups and hydrophobic bonding sites. Nevertheless, lengthy heating (>10 min) caused protein refolding and accelerated aggregation of protein, thus reducing hydrophobic interactions and weakening the resultant capacity of MP to bind to flavor compounds. CONCLUSION The results suggested that hydrophobic interactions were enhanced upon short‐term heating, whereas long‐term heating weakend them. The results provide information concerning improvement of the flavor profile of freshwater fish surimi products. © 2019 Society of Chemical Industry

Binding of aldehydes to myofibrillar proteins as affected by two‐step heat treatments

“…, the initial binding capacity of the four selected aldehydes was between 17 and 25%, which was in accordance with the retention of aldehydes by MPs or myosin . Furthermore, among the four aldehydes, the binding ability to control MPs increased as the carbon chain length increased, which is attributed to the stronger hydrophobic interactions …”

“…The MPs were adjusted to 3 mg mL −1 and blended with SDS‐PAGE sample buffer with and without 50 mL L −1 β ‐mercaptoethanol ( β ‐ME) in a ratio of 1:1 (v/v). SDS‐PAGE was performed according to our previous work . A pre‐stained wide molecular weight marker was used to estimate protein molecular weight.…”

“…Aldehyde binding to proteins was performed according to previous work using an Agilent 7890 gas chromatograph (GC) equipped with an Agilent 5975 quadrupole mass‐selective detector (MS) (Agilent Technologies, USA). After equilibration as described above, samples were incubated and shaken at 50 °C for 10 min.…”

“…Aquatic proteins are odorless in themselves, but their sensory attributes can be altered by adsorbing odor compounds, causing a reduction in consumer acceptability . Myofibrillar proteins (MPs), as the predominant component of surimi, play an important role in the processing of surimi products, with a direct effect on their texture and water‐holding capacity.…”

Vacuum microwave dehydration decreases volatile concentration and soluble protein content of pea (Pisum sativum L.) protein

“…By irreversibly binding volatile flavour compounds, this explained why volatile compound concentration decreased. However, denaturation and aggregation of proteins may also release previously bound flavour molecules 32,33 . This partially explained the varying conclusions regarding protein–flavour binding in the literature.…”