Molecular and thermal characteristics of acid-soluble collagen from orbicular batfish: effects of deep-sea water culturing

Pan, Bonnie Sun; Chen, Hoa En; Sung, Wen Chieh

doi:10.1080/10942912.2018.1476873

Cited by 8 publications

(10 citation statements)

References 36 publications

(42 reference statements)

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“…It shifted to 0.5 Cp when the hydrolysis had been going on for 1 h. After this time, no significant changes ( p ≥ 0.05) were observed. The triple helix structure of native collagen was changed to a random coil form due to the dissociation of the hydrogen bonds [51].…”

Section: Resultsmentioning

confidence: 99%

Hydrolysed Collagen from Sheepskins as a Source of Functional Peptides with Antioxidant Activity

León-López

Fuentes-Jiménez

Hernández-Fuentes

et al. 2019

IJMS

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The extraction and enzymatic hydrolysis of collagen from sheepskins at different times of hydrolysis (0, 10, 15, 20, 30 min, 1, 2, 3 and 4 h) were investigated in terms of amino acid content (hydroxyproline), isoelectric point, molecular weight (Mw) by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) method, viscosity, Fourier-transform infrared (FTIR) spectroscopy, antioxidant capacity by 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) assays, thermal properties (Differential Scanning Calorimetry) and morphology by scanning electron microscopy (SEM) technique. The kinetics of hydrolysis showed an increase in the protein and hydroxyproline concentration as the hydrolysis time increased to 4 h. FTIR spectra allowed us to identify the functional groups of hydrolysed collagen (HC) in the amide I region for collagen. The isoelectric point shifted to lower values compared to the native collagen precursor. The change in molecular weight and viscosity from time 0 min to 4 h promoted important antioxidant activity in the resulting HC. The lower the Mw, the greater the ability to donate an electron or hydrogen to stabilize radicals. From the SEM images it was evident that HC after 2 h had a porous and spongy structure. These results suggest that HC could be a good alternative to replace HC from typical sources like pigs, cows and fish.

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Section: Resultsmentioning

confidence: 99%

Hydrolysed Collagen from Sheepskins as a Source of Functional Peptides with Antioxidant Activity

León-López

Fuentes-Jiménez

Hernández-Fuentes

et al. 2019

IJMS

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“…Viscosity is one of the physicochemical properties of collagen; the native form shows higher values due to stronger electrostatic repulsion among the molecular chains even at low concentrations of collagen solution. However, its hydrolyzed form shows very low viscosity no matter the concentration because of the low molecular weight of the small chain segments [69]. Electrostatic properties of proteins such as the isoelectric point (pI) are important parameters which are related to the proportion of acid amino residues and base amino residues in protein.…”

Section: Hydrolyzed Collagen: Extraction and Propertiesmentioning

confidence: 99%

Hydrolyzed Collagen—Sources and Applications

et al. 2019

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Hydrolyzed collagen (HC) is a group of peptides with low molecular weight (3–6 KDa) that can be obtained by enzymatic action in acid or alkaline media at a specific incubation temperature. HC can be extracted from different sources such as bovine or porcine. These sources have presented health limitations in the last years. Recently research has shown good properties of the HC found in skin, scale, and bones from marine sources. Type and source of extraction are the main factors that affect HC properties, such as molecular weight of the peptide chain, solubility, and functional activity. HC is widely used in several industries including food, pharmaceutical, cosmetic, biomedical, and leather industries. The present review presents the different types of HC, sources of extraction, and their applications as a biomaterial.

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“…However, the nature of thermal collagen is also influenced by the origin of collagen. Collagen derived from marine fish has higher thermal properties by 1.7 °C than collagen originating from cultured fish (41).…”

Section: Collagenmentioning

confidence: 94%

Thermal Behavior of Polymers in Solid-State

Butarbutar

Chaerunisaa

2022

sciphar

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A variety of potential polymers with chemical and physical stability characteristics and abundant availability lead to the rapid application of polymers in various fields. One of the crucial things that are crucial to be discussed from such polymers is the characteristic of thermal behavior. Each type of polymer such as natural and synthetic has different thermal characteristics, including Tc, Tg, Tm, and Td which can be the determining factor of polymer selection of processing and application temperature. The thermal properties will also affect molecular interactions, physical stability in manufacturing, distribution, and storage. Therefore, in this article will appoint a study on the thermal characteristics of natural and synthetic polymers, the effect of modification on the thermal properties of polymers, efforts to increase the stability of thermal, and polymer applications in the field of pharmaceutical technology.

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Molecular and thermal characteristics of acid-soluble collagen from orbicular batfish: effects of deep-sea water culturing

Cited by 8 publications

References 36 publications

Hydrolysed Collagen from Sheepskins as a Source of Functional Peptides with Antioxidant Activity

Hydrolysed Collagen from Sheepskins as a Source of Functional Peptides with Antioxidant Activity

Hydrolyzed Collagen—Sources and Applications

Thermal Behavior of Polymers in Solid-State

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