Effects of α1/α2 ratios and drying temperatures on the properties of gelatin films prepared from tilapia (Tilapia zillii) skins

Chen, Shulin; Tang, Lanlan; Hao, Gengxin; Weng, Wuyin; Osako, Kazufumi; Tanaka, Munehiko

doi:10.1016/j.foodhyd.2015.07.026

Cited by 18 publications

(6 citation statements)

References 20 publications

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“…Zhang et al [40] found α-chains with a MW of 116 kDa of spiked skate skin gelatin (Amblyraja radiata) by alcalase pretreatment and controlled extraction. Furthermore, it is stated that the α chains are easily degraded in liquid solvents, so it is extremely important to strictly control the processing conditions to obtain the intact α-chains to suit a particular application [53].…”

Section: Discussionmentioning

confidence: 99%

“…The lower viscosity of gelatin is thought to be due to the presence of low MW peptide chains as a result of excessive collagen hydrolysis during the extraction stage. Low viscosity gelatin solutions typically produce short, brittle gels, while high-viscosity gelatin solutions produce tough, stretchable gels of high commercial value [53]. Viscosity is also related to pH.…”

Section: Discussionmentioning

confidence: 99%

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Characterization and functional properties of gelatin from goat bone through alcalase and neutrase enzymatic extraction

et al. 2021

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Background and Aim: Gelatin is a dissolved protein that results from partial extraction of collagen, commonly from pig and bovine skin. There was no study on gelatin production from Kacang goat bones through enzymatic extraction. This study aimed to evaluate the chemical, physical, and functional properties of gelatin from bones of Kacang goat using alcalase and neutrase enzymes. Materials and Methods: Male Kacang goat bones aged 6-12 months and two commercial enzymes (alcalase and neutrase) were used for this study. Descriptive analysis and completely randomized design (one-way analysis of variance) were used to analyze the chemical, physical, and functional properties of gelatin. Kacang goat bone was extracted with four concentrations of alcalase and neutrase enzymes, namely, 0 U/g (AG-0 and NG-0), 0.02 U/g (AG-1 and NG-1), 0.04 U/g (AG-2 and NG-2), and 0.06 U/g (AG-3 and NG-3) with five replications. Results: The highest yield of gelatin extraction with alcalase obtained on AG-3 was 9.78%, and that with neutrase on NG-3 was 6.35%. The moisture content of alcalase gelatin was 9.39-9.94%, and that of neutrase gelatin was 9.15-9.24%. The ash and fat content of gelatin with alcalase was lower than that without enzyme treatment with higher protein content. The lowest fat content was noted in AG-1 (0.50%), with protein that was not different for all enzyme concentrations (69.65-70.21%). Gelatin with neutrase had lower ash content than that without neutrase (1.61-1.90%), with the highest protein content in NG-3 (70.89%). The pH of gelatin with alcalase and neutrase was 6.19-6.92 lower than that without enzymes. Melting points, gel strength, and water holding capacity (WHC) of gelatin with the highest alcalase levels on AG-1 and AG-2 ranged from 28.33 to 28.47°C, 67.41 to 68.14 g bloom, and 324.00 to 334.67%, respectively, with viscosity that did not differ, while the highest foam expansion (FE) and foam stability (FS) were noted in AG-1, which were 71.67% and 52.67%, respectively. The highest oil holding capacity (OHC) was found in AG-2 (283%). FS and OHC of gelatins with the highest neutrase levels in NG-2 were 30.00% and 265.33%, respectively, while gel strength, viscosity, FE, and WHC of gelatins with the highest neutrase levels did not differ with those without enzymes at all enzyme concentrations. B chain was degraded in all gelatins, and high-intensity a-chains in gelatin with alcalase and peptide fraction were formed in gelatin with neutrase. Extraction with enzymes showed loss of the triple helix as demonstrated by Fourier transform infrared spectroscopy. Conclusion: Based on the obtained results, the Kacang goat bone was the potential raw source for gelatin production. Enzymatic extraction can increase the quality of gelatin, especially the alcalase (0.02-0.04 U/g bone) method. This can be used to achieve the preferable quality of gelatin with a higher yield.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Characterization and functional properties of gelatin from goat bone through alcalase and neutrase enzymatic extraction

et al. 2021

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“…CD spectra of the WPI solutions were measured using a J‐810 CD spectrometer (Jasco, Tokyo, Japan) according to the method of Chen et al . with minor modification.…”

Section: Methodsmentioning

confidence: 99%

Whey protein isolate with improved film properties through cross‐linking catalyzed by small laccase from Streptomyces coelicolor

et al. 2018

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“…Rectangles of 45 × 20 mm were cut from the film, and the mechanical properties of NC/MC films were measured by a texture analyzer (TMS-PRO, Food Technology Co., Sterling, VA, USA). The test speed was 1 mm/s, and the initial clamping distance was 30 mm [ 58 ]. Six parallels were measured for each sample, and the average value was taken.…”

Section: Methodsmentioning

confidence: 99%

Preparation and Characterization of κ-Carrageenan Modified with Maleic Anhydride and Its Application in Films

Zhou

Chen

et al. 2021

Marine Drugs

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In this work, the physicochemical properties of maleic anhydride (MAH)-modified κ-carrageenan (κCar) (MC) were characterized and compared with those of native κ-carrageenan (NC). The Fourier transform infrared spectrum of MC exhibited that κCar was successfully modified. Thermogravimetric analysis indicated that the thermal stability of MC was decreased. When the degree of substitution was 0.032, MC exhibited a low gel strength (759 g/cm2), gelling temperature (33.3 °C), and dehydration rate (60.3%). Given the excellent film-forming ability of κCar, MC films were then prepared and were found to have better mechanical and barrier properties (UV and water) than NC films. With regard to optical properties, MC films could completely absorb UV light in the range of 200–236 nm. The water contact angle of MC films was higher than that of NC films. Moreover, the elongation at break increased from 26.9% to 163%. These physicochemical property changes imply that MC can be employed in polysaccharide-based films.

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Effects of α1/α2 ratios and drying temperatures on the properties of gelatin films prepared from tilapia (Tilapia zillii) skins

Cited by 18 publications

References 20 publications

Characterization and functional properties of gelatin from goat bone through alcalase and neutrase enzymatic extraction

Characterization and functional properties of gelatin from goat bone through alcalase and neutrase enzymatic extraction

Whey protein isolate with improved film properties through cross‐linking catalyzed by small laccase from Streptomyces coelicolor

Preparation and Characterization of κ-Carrageenan Modified with Maleic Anhydride and Its Application in Films

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