Yield, viscosity, and gel strength of wami tilapia (Oreochromis urolepis hornorum) skin gelatin: Optimization of the extraction process

Alfaro, Alexandre da Trindade; Fonseca, Gustavo Graciano; Balbinot, Evellin; Souza, Nilson Evelázio de; Prentice, Carlos

doi:10.1007/s10068-014-0103-7

Cited by 14 publications

(8 citation statements)

References 20 publications

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“…This result was in accordance with the study on gelatine from Wami tilapia, clown featherback and chum salmon where lower gel strength was reported when gelatine was extracted at a higher temperature. 6,8,13 G45 had a higher gel strength compared to commercial bovine gelatine whereas the gel strength of G55 had no significant different with bovine gelatine ( p < 0.05). On the other, the gel strength of G65 and G75 were lower than bovine gelatine ( p < 0.05).…”

Section: Gel Strengthmentioning

confidence: 83%

Effect of Extraction Temperature on the Physicochemical Properties of Gelatine from the Skin of Black Tilapia (Oreochromis mossambicus)

Tan¹,

Karim²,

Uthumporn³

et al. 2019

JPS

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The physicochemical properties of gelatine from the skin of black tilapia (Oreochromis mossambicus) as affected by different extraction temperatures (45°C, 55°C, 65°C and 75°C) were investigated. The yield of gelatine increased significantly as the extraction temperature increased. Electrophoretic protein pattern and free amino acid content of tilapia gelatine showed that high extraction temperature (75°C) contributed to the decrease in major protein components (α-and β-chains) of the extracted gelatine. Fourier transform infrared (FTIR) spectroscopy showed a significant loss of triple helical structure in all samples. The gel strength, gelling temperature and melting temperature of tilapia gelatine decreased as the extraction temperature increased. The gelling and melting temperature of gelatine extracted at 45°C (G45) was 18.9°C and 26.2°C, respectively, which was about 2°C lower than those of the bovine gelatine tested. This suggested that G45 and bovine gelatine gel possessed similar thermal stability. In addition, the rheological test revealed that, as the extraction temperature increased, the storage modulus (G′) of tilapia gelatine was frequency dependent and took a relatively long time to achieve maximum G′ at 10°C. Black tilapia gelatine showed higher emulsion ability and emulsion stability when lower extraction temperatures were used. The foaming properties of tilapia gelatine was similar among gelatine extracted from 45°C to 65°C. A significant decrease in foamability and stability was observed when extraction temperature further increased to 75°C. Therefore, black tilapia gelatine extracted at 45°C has the functional properties that are comparable to bovine gelatine.

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Section: Gel Strengthmentioning

confidence: 83%

Effect of Extraction Temperature on the Physicochemical Properties of Gelatine from the Skin of Black Tilapia (Oreochromis mossambicus)

Tan¹,

Karim²,

Uthumporn³

et al. 2019

JPS

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“…Gelatin solutions (6.67% w/v) were prepared in distilled water fallowing heating to 60°C. The viscosity (mPa s) of 10 mL of gelatin solutions were evaluated by a Brookfield viscometer (LVDV‐II, Brookfield Engineering Laboratories Ltd., Middleboro, MA) at 90 rpm, at temperature of 25°C according to da Trindade Alfaro, Fonseca, Balbinot, de Souza, and Prentice ().…”

Section: Methodsmentioning

confidence: 99%

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

Mirzapour‐Kouhdasht

Sabzipour

Taghizadeh

et al. 2019

Journal of Texture Studies

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The effects of ultrasound‐assisted extraction (UAE) and microwave‐assisted extraction (MAE) methods on molecular and physicochemical characteristics of the resultant gelatin were examined. Before extraction procedure, we investigated the optimum pH for swelling of Common carp by‐products, which is an important pretreatment for gelatin production. The highest swelling yield was achieved at pH 13 among pH 1–14 with unit intervals. Results indicated that the UAE gelatin has a higher gel strength, viscosity, melting point, and gelling point. The power and time of sonication showed a reverse relation with these characteristics. In addition, as the time of microwave heating was raised, the gel strength, viscosity, melting point, and gelling point were decreased. The FT‐IR spectra showed similar peaks but the Amide B in UAE gelatin slightly vanished. The electrophoretic pattern also revealed the higher gel strength and viscosity of UAE gelatin due to the higher intensity of α and β chains compared to MAE gelatin. It can be concluded from all of the results of this study that the produced gelatin using these procedures can be a good source of gelatin in food and drug industries.

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“…The results were higher than those found for gelatin from lizard scale (Saurida spp. ), which ranged from 3.14 to 5, 80 cP for 6.67% solutions at 25 °C (Wangtueai & Noomhorm, 2009), and gelatin from tilapia skin (Oreochromis urolepis hornorum), which ranged from 2.56 to 6.12 cP at a temperature of 60 °C (Alfaro et al, 2014). Table 2 shows the results for foam expansion capacity (FEC) and foam stability (FS).…”

Section: Viscositymentioning

confidence: 99%

Characterization of hydrolysates of collagen from mechanically separated chicken meat residue

et al. 2020

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Dbtaining collagen and hydrolysates from mechanically separated chicken meat residue is an excellent way to add value to this waste. The aims of this study were to obtain collagen hydrolysates from chicken MSM residue using Alcalase  and Flavourzyme  enzymes, as well characterizing the functional, structural and thermal stability properties. The highest degree of hydrolysis was obtained using Alcalase  , 36.11%, while using Flavourzyme  resulted in 12.02%. The DSC analysis of the collagen indicated a denaturation temperature of 46.47 °C. The FTOR spectra of the crude collagen showed absorption peaks that were characteristic of amide bands A, B, O, OO and OOO. On the spectra of the hydrolysed the area of the amide bands was reduced, and some peaks appeared between 800 and 1,200 cm-1. The disappearance of high molecular weight bands in the SDS-PAGE analysis also confirmed the hydrolysis of collagen. After the hydrolysis, the collagen presented reduced viscosity, the capacity to form foam, and foam stability. The emulsifying activity index was high in the hydrolysates in relation to the crude collagen. Thus, the use of Alcalase  and Flavourzyme  to obtain hydrolysates from collagen derived from chicken MSM residue was shown to be viable, and potentially useful for industrial applications.

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Yield, viscosity, and gel strength of wami tilapia (Oreochromis urolepis hornorum) skin gelatin: Optimization of the extraction process

Cited by 14 publications

References 20 publications

Effect of Extraction Temperature on the Physicochemical Properties of Gelatine from the Skin of Black Tilapia (Oreochromis mossambicus)

Effect of Extraction Temperature on the Physicochemical Properties of Gelatine from the Skin of Black Tilapia (Oreochromis mossambicus)

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

Characterization of hydrolysates of collagen from mechanically separated chicken meat residue

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