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Screening and characterization of amylase and cellulase activities in psychrotolerant yeasts
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Screening and characterization of amylase and cellulase activities in psychrotolerant yeasts
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Screening and characterization of amylase and cellulase activities in psychrotolerant yeasts
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Journal Article
Screening and characterization of amylase and cellulase activities in psychrotolerant yeasts
2016
Overview
Background
Amylases and cellulases have great potential for application in industries such as food, detergent, laundry, textile, baking and biofuels. A common requirement in these fields is to reduce the temperatures of the processes, leading to a continuous search for microorganisms that secrete cold-active amylases and cellulases. Psychrotolerant yeasts are good candidates because they inhabit cold-environments. In this work, we analyzed the ability of yeasts isolated from the Antarctic region to grow on starch or carboxymethylcellulose, and their potential extracellular amylases and cellulases.
Result
All tested yeasts were able to grow with soluble starch or carboxymethylcellulose as the sole carbon source; however, not all of them produced ethanol by fermentation of these carbon sources. For the majority of the yeast species, the extracellular amylase or cellulase activity was higher when cultured in medium supplemented with glucose rather than with soluble starch or carboxymethylcellulose. Additionally, higher amylase activities were observed when tested at pH 5.4 and 6.2, and at 30–37 °C, except for
Rhodotorula glacialis
that showed elevated activity at 10–22 °C. In general, cellulase activity was high until pH 6.2 and between 22–37 °C, while the sample from
Mrakia blollopis
showed high activity at 4–22 °C. Peptide mass fingerprinting analysis of a potential amylase from
Tetracladium
sp. of about 70 kDa, showed several peptides with positive matches with glucoamylases from other fungi.
Conclusions
Almost all yeast species showed extracellular amylase or cellulase activity, and an inducing effect by the respective substrate was observed in a minor number of yeasts. These enzymatic activities were higher at 30 °C in most yeast, with highest amylase and cellulase activity in
Tetracladium
sp. and
M. gelida,
respectively. However,
Rh. glacialis
and
M. blollopis
displayed high amylase or cellulase activity, respectively, under 22 °C. In this sense, these yeasts are interesting candidates for industrial processes that require lower temperatures.
