ReviewPulse proteins: Processing, characterization, functional properties and applications in food and feed
Introduction
Pulses constitute an important source of dietary protein for large segments of the world’s population particularly in those countries in which the consumption of animal protein is limited by nonavailability or is self-imposed because of religious or cultural habits (Liener, 1962). Pulses provide energy, dietary fibre, protein, minerals and vitamins required for human health. Recent research studies suggest that consumption of pulses may have potential health benefits including reduced risk of cardiovascular disease, cancer, diabetes, osteoporosis, hypertension, gastrointestinal disorders, adrenal disease and reduction of LDL cholesterol (Hu, 2003, Jacobs and Gallaher, 2004, Philanto and Korhonen, 2003, Tharanathan and Mahadevamma, 2003). Such studies have contributed significantly to a growing awareness of the usefulness of including pulses in the diet and a steady rise in interest in using pulses and ingredients derived from them in the development of novel food products, especially in North America. From the nutritional perspective, pulses are of particular interest because they contain high amounts of protein (18–32%). In addition to providing a source of essential amino acids and bioactive peptides, pulse proteins possess functional properties such as water holding, fat binding, foaming and gelation which could expand their potential use in the development of a wide variety of food products.
World protein requirements continue to be a global issue with heightened concerns about food security and protein malnutrition. In 1997 the Food and Agriculture Organization of the United Nations (FAO) estimated that over 800 million people in the developing world were undernourished (Blandford & Viatte, 1997). Today the figure is higher. The World Bank estimates there are currently 967 million malnourished people in the world (http://www.reliefweb.int/rw/rwb.nsf/db900SID/MCOI-7KGM87?OpenDocument). Moreover, an estimated 149.6 million children younger than 5 years are malnourished in terms of weight for age. In south central Asia and eastern Africa, about half the children have growth retardation due to protein–energy–malnutrition (PEM), a syndrome resulting from inadequate supplies of protein and other macro and micronutrients (http://emedicine.medscape.com/article/1104623-overview). Programs such as the World Food Program, the Millennium Hunger Task Force and the New Partnership for Africa’s Development (NEPAD)-Hunger Taskforce are undertaking School Feeding Programs aimed at providing adequate nutrition to children and malnourished communities globally. Most hungry and undernourished people live on a mono carbohydrate diet (e.g., maize or rice) and lack the required protein, fat, vitamin A, iodine, zinc and iron. The potential for blending pulses such as pea, chickpea, lentil and beans with other locally grown grains to meet some of the protein malnutrition problem worldwide is, therefore, of tremendous interest.
This paper will attempt to provide a review of the nutritional and functional properties and the current and potential applications of proteins from pulses. The paper will focus specifically on pea, chickpea, lentil and bean. A brief summary of the protein quality of pulse legumes is provided along with the processing technologies available for their fractionation and processing into protein flours, concentrates and isolates. The paper will also briefly address the possible use of pulses as an alternative to priority allergens such as soybean, gluten, dairy, eggs and nuts. As reports in the literature have shown that pulse proteins may themselves be allergenic, a short summary of the body of knowledge on the allergenic properties of pulse proteins is also presented.
Section snippets
Composition, molecular characteristics and nutritional quality of pulse proteins
The proximate composition of different pulses is presented in Table 1. Pea, chickpea, bean and lentil contain 17–30% protein with varying concentrations of essential amino acids (Sathe, Deshpande, & Salunkhe, 1984). The major proteins found in pulses are globulins and albumins. Albumins are water soluble and comprise enzymatic proteins, protease inhibitors, amylase inhibitors and lectins and have molecular masses (MM) ranging between 5000 and 80,000 Da. Globulins on the other hand are salt
Air classification
Air classification is a milling technique that allows the fractionation of grains/seeds into high starch and high protein flours. Milling of pulses results in flours having particles of two discrete sizes and densities. Air classification exploits this phenomenon to separate the light fine fraction (protein) from the heavy coarse fraction (starch). During air classification, whole or de-hulled seed is ground into very fine flour, and the flour is subsequently classified in a spiral air stream
Functional properties of pulse protein flours, concentrates and isolates
Functional properties are defined as the physical and chemical properties which affect the behaviour of proteins in food systems during processing, storage, preparation and consumption (Kinsella, 1982). Protein flours (<65% protein, d.w.b.), concentrates (>65% protein, d.w.b.), and isolates (>90% protein, d.w.b.) may be added to foods to increase the nutritional value and provide specific desired functional attributes. Properties of most interest in food processing include solubility, water
Food applications
Interest in the use of pulses and their constituents in food formulation is growing in many developed countries. Factors contributing to this include their reported nutritional and health benefits, changes in consumer preferences, increasing demand for variety/balance, change in demographics (age, racial diversity), rise in the incidence of food allergies and ongoing research on production and processing technologies. In many developing countries, however, pulses have had a long history of use
Allergenicity of pulse proteins
Food allergy is a growing problem around the world. The big eight priority allergens requiring labelling in the European Union (EU) and in countries such as Canada and the USA include soybean, peanut, tree nut, milk, eggs, gluten-containing cereals, fish, and shellfish. Additionally, labelling is required for sesame in Canada, Australia and the EU and for mustard and celery in the EU.
Pea, chickpea, bean and lentil are not classified as major allergens. Although proteins in these pulse crops
Feed applications
A significant proportion of pulse production goes into feed. Feeding trials have been conducted with rats to asses the nutritional quality of pulses for feed and food applications. Earlier studies using uncooked pulses demonstrated deleterious nutritional effects. Higher relative weights of gastrointestinal sections were determined in rats fed pulse seed meal diets compared to those fed lactalbumin (from milk) (Rubio et al., 1999). Cuadrado et al. (2002) reported that the inclusion of whole
Pest control
Proteinaceous cysteine proteinase inhibitor (CPI), an insecticidal protein found in pulses can be used to control the proteolytic activity of endogenous digestive cysteine proteinase in the mid-gut of some insects. CPI has been suggested to be an albumin-like protein and is readily soluble in water. Hines, Osuala, and Nielsen (1992) evaluated black bean, chickpea, common bean, cowpea, lentil, lima bean, mung bean, pea, soybean, lupin, and tepary bean seeds as potential sources of CPI. Soybean,
Conclusion
In the last few years, concern has grown regarding adequate supplies of food for the current (and growing) world population of nearly seven billion. The media has been replete with stories of food crises in many developing countries. At the same time we have witnessed a very unstable world economy, even in the developed world, which has put pressure on many industries including production agriculture and food processing. Protein malnutrition continues to be a major problem in many places in
Acknowledgements
Funding from Pulse Canada for the writing of this paper is gratefully acknowledged. We would also like to thank Dr. Sahul H. Rajamohamed for his assistance with the preparation of the manuscript.
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