2019
DOI: 10.1016/j.pep.2018.11.009
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Heterologous expression and biochemical characterization of a novel cold-active α-amylase from the Antarctic bacteria Pseudoalteromonas sp. 2-3

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Cited by 27 publications
(9 citation statements)
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“…The bacterial genera Bacteroides , Clostridium , and Pseudoalteromonas are significantly correlated with amylase activity in the midgut of mud crabs during molting ( Fig. 7C ), which is consistent with the results of previous studies that many members of these genera can produce amylase ( 65 67 ). Collectively, the results of this study suggest that digestive enzymes could regulate the microbiota in the hepatopancreas and midgut of mud crab during molting, which provides a suitable condition for the restoration and reconstruction of host-microbiome homeostasis in crab molting.…”
Section: Discussionsupporting
confidence: 91%
“…The bacterial genera Bacteroides , Clostridium , and Pseudoalteromonas are significantly correlated with amylase activity in the midgut of mud crabs during molting ( Fig. 7C ), which is consistent with the results of previous studies that many members of these genera can produce amylase ( 65 67 ). Collectively, the results of this study suggest that digestive enzymes could regulate the microbiota in the hepatopancreas and midgut of mud crab during molting, which provides a suitable condition for the restoration and reconstruction of host-microbiome homeostasis in crab molting.…”
Section: Discussionsupporting
confidence: 91%
“…Recently, a cold‐active α‐amylase was expressed from Pseudoalteromona sp., a bacterium isolated from the Chilean Antarctic seawater. The pH optimum of this enzyme was 8.0, while the optima temperature was 20°C (Sanchez, Ravanal, Andrews, & Asenjo, 2019). The low optimum temperature reported for this enzyme makes it an excellent alternative in the food industry where low‐temperature processes are required, thus, minimizing cost.…”
Section: Categories and Applications Of Food Enzymes From Extremophilesmentioning
confidence: 99%
“…The heterologous expression of α-amylase from Antarctic bacterium Pseudoalteromonas sp. 2-3 in E. coli BL21 (DE3) showed the optimum temperature at 20 °C with activation by Ca 2+ , the enzyme being active on potato starch giving a K m of 6.94 mg/mL and V max of 0.27 mg/mL.min [84]. Kim et al [85] in 2017 boosted the stability of psychrophilic α-amylase by cloning the gene encoding an α-amylase from a psychrophilic Arthrobacter agilis PAMC 27388 strain into a pET-28a (+) vector and this was heterologously expressed in E. coli BL21 (DE3).…”
Section: Strategies To Improve Stability During Cold Adaptationmentioning
confidence: 99%
“…A classic example for this is represented by the cold adapted α-amylase, Amy13c6 from a metagenomic library of the cold and alkaline environment of Greenland. This enzyme had an optimal pH of 8.0-9.0, so that it can be used in laundry applications at very low temperatures [84]. The α-amylase gene (amyM) derived using the pUC19 vector from soil metagenomic library when overexpressed and purified was stable at pH 9.0 [54].…”
Section: Enhancement Of Acid/base Stability By Protein Engineering Stmentioning
confidence: 99%