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The STUDIA UNIVERSITATIS BABEŞ-BOLYAI issue article summary
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Abstract: The enzymes produced by halophilic archaea are capable of withstanding extreme conditions such as high temperature, high or low pH, organic solvent and high salt concentration environments. Starch degrading enzyme, amylase, catalyzes the hydrolysis of internal alpha-1,4 glycosidic bonds in polysaccharides with the retention of alpha anomeric configuration in the products. Amylases are widely used during processing of food, medicines, paper, textile, etc. Amylases are increasingly studied due to the relative ease of large-scale production. Halophilic archaea within the class Halobacteria include a large group of aerobic microbes that live and grow in hypersaline environments. Many halophilic archaea are known to produce amylase. Research on chracterization of halophilic amylase, however, is hardly ever reported (Santorelli et al., 2016). We explored halophilic archaea producing amylase with basic halophilic archaea medium that contained soluble starch. We isolated an extremely halophilic, starch-degraging strain U243S from sea salt samples made in Okinawa, Japan. The extracellular amylase in supernatant had pH optimum at 7.0, optimum temperature at 60o C, optimum NaCl concentration at 20% (w/v), and showed 80% relative activity after 2 hours of heating at 50o C. The 16S rRNA partial gene sequence of strain U243S (1353 bp) indicated its relatedness to Halomicroarcula pellucida strain BNERC31T (100% similarity) (Echigo et al., 2013). amylase, haloarchaea, halophilic amylase. |
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