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The article reports on the molecular cloning of cDNA for trehalase from the European honeybee, Apis mellifera and its heterologous expression in Pichia pastoris. The mature enzyme comprised of 591 amino acids. The six peptide sequences analyzed were found in the deduced amino acid sequence, which exhibited high identity with trehalases which belong to the glycoside hydrolase family.

The article discusses a study which describes the molecular cloning of chromosomal deoxyribonucleic acids (cDNA) encoding three alpha-glucosidases including HBGases I, II and III from European honeybees, Apis mellifera, which are expressed in Pichia pastoris. It is showed that the gene of HBGase I composed of eight exons and seven introns. The HBGase II was not divided by intron and the gene of HBGase III was confirmed to be made up of nine exons and eight introns.

The article discusses the purification and characterization of a-Glucosidase (JHGase I) from a Japanese subspecies of eastern honeybee (Apis cerena japonica). The JHGase I was isolated from component 1 to undergo further purification using CM-Tojopearl 650M and Sepharel S-100. JHGase I showed unusual kinetic features: the negative cooperative behavior on the intrinsic reaction and positive cooperative on turanose. In addition, JHGase I is a member of a-amylase family enzymes.

Focuses on localization of α-glucosidases I,II and III in organs of European honeybees, Apis mellifera L. and the origin of α-glucosidase in honey. Preparation of specific antisera against the α-glucosidases to examine the localization of α-glucosidases in the organs of honeybees; Confirmation for the fist time that α-glucosidase I was present in ventriculus and haemolymph; Suggestion that honey may be finally made up through the process whereby sucrose in nectar is hydrolyzed by secreted α-glucosidase III.