Location: Bioproducts Research
Title: Mechanical and thermal behavior of canola protein isolate films as improved by cellulose nanocrystalsAuthor
OSORIO-RUIZ, ALEX - Instituto Politécnico Nacional, Centro De Desarrollo De Productos Bioticos (CEPROBI) | |
Avena-Bustillos, Roberto | |
Chiou, Bor-Sen | |
MARTINEZ-AYALA, ALMA-LETICIA - Instituto Politécnico Nacional, Centro De Desarrollo De Productos Bioticos (CEPROBI) |
Submitted to: ACS Omega
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 10/25/2019 Publication Date: 11/8/2019 Citation: Osorio-Ruiz, A., Avena Bustillos, R.D., Chiou, B., Martinez-Ayala, A. 2019. Mechanical and thermal behavior of canola protein isolate films as improved by cellulose nanocrystals. ACS Omega. 4(21):19172-19176. https://doi.org/10.1021/acsomega.9b02460. DOI: https://doi.org/10.1021/acsomega.9b02460 Interpretive Summary: We produced canola protein films containing cellulose nanocrystals with improved thermal and mechanical properties. The canola protein is a by-product of canola oil pressing industry. The films containing nanocrystals had higher thermal stability than the films without nanocrystals, indicating it can be used at higher temperatures. The films with the nanocrystals were also stronger. These improved properties indicated the films can be used in food packaging applications. Since canola protein is derived from a renewable resource and is biodegradable, these films can be an environmentally friendly alternative to petroleum derived ones. Technical Abstract: The effects of cellulose nanocrystals (12, 24 and 36% w/w) on microstructure, mechanical and thermal properties of canola protein isolate (CPI) films was evaluated. The incorporation of cellulose nanocrystals (CNC) led to more homogeneous films. The addition of CNC also improved thermal stability of the films, since higher temperatures were required for their thermal decomposition. In addition, CNC addition resulted in an increase in tensile strength and a decrease in elongation at break values due to the formation of a three-dimensional network structure that was stabilized by strong interactions between the OH groups in proteins, glycerol and CNC. |