The Role of Water Activity in Terms of Enzyme Activity and Enantioselectivity during Enzymatic Esterification in Non-conventional Media

Lajtai-Szabó, Piroska; Nemestóthy, Nándor; Gubicza, L.

doi:10.33927/hjic-2020-22

Cited by 3 publications

(2 citation statements)

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“…This enzymatic reaction in non-conventional media continuously produces water which strongly affects enzyme activity. To maintain the reaction parameters, the water activity (aw) should remain constant [10]. In lipase-catalyzed esterification reactions, water activity is a major factor because a sufficient amount of water must be present to retain the active structure of the enzyme, however, if in excess in the reaction medium, the lipase will catalyze a competing hydrolysis reaction [11].…”

Section: Introductionmentioning

confidence: 99%

Synthesis of Sugar Esters Using Maize Seed Lipase as a Biocatalyst

Ferdjani,

Selaimia

2024

Hung. J. Ind. Chem.

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This work is devoted to the extraction of a lipase from maize seeds obtained at low cost without extensive purification technology and used as a biocatalyst in the synthesis of various sugar esters as potential biosurfactants in the detergent industry. Indeed, several reactions have been carried out between different sugars - namely glucose, galactose, saccharose, lyxose, fructose and sorbitol - and stearic acid in a ratio of 2.5:1 in hexane at 50 °C. Kinetic monitoring of the target reactions was carried out by volumetric analysis in order to determine the conversions (C). The best results obtained were C = 76, 71 and 67% in the presence of glucose, lyxose and galactose, respectively. In addition, HPLC and TLC analyses revealed that for every sugar used two types of esters formed.

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Section: Introductionmentioning

confidence: 99%

Synthesis of Sugar Esters Using Maize Seed Lipase as a Biocatalyst

Ferdjani,

Selaimia

2024

Hung. J. Ind. Chem.

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“…Asymmetric syntheses are preferentially obtained using enzymes, given the capability of most to catalyse organic reactions with high enantioselectivity under mild conditions [4,5]. Besides isolated enzymes, whole cells are also being applied more and more often as biocatalysts, given the disparate attributes of both.…”

Section: Introductionmentioning

confidence: 99%

Production of Chiral (S)-2-Phenyl-1-Propanol by Enantioselective Biocatalysts

Lajtai-Szabó¹,

Bagó²,

Nemestóthy³

2022

Hung. J. Ind. Chem.

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Enantioselective production of (S)-2-phenyl-1-propanol is important as in order to be applied in industry, a high degree of optical purity is required. Besides organocatalysts and metal complexes, biocatalysts can be used for its synthesis in their isolated form or as whole-cell biocatalysts, both of which have various advantages and disadvantages. In this research, Saccharomyces cerevisiae, as a whole-cell biocatalyst, and recombinant horse-liver alcohol dehydrogenase (ADH), as an isolated enzyme, were investigated in terms of their activity, kinetics and enantioselectivity. In the case of yeast, therate of cofactor regeneration was twice that of substrate conversion, moreover, the biocatalyst Saccharomyces cerevisiae can be characterised by substrate-limited kinetics and low nantioselectivity. In contrast, the isolated enzyme recombinant horse-liver ADH exhibited biphasic kinetics and cofactor regeneration was the rate-limiting step. The outstanding enantioselectivity of recombinant horse-liver ADH renders it a promising catalyst for the purpose of this synthesis.

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