DE MOT, R., and H. VERACHTERT. 1986. Secretion of a-amylase and multiple forms of glucoamylase by the yeast Trichosporon pullulans. Can. J . Microbiol. 32: 47-51. Trichosporon pullulans IGC 3488 produced extracellular a-amylase and glucoamylase activities when grown in batches in a medium containing corn steep liquor and soluble starch or corn starch. a-Amylase, unlike glucoamylase activity, was secreted biphasically. For both amylases the maximum concentration was found in stationary phase cultures. The amylolytic enzymes, previously concentrated by ammonium sulfate precipitation, were separated into a glucoamylase fraction and an a-amylase fraction by Ultrogel AcA 54 gel filtration. Pullulanase activity was located in the glucoamylase fraction, whereas cyclodextrinase activity was restricted to the a-amylase fraction. Isoamylase and a-glucosidase were not detected. Electrophoretic analysis showed that a-amylase activity was due to a single protein. Glucoamylase, however, occurred in multiple forms. The four glucoamylases and the a-amylase were glycoproteins.DE MOT, R., et H. VERACHTERT. 1986. Secretion of a-amylase and multiple forms of glucoamylase by the yeast Trichosporon pullulans. Can. J. Microbiol. 32: 47-51. La levure Trichosporon pullulans IGC 3488, croissant en vrac dans un milieu contenant une solution de mais trempk, additionnke d'amidon soluble ou de fCcule de mais, a produit des activitiCs d'a-amylase et de glucoamylase extracellulaires. L'activitk de I'a-amylase, contrairement ti celle de la glucoamylase, fut sCcrktCe de f a~o n biphasique. La concentration maximale pour les deux types d'amylase a Ct C dCcelte dans les cultures en phase stationnaire. Les deux enzymes amylolytiques, prkalablement concentrkes par prkcipitation en prksence de sulfate d'amrnonium, ont Ct C skparkes par filtration sur Ultrogel AcA 54 en fraction glucoamylase et fraction a-amylase. Une activitC pullulanase a Ct C dCcelCe dans la fraction glucoamylase alors qu'une activitk cyclodextrinase fut strictement relike a la fraction a-amylase. I1 n'y a pas eu de dCtection d'isoamylase et d'a-glucosidase. L'activitk a-amylase mise en Cvidence par klectrophor&se s'est rCvClCe like 3 une seule protkine. Toutefois, la glycoamylase a prCsentC des formes multiples. Les quatre glucoamylases ainsi que I'a-amylase se sont avkr6es des glycoprotkines.[Traduit par la journal]