The first gene (${alpha}$-gal1) encoding an extracellular ${alpha}$-Dgalactosidase from the thermophilic fungus Talaromyces emersonii was cloned and characterized. The ${alpha}$-gal1 gene consisted of an open reading frame of 1,792 base pairs interrupted by six introns that encoded a mature protein of 452 amino acids, including a 24 amino acid secretory signal sequence. The translated protein had highest identity with other fungal ${alpha}$-galactosidases belonging to glycosyl hydrolase family 27. The ${alpha}$-gal1 gene was overexpressed as a secretory protein with an N-terminal histidine tag in the methylotrophic yeast Pichia pastoris. Recombinant ${alpha}$-Gal1 was secreted into the culture medium as a monomeric glycoprotein with a maximal yield of 10.75 mg/l and purified to homogeneity using Hisbinding nickel-agarose affinity chromatography. The purified enzyme was maximally active at $70^{circ}C$, pH 4.5, and lost no activity over 10 days at $50^{circ}C$. ${alpha}$-Gal1 followed Michaelis-Menten kinetics ($V_{max};of;240.3{mu}M/min/mg,;K_m;of;0.294 mM$) and was inhibited competitively by galactose ($K_m{^{obs}}$ of 0.57 mM, $K_i$ of 2.77 mM). The recombinant T. emersonii ${alpha}$-galactosidase displayed broad substrate preference, being active on both oligo- and polymeric substrates, yet had strict specificity for the ${alpha}$-galactosidic linkage. Owing to its substrate preference and noteworthy stability, ${alpha}$-Gal1 is of particular interest for possible biotechnological applications involving the processing of plant materials.