Structural, functional, rheological, and biological properties of the swim bladder collagen extracted from grass carp (Ctenopharyngodon idella)

Li, Yushuang; Yang, Likun; Wu, Sijia; Chen, Junde; Lin, Hsuan-Yin

doi:10.1016/j.lwt.2021.112518

Cited by 29 publications

(70 citation statements)

References 23 publications

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“…As an essential structural protein in fish, mainly distributed in fish skin and bone [ 46 ], collagen contains more modifications than its counterpart proteins. Take collagen type I alpha 2 as an example.…”

Section: Resultsmentioning

confidence: 99%

Ozone-Microbubble-Washing with Domestic Equipment: Effects on the Microstructure, and Lipid and Protein Oxidation of Muscle Foods

Pian

Dong

et al. 2022

Foods

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This study aimed to compare ozone-microbubble-washing (OM) performed by domestic equipment with conventional water-washing (CW) regarding resultant quality attributes of muscle foods. For this purpose, muscle microstructure and lipid and protein oxidation were evaluated in pork and fish samples after OM and CW treatments. The assessment of muscle microstructure showed that OM treatment did not damage the microstructure of muscle fibers in both pork and fish samples. Thiobarbituric acid reactive substances (TBARS) values were not detected in both treatment groups, and they were substantially below the generally acceptable threshold (1 mg MDA/kg). The methylglyoxal (MGO) level of OM-treated fish samples was significantly higher than that of CW-treated fish samples. However, glyoxal (GO) and MGO levels of OM-treated pork samples were significantly lower than that of CW-treated pork samples. Similar types and sites of oxidative modification and similar numbers of modified peptides, as well as no significant difference in the concentration of total and most of the free amino acids (FAA) between treatment groups, indicated that OM treatment did not accelerate protein oxidation.

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Section: Resultsmentioning

confidence: 99%

Ozone-Microbubble-Washing with Domestic Equipment: Effects on the Microstructure, and Lipid and Protein Oxidation of Muscle Foods

Pian

Dong

et al. 2022

Foods

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“…The absorbance of the diluted solution was measured at a wavelength of 260 nm using a UH4150 spectrophotometer (Hitachi, Japan) with a 10 mm quartz cell and the baseline was set with the LSL solution (the same concentration with the mixed solution). EAI and ESI were calculated using the following Equations (4) and (5) [ 24,25 ] :

EAI ((), m^{2} / normalg) goodbreak= \frac{((), 2 goodbreak\times 2.303 goodbreak\times A_{0})}{φ \times m_{COP}}

ESI ((), m^{2} / normalg) goodbreak= \frac{A_{0} \times normalΔ t}{normalΔ A}

where A 0 is the absorbance at 0 min after homogenization, m COP is the weight of COP, φ is the oil volume fraction, ∆ t is the time difference (10 min), and ∆ A is the absorbance difference at 0 min and 10 min.…”

Section: Methodsmentioning

confidence: 99%

“…The emulsifying activity index (EAI) and emulsion stability index (ESI) of COP/LSL samples were determined according to the reference with slight modifications. [24,25] Samples of sunflower oil (5 ml) and 0.1 g/L COP/LSL solutions (15 ml) were homogenized for 1 min at a speed of 22,000 rpm. The emulsion from the bottom was collected at 0 min and 10 min then diluted 100-fold with water.…”

Section: Emulsifying Propertiesmentioning

confidence: 99%

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Interactional, functional, and biological properties of lactone sophorolipid (LSL) and collagen oligopeptides (COP) in aqueous solution

Chen¹,

Hao²,

Xuan

et al. 2022

Luminescence

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“…It accounts for about 30% of total proteins and is the most abundant and widely distributed functional protein in animals [ 3 , 4 , 5 ]. At least 29 different types of collagens are distributed throughout all kinds of tissues, and they play important roles in animals and have a distinctive amino acid sequence and molecular structure [ 5 , 6 ]. Because it is characterized by low antigen activity, high cell adhesion, biocompatibility, moisture retention, degradability, and promotion of platelet condensation, collagen is widely used in food, cosmetics, biomedicine, tissue engineering, and other fields [ 5 , 7 , 8 ].…”

Section: Introductionmentioning

confidence: 99%

Properties of Grass Carp (Ctenopharyngodon idella) Collagen and Gel for Application in Biomaterials

Shen

Zhang

et al. 2022

Gels

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The biochemical properties of collagens and gels from grass carp (Ctenopharyngodon idella) were studied to explore the feasibility of their application in biomaterials. The yields of skin collagen (SC) and swim bladder collagen (SBC) extracted from grass carp were 10.41 ± 0.67% and 6.11 ± 0.12% on a wet basis, respectively. Both collagens were characterized as type I collagen. Denaturation temperatures of SC and SBC were 37.41 ± 0.02 °C and 39.82 ± 0.06 °C, respectively. SC and SBC had high fibril formation ability in vitro, and higher values of salinity (NaCl, 0–280 mM) and pH (6–8) in formation solution were found to result in faster self-assembly of SC and SBC fibrils as well as thicker fibrils. Further tests of SC gels with regular morphology revealed that their texture properties and water content were affected by pH and NaCl concentration. The hardness, springiness, and cohesiveness of SC gels increased and the chewiness and water content decreased as pH increased from 7 to 8 and NaCl concentration increased from 140 to 280 mM. These properties suggest that collagens from grass carp may be useful in biomaterial applications in the future.

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Structural, functional, rheological, and biological properties of the swim bladder collagen extracted from grass carp (Ctenopharyngodon idella)

Cited by 29 publications

References 23 publications

Ozone-Microbubble-Washing with Domestic Equipment: Effects on the Microstructure, and Lipid and Protein Oxidation of Muscle Foods

Ozone-Microbubble-Washing with Domestic Equipment: Effects on the Microstructure, and Lipid and Protein Oxidation of Muscle Foods

Interactional, functional, and biological properties of lactone sophorolipid (LSL) and collagen oligopeptides (COP) in aqueous solution

Properties of Grass Carp (Ctenopharyngodon idella) Collagen and Gel for Application in Biomaterials

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