Production of D-tagatose and D-fructose from whey by co-immobilized enzymatic system

ENZIMAS

SUERO

FRUCTUOSA

INMOVILIZACION DE ENZIMAS

BIBLIOGRAFIA NACIONAL QUIMICA

2019

β-Galactosidase from Bacillus circulans, l-arabinose (d-galactose) isomerase from Enterococcus faecium and d-xylose (d-glucose) isomerase from Streptomyces rubiginosus, immobilized individually and co-immobilized onto Eupergit C and Eupergit C 250 L, were used batchwise in mono- and multi-bioreactor systems for lactolysis/isomerization processes in Mozzarella cheese whey. The degrees of lactolysis achieved with the multienzymatic systems were significantly higher than those obtained by using mono-enzymatic processes with immobilized β-galactosidase. This effect was observed when at least one of the isomerases was present in the reactor, suggesting a reduction in product inhibition of lactolysis as a result of decrease in d-galactose and/or d-glucose levels during reaction. Temperature was the main factor that affected d-tagatose/d-galactose and d-fructose/d-glucose ratios. Degree of lactolysis achieved at 50 °C was between 88% and 100%. Mono-reactor processes with co-immobilized stabilized tri-enzymatic systems exhibited the best performances regarding conversion degrees (producing complete lactolysis, 45% d-tagatose and 39% d-fructose against 93% lactolysis, 40% d-tagatose and 29% d-fructose for mono-reactor processes with individually immobilized enzymes). Stabilized co-immobilized enzymes were able to improve further to 53% the yield in d-fructose when demineralized Mozzarella cheese whey was employed as substrate. The productivities were moderate, ranging 9.5–10 g/Lh in terms of d-tagatose. Stabilized derivatives could be reused for at least 12 cycles in batch bio-reactors.

Molecular Catalysis  v. 463, 2019. -- p. 99-109

Elsevier

2019

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Artículo

DOI: 10.1016/j.mcat.2018.11.017

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