Guar gum is a novel agrochemical processed from endosperm of cluster bean. It is largely used in the form of guar gum powder as an additive in food, pharmaceuticals, paper, textile, explosive, oil well drilling and cosmetics industry. Industrial applications of guar gum are possible because of its ability to form hydrogen bonding with water molecule. Thus, it is chiefly used as thickener and stabilizer. It is also beneficial in the control of many health problems like diabetes, bowel movements, heart disease and colon cancer. This article focuses on production, processing, composition, properties, food applications and health benefits of guar gum.

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Two wheat varieties 'C 306' and 'WH 542' were milled to obtain flour fractions of different particle sizes. Various physicochemical parameters such as wet and dry gluten, falling number, solvent retention capacity (SRC), alkaline water retention capacity (AWRC) and damaged starch content of the flour fractions were analyzed. The damaged starch values ranged from 5.14% to 14.79% for different flour fractions and increased significantly with decrease in particle size. AWRC and SRC of the flour fractions also increased with decrease in particle size. AWRC(r00.659) showed positive correlation and cookie spread ratio (r0−0.826) was strongly negatively correlated with the damaged starch levels. Hardness of the cookies in term of compression force showed increasing trend as damaged starch of the flour fractions increased. Spread ratio of the cookies ranged from 6.72 to 10.12. Wheat flour of particle size greater than 150 μm produced cookies with best quality.

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Gliadins account for 40-50% of the total storage proteins of wheat and are classified into four subcategories, α-, β-, γ-, and ω-gliadins. They have also been classified as ω5-, ω1, 2-, α/β-, and γ-gliadins on the basis of their primary structure and molecular weight. Cysteine residues of gliadins mainly form intramolecular disulfide bonds, although α-gliadins with odd numbers of cysteine residues have also been reported. Gliadins are generally regarded to possess globular protein structure, though recent studies report that the α/β-gliadins have compact globular structures and γ- and ω-gliadins have extended rod-like structures. Newer techniques such as Mass Spectrometry with the development of matrix-assisted laser desorption/ionization (MALDI) in combination with time-of-flight mass spectrometry (TOFMS) have been employed to determine the molecular weight of purified ω- gliadins and to carry out the direct analysis of bread and durum wheat gliadins. Few gliadin alleles and components, such as Gli-B1b, Gli-B2c and Gli-A2b in bread wheat cultivars, γ-45 in pasta, γ-gliadins in cookies, lower gliadin content for chapatti and alteration in Gli 2 loci in tortillas have been reported to improve the product quality, respectively. Further studies are needed in order to elucidate the precise role of gliadin subgroups in dough strength and product quality.