Inducing secondary structural interplays between scallop muscle proteins and soy proteins to form soluble composites

Abstract

Scallop muscle proteins and soya proteins were packed into a composite with tunable internal, molecular arrangements of the secondary structures.

Co‐folding scallop muscle proteins with soy β‐conglycinin or glycinin towards composites with tunable solubility and digestibility

“…Reducing the proportion of 7S in SPGs from 100% (7S/11S = 1:0) to 0% (7S/11S = 0:1) resulted in an obvious decreased intensity in of the co‐assembled proteins, accompanied by a red shift of from 345–355 nm. The red‐shifting of the spectrum indicated solvent exposure of hydrophilic motifs (Tang et al ., 2009) and, therefore, shed light on the hydrophobic attraction between SMPs and SPGs (Wang et al ., 2020; Wu et al ., 2020a). As larger particle size was found in samples with higher proportion of 11S that was more hydrophobic than 7S (Vivian & Callis, 2001), the aggregation was strengthened during the co‐assembly (Wu et al ., 2020a; Na et al ., 2021).…”

“…SMPs were extracted according to the method of Wu et al . (2020a). The scallop adductor muscle was mixed with deionised water at a solid–liquid ratio of 1:10 (w/v) and further homogenised using a tissue homogeniser for 2 min.…”

“…rationed that at an alkaline environment, proteins from different origins were unfolded, while the followed acidification triggered simultaneous generation of hydrophobic pockets by which they were folded together (Zhang & Lynd, 2004) (Wang et al ., 2020). Soluble composites of SMPs and soy proteins (SPs) were also fabricated in our earlier study (Wu et al ., 2020a). Moreover, soy proteins are composed of two major components, namely conglycinin (7S) and glycinin (11S), and the 7S is a glycoprotein with higher hydrophilicity than 11S (Nielsen, 1985; Clara Sze et al ., 2007).…”

Advancement of food‐derived mixed protein systems: Interactions, aggregations, and functional properties

“…During this process, the unfolding of proteins can be easily determined by fluorescence and near‐UV circular dichroism (CD) instruments. Based on the MG environment where high basicity (pH 12) enabled complete unfolding of proteins, the intact secondary structures from two different origins intertwined into shared structures (Wu, Wang, Na, et al., 2020).…”

“…Relying on the above techniques, several hydrophobic proteins, such as rice proteins (Wang, Xu, et al., 2019), wheat prolamins (He et al., 2020), and scallop myofibrillar proteins (Wu, Wang, Na, et al., 2020) generally insoluble in water, were combined into water‐dispersible composites. One major finding was that the co‐folded secondary structures obtained greater structural strength relative to each individuals.…”