Effects of preheat treatment and polyphenol grafting on the structural, emulsifying and rheological properties of protein isolate from Cinnamomum camphora seed kernel.

In this study, protein isolate (PI) and purified polyphenol extract (PPE) were prepared from Cinnamomum camphora seed kernel (CCSK). The effects of preheat treatment (50-90 °C) combined with polyphenol grafting (5 % PPE, w/w) on the structural, emulsifying and rheological properties of PI were investigated. Results demonstrated the preheat treatments at 80 and 90 °C significantly increased the extent of protein aggregation of PI. Fluorescence spectra and thermal behavior analysis revealed that preheat-treated PI exhibited more compact structure and higher thermal stability. Moreover, the emulsifying stability and apparent viscosity of PI were enhanced after preheat treatments at 50, 60 and 70 °C. After modification by PPE, the secondary structural changes of preheat-treated PI were confirmed by FTIR. PPE modification improved the thermal stability and antioxidant activities of preheat-treated PI. These results provide a novel way to combine the advantages of preheat treatment and polyphenol grafting in developing a novel protein ingredient.

Expression and characterization of a novel lipase from Bacillus licheniformis NCU CS-5 for application in enhancing fatty acids flavor release for low-fat cheeses.

A novel lipase from Bacillus licheniformis NCU CS-5 was expressed in different Escherichia coli cells. The recombinant enzyme achieved a high activity (161.74 U/mL) with protein concentration of 0.27 mg/mL under optimal conditions at the large-scale expression of 12 h. The recombinant lipase showed optimal activity at 40 ℃ and pH 10.0, and maintained more than 80% relative activity after 96 h of incubation at pH 9.0-10.0. This typical alkaline lipase was activated under medium temperature conditions (30 and 45 ℃ for 96 h). The lipase exhibited a degree of adaptability in various organic solvents and metal ions, and showed high specificity towards triglycerides with short and medium chain fatty acids. Among different substrates, the lipase showed the strongest binding affinity towards pNPP (Km = 0.674 mM, Vmax = 950.196 µM/min). In the experiments of its application in enhancing fatty acids flavor release for low-fat cheeses, the lipase was found to hydrolyze cheeses and mainly increase the contents of butyric acid, hexanoic acid, caprylic acid and decanoic acid. The results from NMR and GC provided the possibility of enhancing fatty acids flavor released from low-fat cheeses by the lipolysis method.