Research has proved a relationship between functional components of food, health and well-being. Thus, functional components of food can be effectively applied in the treatment and prevention of diseases. They act simultaneously at different or identical target sites with the potential to impart physiological benefits and promotion of wellbeing including reducing the risk of cancer, cardiovascular disease, osteoporosis, inflammation, type II diabetes, and other chronic degenerative diseases, lowering of blood cholesterol, neutralization of reactive oxygen species and charged radicals, anticarcinogenic effect, low-glycaemic response, etc. Previously, it was thought that functional ingredients such as non-starchy carbohydrates including soluble and insoluble dietary fibres, fucoidan; antioxidants including polyphenols, carotenoids, tocopherols, tocotrienols, phytosterols, isoflavones, organosulphur compounds; plant sterols and soy phytoestrogens occur only in plant foods (whole grains, fruits, and vegetables) as phytochemicals. However, probiotics, prebiotics, conjugated linolenic acid, long-chain omega-3, -6 and -9-polyunsaturated fatty acids, and bioactive peptides have proved that functional components are equally available in animal products such as milk, fermented milk products and cold-water fish. The way a food is processed affects its functional components. Many processing techniques have been found to lower the concentration of functional components in food. Conversely, other techniques were found to increase them. Hence, in a time when the role of a healthy diet in preventing non-communicable diseases is well accepted, the borderline between food and medicine is becoming very thin.

No abstract

Initially, large‐scale lager beer brewing with sorghum malts proved highly intractable due to a number of biochemical problems including: high malting losses estimated at 10–30% as against 8–10% for barley; high gelatinisation temperatures which limited starch solubilisation/ hydrolysis by the amylolytic enzymes during mashing; low extract yield/low diastatic power (DP) due to inadequate hydrolytic enzyme activities especially β‐amylase; low free α‐amino nitrogen (FAN) due to inadequate proteolysis limiting yeast growth during fermentation; high wort viscosities/beer filtration problems due to low endo‐β‐1,3; 1–4‐glucanase activities on the endosperm cell walls causing the release of some β‐glucans. Strident research efforts using improved Nigerian sorghum malt varieties (SK5912, KSV8 and ICSV400) have reported some encouraging results. The knowledge of the biochemical integrity of the endo‐β‐glucanases of the sorghum malt is helping to elucidate their mode of activity in the depolymerisation of the β‐glucans. This is bound to ensure process efficiency in sorghum beer brewing, reduce beer production costs and ultimately, produce a Pilsner‐type of lager beer with 100% sorghum malt.

No abstract

A protease from sorghum malt variety KSV8-11 was purified by a combination of dialysis against 4 M sucrose, ion-exchange chromatography on Q-Sepharose (Fast flow), gel filtration chromatography on Sephadex G-100 and hydrophobic interaction chromatography on Phenyl Sepharose CL-4B. The enzyme was purified 5-fold to give a 14.1% yield relative to the total activity in the crude extract and a final specific activity of 1348.9 U mg -1 protein. SDS-PAGE revealed a single migrating protein band corresponding to a relative molecular mass of 16 KDa. Using casein as substrate, the purified protease had optimal activity at 50°C and maximal temperature stability between 30°C and 40°C but retained over 64% of its original activity after incubation at 60°C for 30 min. The pH optimum was 5.0 with maximum stability at pH 6.0 but 60% of the activity remained after 24 h between pH 5.0 and 8.0. The protease was inhibited by Ag + , Ca 2+ , Co 2+ , Fe 2+ , Mg 2+ , iodoacetic acid (IAA) and p-chloromercuribenzoate (p-CMB), stimulated by Cu 2+ , Sr 2+ , phenylmethylsulfonyl-fluoride (PMSF) and 2-mercaptoethanol (2-ME) while Mn 2+ and ethylenediaminetetraacetic acid (EDTA) had no effect. The purified enzyme had a K m of 18 mg · mL -1 and a V max of 11.1 µmol · mL -1 · min -1 with casein as substrate.