Improved thermal-stability and mechanical properties of type I collagen by crosslinking with casein, keratin and soy protein isolate using transglutaminase.
The inferior thermal- stability of collagen hinders its extensive application in food industry, including edible packaging. To improve the thermal- stability and mechanical properties of collagen, we attempted to crosslink collagen with some proteins possessing excellent thermal stability (i. e., casein, keratin and soy protein isolate (SPI)). Observed from the SDS- PAGE and particle size distribution, some complexes with higher molecule weight and relative bigger size particle occurred in the protein mixture, especially after TGase crosslinking. Importantly, the crosslinking greatly improved the thermal- stable property of protein complex, especially that of the collagen- casein complex judged from differential scanning calorimetric (DSC). Moreover, the crosslinking enhanced the mechanical properties of the combined films in terms of tensile strength (TS) and elongation at break (EAB). Also, some obvious differences in morphology of proteins before and after TGase crosslinking were observed by scanning electron microscopy (SEM). These impacts of TGase crosslinking with heat- resistant proteins on collagen features were associated with the conformational changes of the protein complex analyzed by Fourier transform infrared spectroscopy (FTIR). In conclusion, TGase crosslinking with higher thermally stable proteins could be an effective method to contribute to collagen' application in food packaging field.
Key Laboratory of Food Nutrition and Safety, Ministry of Education, College of Food Engineering and Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China.
Xiaomeng
X
Wu
Key Laboratory of Food Nutrition and Safety, Ministry of Education, College of Food Engineering and Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China.
Yaowei
Y
Liu
Key Laboratory of Food Nutrition and Safety, Ministry of Education, College of Food Engineering and Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China. Electronic address: laj@tust.edu.cn.
Anjun
A
Liu
Key Laboratory of Food Nutrition and Safety, Ministry of Education, College of Food Engineering and Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China; Tianjin Food Safety & Low Carbon Manufacturing Collaborative Innovation Center, 300457, Tianjin China. Electronic address: wangwenhang@tust.edu.cn.
Wenhang
W
Wang
D002364:Caseins / Q000737:chemistry*; D024042:Collagen Type I / Q000737:chemistry*; D007633:Keratins / Q000737:chemistry*; D010316:Particle Size; D055550:Protein Stability; D030262:Soybean Proteins / Q000737:chemistry*; D013696:Temperature; D013718:Tensile Strength; D011503:Transglutaminases / Q000378:metabolism*
D002364:Caseins; D024042:Collagen Type I; D030262:Soybean Proteins; D007633:Keratins; D011503:Transglutaminases
Collagen; Crosslinking; Transglutaminase