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Ile‐Pro‐Pro and Val‐Pro‐Pro are two most well‐known food‐derived bioactive peptides, initially identified as inhibitors of angiotensin I‐converting enzyme (ACE) from a sample of sour milk. These two peptides were identified in fermented and enzymatic hydrolyzed cow and non‐cow (that is, goat, sheep, buffalo, yak, camel, mare, and donkey) milk, as well as sourdough prepared from wheat, rye, and malt. Similar to other bioactive peptides, bioavailability of these peptides is low (about 0.1%), reaching picomolar concentration in human plasma; they showed blood pressure lowering activity in animals and in human, via improved endothelial function, activation of ACE2, and anti‐inflammatory property. Emerging bioactivities of these two peptides toward against metabolic syndrome and bone‐protection received limited attention, but may open up new applications of these peptides as functional food ingredients. Further studies are warranted to determine the best source as well as to identify novel enzymes (particularly from traditional fermented milk products) to improve the efficiency of production, to characterize possible peptide receptors using a combination of omics technology with molecular methods to understand if these two peptides act as signal‐like molecules, to improve their bioavailability, and to explore new applications based on emerging bioactivities.

A series of organically–inorganically functionalized MCM-41 compounds have been prepared with 3-aminopropyltrimethoxysilane (APTMS) as the organic component and CuO and/or Cu(NO3)2 as the inorganic component. The textural properties of functionalized MCM-41 were characterized by powder X-ray diffraction (XRD), nitrogen adsorption–desorption, and transmission electron microscopy (TEM). The results indicate that the hexagonally ordered structure of MCM-41 remained intact after functionalization. The presence of grafted organosilanes was confirmed by Fourier transform infrared (FTIR) spectra, 13C nuclear magnetic resonance (13C CP-MAS NMR), and 29Si nuclear magnetic resonance (29Si MAS NMR). All adsorbents showed similar desulfurization performances for different sulfur compounds in the order tert-butyl mercaptan (TBM) > dimethyl sulfide (DMS) > dimethyl disulfide (DMDS), which is due to the poor reactivities and polarities of DMS and DMDS. MCM-41-NH2-Cu functionalized with Cu2+ as the active sites is the most efficient adsorbent for the removal of TBM. The desulfurization mechanism was discussed based on the experimental results and X-ray photoelectron spectroscopy (XPS) characterization. The results show that CuO plays a more dominant role than Cu2+ for the removal of DMS and DMDS.

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