Physicochemical, rheological, and molecular characterization of colloidal gelatin produced from Common carp by‐products using microwave and ultrasound‐assisted extraction

Mirzapour‐Kouhdasht, Armin; Sabzipour, Forouzan; Taghizadeh, Mohammad Sadegh; Moosavi‐Nasab, Marzieh

doi:10.1111/jtxs.12408

Cited by 37 publications

(24 citation statements)

References 37 publications

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“…Gelatin solutions (6.67% w/v) were prepared in distilled water following heating to 60°C. The viscosity (cP) of 10 ml of gelatin solutions was evaluated using a Brookfield viscometer (DV-II, Brookfield Scientific Promotion Co., Ltd. Middleboro, MA) operated at 90 rpm and 25°C [ 29 ].…”

Section: Methodsmentioning

confidence: 99%

Influence of collagen and some proteins on gel properties of jellyfish gelatin

et al. 2021

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Marine gelatin is one of the food proteins used in food and non-food products, offering desirable functionalities such as gelling, thickening, and binding. Jellyfish has been chosen for this gelatin research, in view of the benefits of its main collagen protein and lower fat content, which may reduce the amounts of chemicals used in the preparative steps of gelatin production. To date, the lack of identified proteins in gelatin has limited the understanding of differentiating intrinsic factors quantitatively and qualitatively affecting gel properties. No comparison has been made between marine gelatin of fish and that of jellyfish, regarding protein type and distribution differences. Therefore, the study aimed at characterizing jellyfish gelatin extracted from by-products, that are i.e., pieces that have broken off during the grading and cleaning step of salted jellyfish processing. Different pretreatment by hydrochloric acid (HCl) concentrations (0.1 and 0.2 M) and hot water extraction time (12 and 24 h) were studied as factors in jellyfish gelatin extraction. The resultant jellyfish gelatin with the highest gel strength (JFG1), as well as two commercial gelatins of fish gelatin (FG) and bovine gelatin (BG), were analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). The results show that the jellyfish gelatin (JFG1) extracted with 0.1 M HCl at 60°C for 12 h delivered a maximum gel strength of 323.74 g, which is lower than for FG and BG, exhibiting 640.65 and 540.06 g, respectively. The gelling and melting temperatures of JFG1 were 7.1°C and 20.5°C, displaying a cold set gel and unstable gel at room temperature, whereas the gelling and melting temperatures of FG and BG were 17.4°C, 21.3°C, and 27.5°C, 32.7°C, respectively. Proteomic analysis shows that 29 proteins, of which 10 are types of collagen proteins and 19 are non-collagen proteins, are common to all BG, FG, and JFG1, and that JFG1 is missing 3 other collagen proteins (collagen alpha-2 (XI chain), collagen alpha-2 (I chain), and collagen alpha-2 (IV chain), that are important to gel networks. Thus, the lack of these 3 collagen types influences the inferior gel properties of jellyfish gelatin.

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Section: Methodsmentioning

confidence: 99%

Influence of collagen and some proteins on gel properties of jellyfish gelatin

et al. 2021

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“…Therefore, a high amount of CBJ has an antagonistic effect on the gelling process with a low amount of gelatin gel solution, leading to a fragile structure, which is prone to severe internal changes when subjected to external factors. Even so, M5 showed a viscosity in the range of commercial gelatin gels (2-7 (kPa•s)) [48], allowing a marketable advantage to develop aerated gelatin gel-based products with a liquid ingredient such as cryoconcentrated juice.…”

Section: Apparent Viscosity Density and Gas Hold-up Measurementsmentioning

confidence: 99%

Comparative Study of the Structural Properties, Color, Bioactive Compounds Content and Antioxidant Capacity of Aerated Gelatin Gels Enriched with Cryoconcentrated Blueberry Juice during Storage

2020

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Cryoconcentrated blueberry juice (CBJ) was incorporated into aerated gelatin gel and the effects on the mechanical properties, phenolic compounds and antioxidant activity (AA) were evaluated at day 1 and day 28 under refrigerated storage. At day 1, 8 g of gelatin gel and 40 g of CBJ (called M5) exhibited a soft texture and heterogeneous and non-spherical small bubbles, with values close to 10.5, 8.0 and 7.1 N, for hardness, gumminess and chewiness, respectively. M5 presented an increase of approximately 1.7, 1.9 and 1.9, and 1.2, 1.8, 2.1 and 1.3 times in comparison to the other samples, for total polyphenol, anthocyanin and flavonoid contents, and individual phenolic compounds, 2,2-diphenyl-1-picrylhydrazyl (DPPH), ferric reducing antioxidant power (FRAP) and oxygen radical absorbance capacity (ORAC) assays, respectively. At day 28, the samples showed a weakening of the 3D network, with high degradation of phenolic compounds and AA due to the oxidation, polymerization and syneresis. Therefore, CBJ might be an interesting functional ingredient to add to (aerated and non-aerated) gelatin gel without affecting its properties, and thus different food products with high nutritional values and without added artificial sweeteners could be developed. Additionally, the gelatin gel/CBJ combinations might be suitable for additive manufacturing as a coating of food matrices.

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“…However, in the experimental range of microwave extraction time, the yield of gelatin extracted by MAE was relatively lower than that of WBE (7.50%) (p < .05). In the published articles, the yield of gelatin extracted by microwave is relatively low, and the values are 0.75% [17] and 1.27%, [29] respectively. Generally, a longer extraction time was beneficial for obtaining a higher yield because more collagen was hydrolyzed and converted into gelatin, which could be revealed by the results of Figure 1.…”

Section: Yield Of Rabbit Skin Gelatinmentioning

confidence: 99%

Structure of Hyla rabbit skin gelatin as affected by microwave-assisted extraction

Liu

Dai

et al. 2019

International Journal of Food Properties

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In this study, we investigated the effect of microwave-assisted extraction (MAE) on the yield, structure, and properties of rabbit skin gelatin. Compared to water bath extraction gelatin, short-term (5-30 min) MAE gelatin had better gel properties, which formed gels at a slower rate due to destruction of more hydrogen bonds, but had more powerful triple helix-like structures after a sufficiently long maturity (16-18 h) since more high-molecular-weight subunits were retained. Scanning electron microscope showed that MAE could form numerous holes on the surface of gelatin. This study will be of great significance for high efficiency of gelatin extraction.

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Physicochemical, rheological, and molecular characterization of colloidal gelatin produced from Common carp by‐products using microwave and ultrasound‐assisted extraction

Cited by 37 publications

References 37 publications

Influence of collagen and some proteins on gel properties of jellyfish gelatin

Influence of collagen and some proteins on gel properties of jellyfish gelatin

Comparative Study of the Structural Properties, Color, Bioactive Compounds Content and Antioxidant Capacity of Aerated Gelatin Gels Enriched with Cryoconcentrated Blueberry Juice during Storage

Structure of Hyla rabbit skin gelatin as affected by microwave-assisted extraction

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