Possibilities of valorization of spp leaves in modern gastronomy: Production and characterization of new vegetable tarts and salads.

spp is a green creeper plant abundantly found in the Central African forests. Their leaves are eaten as vegetable by inhabitants. In order to valorize this vegetable in modern gastronomy, a survey was carried out in three towns of Cameroon to evaluate its importance in the feeding habits.

Inclusion of partly purified protease from Linn in Ca-alginate gel beads.

is an edible endemic plant in Cameroon. In the northern regions of Cameroon, the leaves of this plant are used as traditional medications, for the liquefaction of wort obtained after mashing of sorghum or millets for processing the local fermented beer called and to sweeten gruels made from red millet. has also being explored as a potential source of proteolytic enzymes.

Indigenous spices consumed in the food habits of the populations living in some countries of Sub-Saharan Africa: Utilisation value, nutritional and health potentials for the development of functional foods and drugs: A review.

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.

Extraction, purification, and biochemical characterization of serine protease from leaves of Abrus precatorius.

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 ∼ 28 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The optimum pH and temperature for the purified protease was 8 and 40°C, respectively.