|OTONI, CAIO - Universidade Federal De Vicosa|
|Avena Bustillos, Roberto|
Submitted to: Journal of Food Science
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/4/2012
Publication Date: 8/17/2012
Publication URL: http://dx.doi.org/10.1111/j.1750-3841.2012.02839.x
Citation: Otoni, C.G., Avena Bustillos, R.D., Chiou, B., Bilbao-Sainz, C., Bechtel, P.J., Mchugh, T.H. 2012. Ultraviolet-B radiation induced crosslinking improves physical properties of cold- and warm-water fish gelatin gels and films. Journal of Food Science. DOI:10.1111/j1750-3841.2012.02839.x.
Interpretive Summary: Cold- and warm-water fish gelatin exposed to ultraviolet-B radiation resulted in chemical crosslinking of gelatin chains displaying higher gel strengths, increase in viscosity and greater tensile strength. This technology has potential to improve physical properties of cold- and warm-water fish gelatin.
Technical Abstract: Cold- and warm-water fish gelatin granules were exposed to ultraviolet-B radiation for doses up to 29.7 J/cm2. Solutions and films were prepared from the granules. Gel electrophoresis and refractive index were used to examine changes in molecular weight of the samples. Also, the gel strength and rheological properties of the solutions as well as the tensile and water vapor barrier properties of the films were characterized. SDS-PAGE and refractive index results indicated crosslinking of gelatin chains after exposure to radiation. Interestingly, UV-B treated samples displayed higher gel strengths, with cold-water and warm-water fish gelatin having gel strength increases from 1.39 to 2.11 N and from 7.15 to 8.34 N, respectively. In addition, both gelatin samples exhibited an increase in viscosity for higher UV doses. For gelatin films, the cold-water fish gelatin samples made from irradiated granules showed greater tensile strength. In comparison, the warm-water gelatin films made from irradiated granules had lower tensile strength, but better water vapor barrier properties. This might be due to the UV induced crosslinking in warm-water gelatin that disrupted helical structures.