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Sample Preparation for Mass-spectrometry-based Proteomics Analysis of Ocular Microvessels
Published on: February 22, 2019
A comparative study of physicochemical characteristics and functionalities of pinto bean protein isolate (PBPI)
Ee-San Tan1, Ngoh Ying-Yuan2, Chee-Yuen Gan2
1Bioprocess 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.
Abstract:
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.

