Effect of high pressure treatment on functional, rheological and structural properties of kidney bean protein isolate
Introduction
Among legumes, kidney bean (Phaseolus vulgaris L.) is one the important produce, and is consumed as a cheap protein source in many developing countries. Kidney beans contain 20–30 g/100 g protein on a dry weight basis with a balanced amino acid composition; nonetheless, it is low in sulfur-containing amino acids, namely, methionine and tryptophan (Sathe, Iyer, & Salunkhe, 1981). Epidemiologic studies have revealed that consumption of kidney beans has several health benefits including the reduction of the risk of cardiovascular diseases, type II diabetes, obesity, and several/specific types of cancer (Dueñas, Martínez-Villaluenga, Limón, Peñas, & Frias, 2015).
Phaseolin or vicilin or 7-8S globulins, is the major storage protein from the kidney bean, and it constitutes about 75 and 82 g/100 g of the total seed proteins (Yin, Tang, Wen, Yang, & Yuan, 2009). It is an oligomeric protein, comprising of three polypeptide subunits namely α-, β-, and γ-phaseolin, and the molecular weight distribution ranged between 43 and 53 kDa (Romero, Sun, McLeester, Bliss, & Hall, 1975). Interestingly, vicilin present in kidney beans shows the unique structural peculiarity by low susceptibility to trypsin digestion and greater subunit homogeneity, than other vicilin components (Jivotovskaya et al., 1996, Yin et al., 2008). Because of the unique peculiarity of vicilin, the kidney bean protein isolate (KBPI) exhibits a good gelation and emulsifying ability compared to other bean isolates (Kimura et al., 2008, Tang, 2008). Additionally, KBPI have potential to be applied as an excellent food functional ingredient in various food formulations, in particular, baking, meat, and extruded products.
High-pressure (HP) treatment – a novel processing technology is commonly employed for the protein gelation purpose as an alternative of heat processing. Application of HP denatures proteins, and forms gel. Influence of HP treatment on functionality and in vitro trypsin digestibility of KBPI has been reported (Yin et al., 2008). Soy protein forms gel at and above 300 MPa by rupturing noncovalent interactions within protein molecule, and it was found that the produced gel is relatively softer than the thermally treated gel (Ahmed et al., 2007a, Dumoulin et al., 1998). The gel rigidity during pressure-assisted gelation, is mostly, measured through the evolution of the complex viscosity or by measuring the elastic modulus, G′. However, HP-induced changes in rheological and structural properties of KBPI has not been investigated so far.
The objective of this work was to study the effect of high-pressure treatment (200, 400, and 600 MPa) on the physicochemical, functional, thermal, rheological, and structural properties of freeze-dried kidney bean protein isolate.
Section snippets
Materials
Red kidney beans (Phaseolus vulgaris), cultivated in India (Cv. VL Rajma 125) were procured locally. The beans were ground using a laboratory mill (Quadrumat Junior, Brabender, Germany) followed by passing through a 297-μm sieve to obtain uniform particle size. The screened flour samples were packed in air-tight plastic containers, and stored until further use.
Preparation of kidney bean protein isolates
The kidney bean protein isolate (KBPI) was prepared following the method described by Fan and Sosulski (1974), with a minor
Physicochemical properties
The protein content of the KBPI was 80.82 g/100 g, and the value is comparable with the literature values (77–84 g/100 g) (Rui et al., 2011, Wani et al., 2015). The moisture content of the freeze dried isolate was less than 4 g/100 g by weight. The observed ash content (4.1 ± 0.3 g/100 g) is in the range of the reported values for different varieties of kidney beans (Rui et al., 2011, Wani et al., 2015). A difference in those values could be attributed to the type of kidney beans used and the
Conclusion
HP-treatment of KBPI influenced the extent of protein denaturation resulting change in functional properties. The WHC, EAI increased, and foaming properties decreased with increasing the pressure level from 200 to 600 MPa. The thermal denaturation temperature (Td) of KBPI dispersions was complimented by both rheometry and DSC measurement. A reduction and agglomeration of particle sizes were observed, the observation was pressure dependent indeed. A change in the protein secondary structure is
Acknowledgement
The authors would like to thank the Kuwait Institute for Scientific Research for funding the project (FB 121K).
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