Review
Pulse proteins: Processing, characterization, functional properties and applications in food and feed

https://doi.org/10.1016/j.foodres.2009.09.003Get rights and content

Abstract

Pulses (pea, chickpea, lentil, bean) are an important source of food proteins. They contain high amounts of lysine, leucine, aspartic acid, glutamic acid and arginine and provide well balanced essential amino acid profiles when consumed with cereals and other foods rich in sulphur-containing amino acids and tryptophan. The protein content of most pulse legumes fall within the range of 17–30% (d.w.b.). Apart from their nutritional properties, pulse proteins also possess functional properties that play an important role in food formulation and processing. Examples of such functional properties include solubility, water and fat binding capacity and foaming. Various research studies indicate that some functional properties of pulse proteins may be comparable to those of other frequently used proteins such as soy and whey. The functional properties of pulse proteins have been exploited in the preparation and development of products such as bakery products, soups, extruded products and ready to eat snacks. The growing body of research on the health benefits associated with the consumption of pulses has increased interest in developing innovative technologies to expand the use of pulses in food products. At the same time, there are growing global food security challenges and protein malnutrition continues to be a problem in many countries around the world. Pulses, especially when blended with cereal proteins, may offer a promising alternative source for nutritional and functional proteins. This review provides an overview of the characteristics of pulse proteins, current and emerging techniques for their fractionation, their major functional properties and opportunities for their use in various applications.

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.

References (171)

  • R.Y. Khattab et al.

    Nutritional quality of legume seeds as affected by some physical treatments, part 1: Protein quality evaluation

    LWT – Food Science and Technology

    (2009)
  • I.E. Liener

    Toxic factors in edible legumes and their elimination

    American Journal of Clinical Nutrition

    (1962)
  • G. Lopez-Torrejon et al.

    Len c 1, a major allergen and vicilin from lentil seeds: Protein isolation and cDNA cloning

    Journal of Allergy and Clinical Immunology

    (2003)
  • U.M.L. Marquez et al.

    Chemically determined total and available methionine in beans (Phaseolus vulgaris L.) and isolated protein fractions

    Food Chemistry

    (1996)
  • R.C. McLeester et al.

    Comparison of globulin proteins from Phaseolus vulgaris with those from Vicia faba

    Phytochemistry

    (1973)
  • C. Melito et al.

    Cell walls limit in vitro protein digestibility in processed legume seeds

    Food Chemistry

    (1995)
  • G.M.A. Abd El-Moniem

    Sensory evaluation and in vitro protein digestibility of mung bean as affected by cooking time

    Journal of the Science of Food and Agriculture

    (1999)
  • E.M. Abdel-Aal et al.

    Some legume proteins as bread fortifier and meat extender

    Alexandria Journal of Agricultural Research

    (1987)
  • Y. Abebe et al.

    Nutritive value and sensory acceptability of corn and kocho-based foods supplemented with legumes for infant feeding in southern Ethiopia

    African Journal of Food, Agriculture, Nutrition and Development

    (2006)
  • T.M. Abu Bakr et al.

    Upgrading and utilization of by products of slaughter houses. I. Fresh and canned sausage incorporating legume extenders in their meat emulsions

    Alexandria Science Exchange

    (1986)
  • J.M. Aguilera et al.

    Air classification and extrusion of navy bean fractions

    Journal of Food Science

    (1984)
  • I. Alli et al.

    Identification and characterization of phaseolin polypeptides in a crystalline protein isolated from white kidney beans (Phaseolus vulgaris)

    Journal of Agricultural and Food Chemistry

    (1993)
  • K. Anjou et al.

    Nutritional assessment of rapeseed protein concentrate in combination with soya proteins as a meat extender

    Nutrition Reports International

    (1978)
  • Y. Bahnassey et al.

    Fortification of spaghetti with edible legumes. I. Physicochemical, antinutritional, amino acid, and mineral composition

    Cereal Chemistry

    (1986)
  • R.S. Bhatty

    Protein subunits and amino acid composition of wild lentil

    Phytochemistry

    (1982)
  • S. Bishnoi et al.

    Protein digestibility of vegetables and field peas (Pisum sativum) Varietal differences and effect of domestic processing and cooking methods

    Plant Foods for Human Nutrition

    (1994)
  • D. Blandford et al.

    Ensuring global food security

    OECD Observer

    (1997)
  • Bodnaryk, R., Fields, P., Xie, Y., & Fulcher, K. (1999). Insecticidal factors from field pea. United States Patent...
  • E.E. Braudo et al.

    Plant protein interactions with polysaccharides and their influence on legume protein functionality

    Nahrung/Food

    (2001)
  • D. Bulter

    The composition and nutritional value of legumes in relationship to crop improvement by breeding

  • R. Cai et al.

    Preparation of bean curds from protein fractions of six legumes

    Journal of Agricultural and Food Chemistry

    (2001)
  • M. Candela et al.

    Cooking and warm-holding: Effect on general composition and amino acids of kidney beans (Phaseolus vulgaris), chickpeas (Cicer arietimum), and lentils (Lens culinaris)

    Journal of Agricultural and Food Chemistry

    (1997)
  • M. Carbanaro et al.

    Solubility–digestibility relationship of legume proteins

    Journal of Agricultural and Food Chemistry

    (1997)
  • S. Celik et al.

    Effect of irradiation on protein electrophoretic properties, water absorption and, cooking quality of dry bean and chickpea

    Food Science and Technology Research

    (2004)
  • P. Chakraborty et al.

    Ultracentrifugation of salt soluble proteins in ten legume species

    Journal of the Science of Food and Agriculture

    (1979)
  • U. Chitra et al.

    Phytic acid, in vitro protein digestibility, dietary fiber, and minerals of pulses as influenced by processing methods

    Plant Foods for Human Nutrition

    (1996)
  • U. Chitra et al.

    Variability in phytic acid content and protein digestibility of grain legumes

    Plant Foods for Human Nutrition

    (1995)
  • A. Clemente et al.

    Effect of cooking on protein quality of chickpea (Cicer arietinrum) seeds

    Food Chemistry

    (1998)
  • C.W. Coffman et al.

    Functional properties and amino acid content of a protein isolate from mung bean flour

    Journal of Food Technology

    (1977)
  • R.R. Croy et al.

    The purification and characterization of a third storage protein (convicilin) from the seeds of pea (Pisum sativum L.)

    Biochemical Journal

    (1980)
  • Z.S. Cserhalmi et al.

    Emulsifying properties, surface hydrophobicity and thermal denaturation of pea protein fractions

    Acta Alimentaria

    (1998)
  • C. Cuadrado et al.

    Nutritional utilization by the rat of diets based on lentil (Lens culinaris) seed meal or its fractions

    Journal of Agricultural and Food Chemistry

    (2002)
  • M.A. da Silva et al.

    Protein fractions and major globulin from chickpea (Cicer arietinum L.)

    Alimentos e Nutrição

    (2001)
  • C. Dagorn-Scaviner et al.

    Emulsifying properties of pea globulins as related to their adsorption behaviours

    Journal of Food Science

    (1987)
  • D.D. Dalgetty et al.

    Fortification of bread with hulls and cotyledon fibers isolated from peas, lentils and chickpeas

    Cereal Chemistry

    (2006)
  • J. Davidson

    Attempts to eliminate from field beans the anti nutritive factor which reduces egg production

    British Poultry Science

    (1980)
  • K. Dhawan et al.

    Seed protein fractions and amino acid composition in gram (Cicer arietinum)

    Plant Foods for Human Nutrition

    (1991)
  • W. Duszkiewicz-Reinhard et al.

    Shelf life stability of spaghetti fortified with legume flours and protein concentrates

    Cereal Chemistry

    (1988)
  • T.A. El-Adawy et al.

    Nutritional potential and functional properties of germinated mung bean, pea and lentil seeds

    Plant Foods for Human Nutrition

    (2003)
  • K. Elkowicz et al.

    Antinutritive factors in eleven legumes and their air-classified protein and starch fractions

    Journal of Food Science

    (1982)
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