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Biochemical characterization of the amylase activity from the New Haloarchaeal Strain Haloarcula sp. HS isolated in the Odiel Marshlands
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Orientador(es)
Resumo(s)
Alpha-amylases are a large family of α,1-4-endo-glycosyl hydrolases distributed in all
kingdoms of life. The need for poly-extremotolerant amylases encouraged their search in extreme
environments, where archaea become ideal candidates to provide new enzymes that are able to work
in the harsh conditions demanded in many industrial applications. In this study, a collection of
haloarchaea isolated from Odiel saltern ponds in the southwest of Spain was screened for their amylase activity. The strain that exhibited the highest activity was selected and identified as Haloarcula sp.
HS. We demonstrated the existence in both, cellular and extracellular extracts of the new strain, of
functional α-amylase activities, which showed to be moderately thermotolerant (optimum around
60 ◦C), extremely halotolerant (optimum over 25% NaCl), and calcium-dependent. The tryptic digestion followed by HPLC-MS/MS analysis of the partially purified cellular and extracellular extracts
allowed to identify the sequence of three alpha-amylases, which despite sharing a low sequence identity, exhibited high three-dimensional structure homology, conserving the typical domains and most
of the key consensus residues of α-amylases. Moreover, we proved the potential of the extracellular
α-amylase from Haloarcula sp. HS to treat bakery wastes under high salinity conditions.
Descrição
Palavras-chave
Amylase Extremozymes Haloarchaea Enzymatic characterization Proteomics
Contexto Educativo
Citação
Biology 10 (4): 337 (2021)
Editora
MDPI