2011
DOI: 10.1002/btpr.687
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Enzyme activity evaluation of organic solvent‐treated phenylalanine ammonia lyase

Abstract: The direct one-step synthesis of L-phenylalanine methyl ester in an organic-aqueous biphasic system using phenylalanine ammonia lyase (E.C.4.3.1.5, PAL) containing Rhodotorula glutinis yeast whole cells was reported earlier. We report here further optimization of this biotransformation using isolated PAL, when the lyophilized enzyme is treated with different water miscible and water immiscible organic solvents. Use of isolated PAL enzyme is advantageous in overcoming diffusion barriers encountered when using P… Show more

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Cited by 11 publications
(3 citation statements)
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“…There was no pronounced effect on PTAL enzyme activity when the speed of agitating the reaction mixture during the incubation period was increased above 50 rpm ( Table 1 ). These results correspond well with almost all studies on effect of agitation on PAL protein using L -Phe, L -PM, t -CA, and t -CM substrates; optimal enzymatic conversions have been obtained at ∼50–100 rpm ( Yamada et al, 1981 ; Evans et al, 1987a , b ; D’Cunha et al, 1994 , 1996 ; Quinn et al, 2011 ).…”
Section: Resultssupporting
confidence: 90%
“…There was no pronounced effect on PTAL enzyme activity when the speed of agitating the reaction mixture during the incubation period was increased above 50 rpm ( Table 1 ). These results correspond well with almost all studies on effect of agitation on PAL protein using L -Phe, L -PM, t -CA, and t -CM substrates; optimal enzymatic conversions have been obtained at ∼50–100 rpm ( Yamada et al, 1981 ; Evans et al, 1987a , b ; D’Cunha et al, 1994 , 1996 ; Quinn et al, 2011 ).…”
Section: Resultssupporting
confidence: 90%
“…Phenylalanine ammonia-lyase (E.C.4.3.1.5-PAL) belongs to the family of lyases [16] , [17] . It has been used chiefly in the manufacture of L-phenylalanine by reversing the enzyme reaction with high concentration of trans-cinnamic acids and ammonia at an elevated pH.…”
Section: Introductionmentioning
confidence: 99%
“…For example, lyophilisation in the presence of kosmotropic salts can allow for recovery of enzyme activity upon solubilization in organic solvent. 14 While the main thrust of research in this area dates back to the 1980's and 1990's, developments in this area continue to be of interest, as illustrated by specific, recent reports on the activity of a phenylalanine ammonia lyase 15 or of a feruloyl esterase for breakdown of lignocellulosic biomass. 16 The choice of co-solvent has an important impact not only on enzyme activity and reagent solubilisation, but also on reaction 'greenness'; an excellent source of information is the 'GSK solvent selection guide', which considers the environmental sustainability of over 100 solvents, in the context of manufacturing active pharmaceutical ingredients.…”
Section: Box 1: How Green Is My Biocatalysis?mentioning
confidence: 99%