2007
DOI: 10.1016/j.pep.2006.06.020
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High level production of the Magnaporthe grisea fructose 1,6-bisphosphate aldolase enzyme in Escherichia coli using a small volume bench-top fermentor

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Cited by 7 publications
(2 citation statements)
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“…pWT has been characterized extensively and exhibits essentially the same stability, enzymatic activity and structure as WT SOD1 [19,22,23]. Recombinant pWT and mutant SOD1s were expressed as described previously using shaker flask cultures [26,27] or fed-batch fermentation [28]. In the expression system used, SOD1 is exported to the periplasm from which it is obtained by osmotic shock for shaker flask cultures, or from the culture supernatant of fermentation cultures using ammonium sulfate (40% w/v) precipitation.…”
Section: Preparation and Purification Of Recombinant Sod1mentioning
confidence: 99%
“…pWT has been characterized extensively and exhibits essentially the same stability, enzymatic activity and structure as WT SOD1 [19,22,23]. Recombinant pWT and mutant SOD1s were expressed as described previously using shaker flask cultures [26,27] or fed-batch fermentation [28]. In the expression system used, SOD1 is exported to the periplasm from which it is obtained by osmotic shock for shaker flask cultures, or from the culture supernatant of fermentation cultures using ammonium sulfate (40% w/v) precipitation.…”
Section: Preparation and Purification Of Recombinant Sod1mentioning
confidence: 99%
“…The mass spectrometry and bioinformatics of spots 17 and 18 resulted in the identification of the fructose-1,6-bisphosphate aldolase (Fba) protein with a molecular mass of 43 KDa and isoelectric points of 6.00 and 6.14, respectively. Fba proteins are enzymes used in glycolysis and gluconeogenesis and are classified into class I and class II [70][71][72]. Class I enzymes are present in plants, animals, algae, and prokaryotes.…”
Section: Discussionmentioning
confidence: 99%