Bioprocess Division, School of Industrial Technology, Universiti Sains Malaysia, 11800 USM, Penang, Malaysia; Centre for Advanced Analytical Toxicology Services, Universiti Sains Malaysia, 11800 USM, Penang, Malaysia.
Centre for Advanced Analytical Toxicology Services, Universiti Sains Malaysia, 11800 USM, Penang, Malaysia.
Food Chem. 2014;152:447-55. doi: 10.1016/j.foodchem.2013.12.008. Epub 2013 Dec 10.
Optimisation of protein extraction yield from pinto bean was investigated using response surface methodology. The maximum protein yield of 54.8 mg/g was obtained with the optimal conditions of: temperature=25 °C, time=1 h and buffer-to-sample ratio=20 ml/g. PBPI was found to obtain high amount of essential amino acids such as leucine, lysine, and phenylalanine compared to SPI. The predominant proteins of PBPI were vicilin and phytohemagglutinins whereas the predominant proteins of SPI were glycinin and conglycinins. Significantly higher emulsifying capacity was found in PBPI (84.8%) compared to SPI (61.9%). Different isoelectric points were found in both PBPI (4.0-5.5) and SPI (4.0-5.0). Also, it was found that PBPI obtained a much higher denaturation temperature of 110.2 °C compared to SPI (92.5 °C). Other properties such as structural information, gelling capacity, water- and oil-holding capacities, emulsion stability as well as digestibility were also reported.
利用响应面法优化了利马豆中蛋白质的提取率。在最佳条件下（温度=25°C，时间=1 小时，缓冲液与样品的比例=20 ml/g），蛋白质的最大提取率为 54.8mg/g。与 SPI 相比，PBPI 中发现含有大量的必需氨基酸，如亮氨酸、赖氨酸和苯丙氨酸。PBPI 的主要蛋白质为伴大豆球蛋白和植物血球凝集素，而 SPI 的主要蛋白质为大豆球蛋白和 conglycinin。与 SPI（61.9%）相比，PBPI 的乳化能力显著更高（84.8%）。在 PBPI（4.0-5.5）和 SPI（4.0-5.0）中均发现了不同的等电点。此外，还发现 PBPI 的变性温度（110.2°C）明显高于 SPI（92.5°C）。还报告了其他性质，如结构信息、胶凝能力、水和油保持能力、乳液稳定性以及消化率。
