In all of these environments, the most ubiquitous species are Rhodotorula laryngis and Cr. victoriae.

On the other hand, C. sake, D. fristingensis, G. antarctica and Sp. salmonicolor have been isolated only in the Southern Cone (South American glaciers and Antarctica). This work reports CHIR-99021 in vivo for the first time the isolation of Cryptococcus gastricus, Cryptococcus gilvescens, D. fristingensis and Leucosporidiella creatinivora from an Antarctic region. Also isolated was W. anomalus, which is not generally found in cold regions. During molecular analysis of the yeasts, most isolates assigned to the same species possessed identical D1/D2 and ITS sequences. Thus, combining these rDNA regions is a useful technique for rapid identification and typing of yeasts, as others have suggested [14, 20, 21]. However, the isolates identified as Leuconeurospora sp. were 0.7% and 0.9% different in their D1/D2 (578 bp) and ITS (534 bp) sequences, respectively.

Similarly, the isolates identified as D. fristingensis exhibited identical D1/D2 (456 bp) sequences, but their ITS (479 bp) sequences were markedly different (4.4%), and their overlap was punctuated with several gaps. Furthermore, given the physiological differences between isolates that are identical or similar at molecular level, strongly support that the definitions of yeast species must be supplemented by classical characterizations. Most yeast isolates showed lipase activity, consistent with a previous report in which all of the filamentous fungi from Erlotinib Antarctica displayed this activity [22]. Among the Opaganib concentration “cold loving” yeasts, lipase activity

has been described in Pseudozyma antarctica[23], Leucosporidium antarcticum[24] and in species of Cryptococcus and Rhodotorula[25]. Unlike this last-mentioned study, we detected lipase activity in R. laryngis also. Lipase activity has also been described in W. anomalus from tropical environments [26]. The least common extracellular activity was xylanase, observed only in the D. fristingensis isolate. Although this activity has been previously described in Cryptococcus species [27, 28], no xylanase activity was observed in the Cryptococcus isolates identified here. Consistent with our results, protease, amylase and esterase extracellular activities have been reported in several yeast species isolated from cold and tropical environments [24–26, 29–33]. However, we present the first report of extracellular amylase activity in Le. creatinivora, H. watticus, Leuconeurospora sp. and D. fristingensis. In addition to Mrakia and Rhodotorula species, for which extracellular pectinase activity has been described [33], we detected pectinase activity in species of Wickerhamomyces, Metschnikowia, Dioszegia, Leucosporidiella and Candida.