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Background  Pectinolytic enzymes, which are used in several industries, especially in the clarification process during wine and fruit juice production, represent approximately 10% of the global enzyme market. To prevent the proliferation of undesired microorganisms, to retain labile and volatile flavor compounds, and to save energy, the current trend is to perform this process at low temperatures. However, the commercially available pectinases are highly active at temperatures approximately 50 °C and poorly active at temperatures below 35 °C, which is the reason why there is a constant search for cold-active pectinases. In preliminary studies, pectinolytic activity was detected in cold-adapted yeasts and yeast-like microorganisms isolated from Antarctica. The aim of the present work was to characterize pectinases secreted by these microorganisms and to express the best candidate in  Pichia pastoris .    Results  Degradation of pectin by extracellular protein extracellular extracts obtained from 12 yeast cultures were assayed in plates at 4 °C to 37 °C and pH from 5.4 to 7.0, obtaining positive results in samples obtained from  Dioszegia  sp.,  Phenoliferia glacialis  and  Tetracladium  sp. An enzyme was purified from  Tetracladium  sp., analyzed by peptide mass fingerprinting and compared to genome and transcriptome data from the same microorganism. Thus, the encoding gene was identified corresponding to a polygalacturonase-encoding gene. The enzyme was expressed in  Pichia pastoris , and the recombinant polygalacturonase displayed higher activity at 15 °C than a mesophilic counterpart.    Conclusions  Extracellular pectinase activity was found in three yeast and yeast-like microorganisms from which the highest activity was displayed by  Tetracladium  sp., and the enzyme was identified as a polygalacturonase. The recombinant polygalacturonase produced in  P. pastoris  showed high activity at 15 °C, representing an attractive candidate to be applied in clarification processes in the production of fermented beverages and fruit juices.    Electronic supplementary material  The online version of this article (10.1186/s12934-019-1092-2) contains supplementary material, which is available to authorized users.

microbial cell factories

Pectinase secreted by psychrotolerant fungi: identification, molecular characterization and heterologous expression of a cold-active polygalacturonase from Tetracladium sp.