Cloning and characterization of α-L-rhamnosidase from Chloroflexus aurantiacus and its application in the production of isoquercitrin from rutin.
Biotechnol Lett
; 41(3): 419-426, 2019 Mar.
Article
em En
| MEDLINE
| ID: mdl-30666483
ABSTRACT
OBJECTIVE:
This study was conducted to characterize recombinant α-L-rhamnosidase from Chloroflexus aurantiacus and apply the enzyme in the production of isoquercitrin from rutin.RESULTS:
The α-L-rhamnosidase from C. aurantiacus was cloned and expressed in Escherichia coli BL21 and purified as a soluble enzyme. α-L-rhamnosidase purified from C. aurantiacus has a molecular mass of approximately 105 kDa and is predicted to exist as a homodimer with a native enzyme of 200 kDa. The purified enzyme exhibited the highest specific activity for rutin among the reported isoquercitrin producing α-L-rhamnosidases and was applied in the production of isoquercitrin from rutin. Under the optimised conditions of pH 6.0, 50 °C, 0.6 U mL-1 α-L-rhamnosidase, and 30 mM rutin, α-L-rhamnosidase from C. aurantiacus produced 30 mM isoquercitrin after 2 h with a 100% conversion yield and productivity of 15 mM h-1.CONCLUSIONS:
We achieved a high productivity of isoquercitrin from rutin. Moreover, these results suggest that α-L-rhamnosidase from C. aurantiacus is an effective isoquercitrin producer.Palavras-chave
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Quercetina
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Rutina
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Proteínas Recombinantes
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Chloroflexus
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Glicosídeo Hidrolases
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article