ABSTRACT
This manuscript reviews the literature by giving a brief history of spices in general, how they played an important role in the past for the discovery of the world. The review paper gives the value of spices today then makes a difference between the group of spices on which it is focused (local, indigenous, less-known or under-utilised spices) and the conventional spices. The utilisation value of the spices by the populations is discussed as ethno-nutritional and ethnopharmacological uses, and scientific evidences from laboratory experimentations are reviewed to support some ethnopharmacological claims that are made on this plant materials, as well as their physicochemical composition. The review shows that less-known and under-utilised spices consumed in the food habits of population groups living in some Sub-Saharan African countries constitute an industrial opportunity for the development of modern food products, nutraceuticals and functional foods.
Subject(s)
Functional Food , Spices , Africa South of the Sahara , Feeding Behavior , Nutritive ValueABSTRACT
A protease from fresh leaves of Abrus precatorius was purified using two classical chromatography techniques: ion-exchange (DEAE-Sepharose) and Gel filtration (Sephadex G-75). The purified protease showed a molecular weight of â¼ 28 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The optimum pH and temperature for the purified protease was 8 and 40°C, respectively. The purified protease was stable throughout a wide temperature range from 10 to 80°C and pH from 2 to 12. Protease activity was inhibited in the presence of Co2+, Ni2+, Hg2+, and Zn2+ while its activity has increased in the presence of Ca2+ and Mg2+. The protease was highly specific to casein when compared to its specificity for gelatin, bovine serum albumin, hemoglobin, and defatted flour of Ricinodendron heudelotii. Its Vmax and Km determined using casein as a substrate were 94.34 U/mL and 349.07 µg/mL respectively. Inhibition studies showed that this purified protease was inhibited by both phenylmethane sulfonyl fluoride and aprotinin which are recognized as competitive inhibitors of serine proteases.