Interaction mechanism of collagen peptides with four phenolic compounds in the ethanol-water solution

Abstract

This study demonstrated the interaction mechanism of collagen peptides (CPs) with 4-ethylphenol (4-EP), phenol, guaiacol, and 4-ethylguaiacol (4-EG) in the ethanol-water solution. The ultraviolet visible spectroscopy, zeta potential tests and hydrogen nuclear magnetic spectroscopy manifested that CPs interacted with the phenolic compounds. Meanwhile, Isothermal titration calorimetry determination indicated that the CPs was hydrogen bonded with 4-EP in 52 %(v/v) ethanol-water solution, while the hydrophobic forces played a major role in the interaction of CPs with guaiacol and 4-EG, respectively. Moreover, hydrogen and hydrophobic bonds were involved in the interaction between CPs and phenol. Finally, Head Space-solid Phase Microextraction Gas Chromatography Mass Spectrometry analysis indicated that the content of phenolic compounds in model solution efficiently decreased with the presence of CPs. In the real liquor, it was found that the content of volatile compounds (including phenolic compounds) was obviously decreased after CPs added.

Collagen-Based Organohydrogel Strain Sensor with Self-Healing and Adhesive Properties for Detecting Human Motion

“…The appearance of these two characteristic peaks proved that the extracted Col had the typical triple helix structure . Likewise, the SDS–PAGE images of the extracted Col (Figure S1b) showed three distinct electrophoretic bands, indicating that the prepared Col had two distinct α chains (α1 and α2) and cross-linked β chains …”

“…29 Likewise, the SDS−PAGE images of the extracted Col (Figure S1b) showed three distinct electrophoretic bands, indicating that the prepared Col had two distinct α chains (α1 and α2) and crosslinked β chains. 31 The three-dimensional network skeleton of the CDPAP organohydrogel was mainly composed of two dynamic crosslinking networks. As can be seen in Figure 1b, Schiff base bonding could take place between the side-chain amino groups of Col and the aldehyde groups of DCMC, which constitute the first-layer dynamic cross-linking network of the CDPAP organohydrogel.…”

“…The selection of raw materials is also an important part for the preparation of hydrogel sensors. Collagen is one of the important components of natural animal skins (or hides) and possesses many unique advantages, such as excellent bioactivity, , biocompatibility, − and biodegradability. , It is considered as an ideal raw material for the preparation of biomimetic electronic skin and flexible sensors. However, few literature has reported the incorporation of collagen into conductive hydrogels to prepare self-healing flexible sensors.…”

Collagen Glycopeptides from Transglutaminase-Induced Glycosylation Exhibit a Significant Salt Taste-Enhancing Effect

“…25 Collagen hydrolysates have various functional and physiological properties. 26 Therefore, tilapia skin collagen is an ideal raw material for preparation of salt taste-enhancing peptides. In this study, tilapia fish skin collagen was used as raw material to prepare collagen glycopeptides by Flavourzyme-treated hydrolysis (to avoid generation of bitter peptides), followed by enzymatic glycosylation using transglutaminase.…”

“…Most importantly, collagen hydrolysates without bitter peptides tend to have a mild taste due to the high content of Gly compared to other protein hydrolysates . Collagen hydrolysates have various functional and physiological properties . Therefore, tilapia skin collagen is an ideal raw material for preparation of salt taste-enhancing peptides.…”