Modeling of enzymatic activity of free β-glucosidase from palm weevil, Rhynchophorus palmarum Linn. (Coleoptera: Curculionidae) larvae: Effects of pH and temperature.

Palm weevil, Rhynchophorus palmarum L., is an important pest of palm trees (Elaeis guineensis) around the tropical regions. Characterization of their digestive enzymes could be an important stage to develop appropriate pest control strategies.

Effect of boiling time on chemical composition and physico-functional properties of flours from taro (Colocasia esculenta cv fouê) corm grown in Côte d'Ivoire.

Taro (Colocasia esculenta cv fouê) corm was subjected to different boiling times and the changes in chemical composition and physico-functional properties were investigated using standard method. The change in boiling time led to a significant (P < 0.05) reduction in the moisture, reducing sugars, total sugars, crude fat, crude fibre, total phenolic compound contents and iodine affinity of starch, whereas the total carbohydrate content, water absorption capacity, water solubility index, paste clarity and foam capacity increased significantly (p < 0.

Purification and biochemical characterization of a specific beta-glucosidase from the digestive fluid of larvae of the palm weevil, Rhynchophorus palmarum.

A beta-glucosidase was purified from the digestive fluid of the palm weevil Rhynchophorus palmarum L. (Coleoptera: Curculionidae) by chromatography on anion-exchange, gel filtration, and hydrophobic interaction columns. The preparation was shown to be homogeneous on polyacrylamide gels, beta-glucosidase is a monomeric protein with a molecular weight of 58 kDa based on its mobility in SDS-PAGE and 60 kDa based on gel filtration.

Purification, kinetic properties and physicochemical characterization of a novel acid phosphatase (AP) from germinating peanut (Arachis hypogaea) seed.

Acid phosphatase activity was detected in peanut (Arachis hypogaea) cotyledons during germination. Four (4) to six (6) days of germination was the meantime corresponding to maximum hydrolytic activity of this enzyme. The understanding of the role of acid phosphatase activity during germination led to purify this enzyme by successive chromatography separations on DEAE-Sepharose CL-6B, Sephacryl S-100 HR and Phenyl-Sepharose HP to apparent homogeneity from germinated peanut cotyledon five days old.