The changes in structure analysis of PSPI indicated that ultrasound treatment could induce molecular unfolding of protein, which might be helpful for improving the functional properties and efficiency of enzymatic hydrolysis. © 2018 Society of Chemical Industry.

BackgroundTyro3, Axl, and Mertk (TAMs) are a family of three conserved receptor tyrosine kinases that have pleiotropic roles in innate immunity and homeostasis and when overexpressed in cancer cells can drive tumorigenesis.MethodsIn the present study, we engineered EGFR/TAM chimeric receptors (EGFR/Tyro3, EGFR/Axl, and EGF/Mertk) with the goals to interrogate post-receptor functions of TAMs, and query whether TAMs have unique or overlapping post-receptor activation profiles. Stable expression of EGFR/TAMs in EGFR-deficient CHO cells afforded robust EGF inducible TAM receptor phosphorylation and activation of downstream signaling.ResultsUsing a series of unbiased screening approaches, that include kinome-view analysis, phosphor-arrays, RNAseq/GSEA analysis, as well as cell biological and in vivo readouts, we provide evidence that each TAM has unique post-receptor signaling platforms and identify an intrinsic role for Axl that impinges on cell motility and invasion compared to Tyro3 and Mertk.ConclusionThese studies demonstrate that TAM show unique post-receptor signatures that impinge on distinct gene expression profiles and tumorigenic outcomes.Electronic supplementary materialThe online version of this article (doi:10.1186/s12964-016-0142-1) contains supplementary material, which is available to authorized users.

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The effects of heating (90°C/30 min) or ultrasound (200/400/600 W) treatment on antioxidant and angiotensin-converting enzyme inhibitory (ACEI) activity of hydrolysates from hempseed protein isolates (HPI) were studied. The secondary structure, surface hydrophobicity, intrinsic fluorescence, scanning electron microscopy (SEM) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis of HPI treated by heating or ultrasound were measured. The results showed that hydrolysate from HPI treated with ultrasound at 200 W showed higher hydrolysis degree, proportion of lower molecular mass components (1.0-3.0 kDa), antioxidant and ACEI activity than those from heating or high-power treated. The changes in secondary structure, surface hydrophobicity and intrinsic fluorescence indicated the unfolding of HPI after ultrasound. The SEM results showed that HPI treated with ultrasound at 200 W exhibited decrease in particle size and deformation and further increased in power caused the aggregates of HPI. In conclusion, the ultrasound treatment at low-power was superior to 90°C/30 min treatment in facilitating enzymatic release of antioxidant and ACEI peptides from HPI.

The application of protein-polyphenol complexes is increasing and broadening in recent years. Due to their unique properties, these complexes are attracting increased research interest. In this study, the cyanidin-3-galactoside was grafted to the caseins using free radicles induced by ultrasound. The formation of conjugation between caseins and cyanidin-3-galactoside was confirmed by the decrease in free amino groups and sulfhydryl content. Conjugation with cyanidin-3-galactoside resulted in aggregation of caseins, which also led to increase in particle size, relative fluorescence intensity and random coil. Conjugation also disrupted the hydrogen bonds and decreased the electrostatic repulsion and hydrophobic interactions between caseins. The caseins-cyanidin-3-galactoside conjugate had better emulsifying, gelation properties and lower thermal stability than that of caseins.