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Production of a Recombinant α-l-Rhamnosidase from Aspergillus niger CCTCC M 2018240 in Pichia pastoris
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Production of a Recombinant α-l-Rhamnosidase from Aspergillus niger CCTCC M 2018240 in Pichia pastoris
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Production of a Recombinant α-l-Rhamnosidase from Aspergillus niger CCTCC M 2018240 in Pichia pastoris
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Journal Article
Production of a Recombinant α-l-Rhamnosidase from Aspergillus niger CCTCC M 2018240 in Pichia pastoris
2019
Overview
α-
l
-Rhamnosidases have wide application in the field of biotechnology for derhamnosylation of many natural glycosides. In this study, an α-
l
-rhamnosidase-producing strain,
Aspergillus niger
CCTCC M 2018240, was isolated from decayed orange peels, and the gene encoding α-
l
-rhamnosidase was successfully expressed in
Pichia pastoris
GS115. Three-dimensional structure simulation indicates the enzyme is a member of glycoside hydrolase 78 family. The optimal recombinant strain GS115/pPIC9K-
rha
-14 exhibited an enzyme activity of 0.47 U/mL when cultured in shaking flasks, and the recombinant α-
l
-rhamnosidase hydrolyzed α-1,2 and α-1,6 glycosidic bonds in naringin and rutin, respectively, thus generating prunin and isoquercitrin, respectively. Through high density-induced fermentation based on a glycerol feeding strategy in a 3-L bioreactor, the enzyme activity reached 46.87 U/mL after 7 days of methanol incubation, which was approximately 99 times higher than that produced in shaking flasks. This process offers a simple and effective approach for the large-scale production of α-
l
-rhamnosidase.
Publisher
Springer US,Springer Nature B.V
Subject
/ Aspergillus niger - enzymology
/ Chemistry and Materials Science
/ Enzymes
/ Flasks
/ genes
/ Glycerol
/ Glycoside Hydrolases - biosynthesis
/ Glycoside Hydrolases - chemistry
/ Glycoside Hydrolases - genetics
/ Glycoside Hydrolases - metabolism
/ methanol
/ naringin
/ Recombinant Proteins - biosynthesis
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Rutin
/ Shaking
/ Yeast
