1997
DOI: 10.1016/s1381-1177(96)00021-5
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Pyruvic acid production using methylotrophic yeast transformants as catalyst

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Cited by 42 publications
(31 citation statements)
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“…These process alternatives can be divided into three different approaches using: (i) enzymes (Burdick and Schaeffer, 1987;Eisenberg et al, 1997); (ii) resting cells (Izumi et al, 1982, Ogawa et al, 2001Schinschel and Simon, 1993); and (iii) fermentation processes (Li et al, 2001a(Li et al, , 2001b(Li et al, , 2002Yokota et al, 1994). In comparison to the other approaches, fermentation methods offer the opportunity to produce pyruvate from the sustainable, lowcost substrate, glucose, with high product/substrate yield, while avoiding the coproduction of unwanted byproducts like H 2 O 2 , as is usually the case when enzymatic methods are employed.…”
Section: Introductionmentioning
confidence: 99%
“…These process alternatives can be divided into three different approaches using: (i) enzymes (Burdick and Schaeffer, 1987;Eisenberg et al, 1997); (ii) resting cells (Izumi et al, 1982, Ogawa et al, 2001Schinschel and Simon, 1993); and (iii) fermentation processes (Li et al, 2001a(Li et al, , 2001b(Li et al, , 2002Yokota et al, 1994). In comparison to the other approaches, fermentation methods offer the opportunity to produce pyruvate from the sustainable, lowcost substrate, glucose, with high product/substrate yield, while avoiding the coproduction of unwanted byproducts like H 2 O 2 , as is usually the case when enzymatic methods are employed.…”
Section: Introductionmentioning
confidence: 99%
“…at a concentration of 6 g/L (dry cells) converted 0.5 M L-lactate into pyruvate in 12 h [82]. Permeabilized yeast cells of either Hansenula polymorpha or Pichia pastoris expressing glycolate oxidase and catalase were able to oxidize 0.5 M L-lactate to pyruvate for 12 cycles with 98% conversion of the lactate [83]. An L-lactate concentration above 0.5 M showed substrate inhibition of a whole-cell biocatalyst based on recombinant P. pastoris, and oxygen, a substrate for glycolate oxidase, was important for the conversion [84].…”
Section: Other Biological Methodsmentioning
confidence: 99%
“…As an important substrate, it has been widely used in enzymatic production of amino acids such as l-tyrosine, l-dihydroxyphenylalanine, and l-tryptophan [5,6]. Pyruvate is currently prepared by chemical synthesis, fermentation [7], and biocatalysis [8][9][10][11][12][13]. Due to the increasing concerns on environment-friendly processes, there is growing interest in the pyruvate production by biotechnological methods [14].…”
Section: Introductionmentioning
confidence: 99%