Lipases and whole cell biotransformations of 2-hydroxy-2-(ethoxyphenylphosphinyl)acetic acid and its ester

Majewska, Paulina; Serafin, Monika; Klimek‐Ochab, Magdalena; Brzezińska-Rodak, Małgorzata; Żymańczyk–Duda, Ewa

doi:10.1016/j.bioorg.2016.02.011

Cited by 11 publications

(4 citation statements)

References 18 publications

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“…Comparing the results described in the previous and in the present work it can be seen that lipases catalyze butyryloxycarboxyphosphonates with moderate enantioselectivity and only Aspergillus niger lipase hydrolyzes fairly well all three substrates. Lipases from this fungus, both in the form of a purified enzyme and a lipase produced during a biotransformation reaction using whole cells of the microorganism, have often been used for the preparation of optically active hydroxyphosphonates [9,16,22]. However, in order to obtain pure enantiomers of hydroxyphosphonates the catalyst should be selected individually for each compound.…”

Section: Discussionmentioning

confidence: 99%

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Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-carboxymethylphosphonates

Majewska

2021

Catalysts

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The main objective of this study is the enantioselective synthesis of carboxyhydroxyphosphonates by lipase-catalyzed reactions. For this purpose, racemic dimethyl and dibutyl 1-butyryloxy-1-carboxymethylphosphonates were synthesized and hydrolyzed, using a wide spectrum of commercially available lipases from different sources (e.g., fungi and bacteria). The best hydrolysis results of dimethyl 1-butyryloxy-1-carboxymethylphosphonate were obtained with the use of lipases from Candida rugosa, Candida antarctica, and Aspergillus niger, leading to optically active dimethyl 1-carboxy-1-hydroxymethylphosphonate (58%–98% enantiomeric excess) with high enantiomeric ratio (reaching up to 126). However, in the case of hydrolysis of dibutyl 1-butyryloxy-1-carboxymethylphosphonate, the best results were obtained by lipases from Burkholderia cepacia and Termomyces lanuginosus, leading to optically active dibutyl 1-carboxy-1-hydroxymethylphosphonate (66%–68% enantiomeric excess) with moderate enantiomeric ratio (reaching up to 8.6). The absolute configuration of the products after biotransformation was also determined. In most cases, lipases hydrolyzed (R) enantiomers of both compounds.

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Section: Discussionmentioning

confidence: 99%

“…Lipase-catalyzed reactions were prepared according to a procedure described previously [22]. Reactions were carried out in a biphasic system (3.8 mL) consisting of 0.05 M phosphate buffer (pH 7.0, 3.0 mL) and a mixture of diisopropyl ether (0.2 mL) with hexane (0.6 mL).…”

Section: Enzymatic Hydrolysis General Proceduresmentioning

confidence: 99%

Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-carboxymethylphosphonates

Majewska

2021

Catalysts

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“…Enantioselective hydrolysis of diethyl 2,3-dipalmitoyloxypropylphosphonate (1) by PLA 2 from porcine pancreas was applied in these studies to synthesize (R)-DPPnC (Scheme 1). As enzymatic hydrolysis is a convenient method for the resolution of racemic α and β-hydroxyphosphonate esters [33][34][35][36], the hydrolytic activity of phospholipase A 2 towards DPPnC may be also used for the kinetic resolution of racemic forms of this type of phosphonolipids.…”

Section: Hydrolysis Catalyzed By Phospholipases A2mentioning

confidence: 99%

Comparative Studies on the Susceptibility of (R)-2,3-Dipalmitoyloxypropylphosphonocholine (DPPnC) and Its Phospholipid Analogues to the Hydrolysis or Ethanolysis Catalyzed by Selected Lipases and Phospholipases

2021

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Susceptibility of soybean phosphatidylcholine, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and its phosphono analogue (R)-2,3-dipalmitoyloxypropylphosphonocholine (DPPnC) towards selected lipases and phospholipases was compared. The ethanolysis of substrates at sn-1 position was carried out by lipase from Mucor miehei (Lipozyme®) and lipase B from Candida antarctica (Novozym 435) in 95% ethanol at 30 °C, and the hydrolysis with LecitaseTM Ultra was carried out in hexane/water at 50 °C. Hydrolysis at sn-2 position was carried out in isooctane/Tris-HCl/AOT system at 40 °C using phospholipase A2 (PLA2) from porcine pancreas and PLA2 from bovine pancreas or 25 °C using PLA2 from bee venom. Hydrolysis in the polar part of the studied compounds was carried out at 30 °C in acetate buffer/ethyl acetate system using phospholipase D (PLD) from Streptococcus sp. and PLD from white cabbage or in Tris-HCl buffer/methylene chloride system at 35 °C using PLD from Streptomyces chromofuscus. The results showed that the presence of C-P bond between glycerol and phosphoric acid residue in DPPnC increases the rate of enzymatic hydrolysis or ethanolysis of ester bonds at the sn-1 and sn-2 position and decreases the rate of hydrolysis in the polar head of the molecule. The most significant changes in the reaction rates were observed for reaction with PLD from Streptococcus sp. and PLD from Streptomyces chromofuscus that hydrolyzed DPPnC approximately two times slower than DPPC and soybean PC. The lower susceptibility of DPPnC towards enzymatic hydrolysis by phospholipases D gives hope for the possibility of using DPPnC-like phosphonolipids as the carriers of bioactive molecules that, instead of choline, can be bounded with diacylpropylphosphonic acids (DPPnA).

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“…However, the yields obtained were comparable in terms of cost effectiveness (BALASUBRAMANIAM et al, 2012). Majewska et al (2016) also performed one of the few studies that directly compare the efficiency of whole cell lipases and commercial lipases. They tested five different lipases and whole cells of eight different microorganisms for the hydrolysis of 2-butyryloxy-2-(ethoxyphenylphosphinyl) acetic acid and the whole cells presented the best conversion degrees, enantiomeric excess and enantioselectivity.…”

Section: Biodiesel Synthesismentioning

confidence: 99%

A review between whole-cells and immobilized lipases technologies for biodiesel and flavor esters production

Sardagna

Lopes

Ries

2021

R. Eletr. Cient. da Uergs

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As lipases são enzimas versáteis que catalisam diversas reações e podem ser aplicadas em várias áreas da indústria. No entanto, a biocatálise enfrenta um obstáculo econômico para poder competir com as rotas convencionais. Diferentes estratégias têm sido estudadas com o objetivo de reduzir o custo dos biocatalisadores e melhorar a atividade e estabilidade catalítica. A imobilização enzimática é uma das estratégias mais eficientes para tornar a aplicação de enzimas competitiva em larga escala industrial, proporcionando reutilização contínua, facilidade de separação do meio reacional e maior eficiência do processo. No entanto, apesar dos avanços tecnológicos alcançados, os biocatalisadores ainda são caros para usos industriais devido às etapas de recuperação, purificação e imobilização de enzimas. Nesse contexto, surge a tecnologia de células integras (CI) como uma forma de imobilização, na qual as próprias células, geralmente cultivadas em um suporte, são aplicadas no processo de biotransformação, contendo as proteínas de interesse aderidas à sua superfície, permitindo fácil separação, reutilização e dispensando a etapa de purificação. Embora a tecnologia de células inteiras tenha se tornado uma ferramenta valiosa para muitos processos de biotransformação, existem alguns inconvenientes inerentes, que impediram seu avanço em escala industrial, e muitos estudos foram realizados com o objetivo de otimizar seu desempenho. Este artigo apresenta uma revisão entre as tecnologias de células íntegras e de lipases imobilizadas, principalmente relacionadas às sínteses de biodiesel e de ésteres de sabor, uma vez que estas são amplamente relatadas na literatura.

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Lipases and whole cell biotransformations of 2-hydroxy-2-(ethoxyphenylphosphinyl)acetic acid and its ester

Cited by 11 publications

References 18 publications

Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-carboxymethylphosphonates

Lipase-Catalyzed Kinetic Resolution of Dimethyl and Dibutyl 1-Butyryloxy-1-carboxymethylphosphonates

Comparative Studies on the Susceptibility of (R)-2,3-Dipalmitoyloxypropylphosphonocholine (DPPnC) and Its Phospholipid Analogues to the Hydrolysis or Ethanolysis Catalyzed by Selected Lipases and Phospholipases

A review between whole-cells and immobilized lipases technologies for biodiesel and flavor esters production

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