ArticleFolia microbiologica2025
Purification and biochemical characterization of a novel thermostable acid α-amylase from Geotrichum candidum PO27 with industrial application.
Article in Folia microbiologica, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Algeria imports all of its enzymes for use in different fields, which causes a serious economic problem as the cost of these enzymes is continuously rising. New enzymes with efficient and unique properties are always sought to meet the specific needs of various industry sectors. This study aimed to investigate the purification and characterization of α-amylase from the Algerian Geotrichum candidum PO27, and its potential application as a desizing agent in the textile industry. This enzyme was purified 6.73-fold in two process steps: concentration by ultrafiltration, followed by exclusion chromatography, achieving a final recovery of 9.1%. The results showed that its molecular weight was estimated for the first time by SDS-PAGE as 19.2 kDa. Physicochemical characterization of purified enzyme revealed optimal activity at pH 5 and 70 °C, thermostability properties, and high stability in the presence of Mg
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