Immobilization of phenylalanine dehydrogenase onto Eupergit CM for the synthesis of (S)-2-amino-4-phenylbutyric acid

Ahmad, A.L.; Low, Eva M.; Shukor, Syamsul Rizal Abd

doi:10.1016/j.molcatb.2012.11.014

Cited by 14 publications

(8 citation statements)

References 28 publications

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“…Eupergit CM was applied for PheDH covalent immobilization with the operational pH range for reductive amination slightly broadened (pH 7.5-9.5). 19 Villalonga et al reported the covalent immobilization of PheDH with amino-activated cellulose membrane, which maintained 82% initial activity. 20 However, further study is needed to overcome the problems of complex operation, inactivation, and obtaining high activity recovery.…”

Section: Introductionmentioning

confidence: 99%

Metal ions coordinated immobilization of phenylalanine dehydrogenase by GO‐PEI with high activity recovery and enhanced stability

Yao

Liu

Wang

et al. 2020

J of Chemical Tech & Biotech

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BACKGROUND Dehydrogenases dependent on NAD(P)H are widely applied for biosynthesis of chiral chemicals. However, they are unstable and easy denaturated compared with hydrolases. A new strategy for dehydrogenases immobilization with the advantages of easy operation and high activity recovery should be developed. Biocompatible hybrid materials (GO‐PEI‐M) have been obtained by metal ions coordinated polyethylenimine (PEI) functionalized graphene oxide (GO). RESULTS The immobilized enzyme recovery rates of GO‐PEI‐Mg (magnesium ion coordinated GO‐PEI) and GO‐PEI‐Mn (manganese ion coordinated GO‐PEI). In addition, the stability of GO‐PEI‐Mn‐PheDH (Phenylalanine Dehydrogenase) and GO‐PEI‐Mg‐PheDH was greatly improved, and it maintained 65% and 79% activity, respectively, after seven times reuse. In addition, the stability of GO‐PEI‐Mn‐PheDH (Phenylalanine Dehydrogenase) and GO‐PEI‐Mg‐PheDH was greatly improved. After seven times reuse, GO‐PEI‐Mn‐PheDH and GO‐PEI‐Mn‐PheDH and maintained 65% and 79% activity, respectively. An assembly mechanism was proposed from the perspectives of multi‐level interactions, including hydrogen bonding, electrostatic forces, and coordinated bonds. CONCLUSION GO‐PEI‐Metal ion hybrid materials offer a promising carrier for enzyme immobilization with the advantages of biocompatibility and relatively strong interaction. © 2020 Society of Chemical Industry

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Section: Introductionmentioning

confidence: 99%

Metal ions coordinated immobilization of phenylalanine dehydrogenase by GO‐PEI with high activity recovery and enhanced stability

Yao

Liu

Wang

et al. 2020

J of Chemical Tech & Biotech

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“…[13] In the case of ADH, a coenzyme recycling system is required owing to the dependence on the either NADH or NADPH to yield reducing equivalents; hence, such reactions are not cost-effective. [14] A recent study used Lphenylalanine dehydrogenase derived from Rhodococcus sp. M4 to synthesize PPA.…”

Section: Introductionmentioning

confidence: 99%

Production of α‐Ketoisocaproate and α‐Keto‐β‐Methylvalerate by Engineered L‐Amino Acid Deaminase

et al. 2019

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This study aimed to develop an efficient enzymatic strategy for industrial production of α‐ketoisocaproate (α‐KIC) and α‐keto‐β‐methylvalerate (α‐KMV) from L‐leucine and L‐isoleucine, respectively. L‐amino acid deaminase from Proteus mirabilis (PmLAAD) was heterologously expressed in E. coli BL21(DE3) and modified to increase its catalytic efficiency by engineering the PmLAAD substrate‐binding cavity and entrance tunnel. Four essential residues (Q92, M440, T436, and W438) were identified from structural analysis and molecular dynamics simulations. Residue Q92 was mutated to alanine, and the volume of the binding cavity, enzyme activity, and the kcat/Km value of mutant PmLAAD Q92A increased to 994.2 Å3, 191.36 U mg−1, and 1.23 mM−1 min−1, respectively; consequently, the titer and conversion rate of α‐KIC from L‐leucine were 107.1 g L−1 and 98.1 %, respectively. For mutant PmLAADT436/W438A, the entrance tunnel, enzyme activity, and the kcat/Km value increased to 1.71 Å, 170.12 U mg−1, and 0.70 mM−1 min−1, respectively; consequently, the titer and conversion rate of α‐KMV from L‐isoleucine were 98.9 g L−1 and 99.7 %, respectively. Therefore, augmentation of the substrate‐binding cavity and entrance tunnel of PmLAAD can facilitate efficient industrial synthesis of α‐KIC and α‐KMV.

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“…In spite of the fact that several racemic carboxylic acids have been resolved by lipases, [13][14][15][16][17][18][19][20][21][22] a literature survey shows only few methodologies for the enantioselective esterification of 2-methylbutyric acid. This may be due to the fact that methyl and ethyl moieties have a small size difference making it difficult for the efficient recognition by the lipase.…”

Section: Introductionmentioning

confidence: 99%

Convenient enzymatic resolution of (R,S)‐2‐methylbutyric acid catalyzed by immobilized lipases

et al. 2017

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The application of several immobilized lipases has been explored in the enantioselective esterification of (R,S)-2-methylbutyric acid, an insect pheromone precursor. With the use of Candida antarctica B, using hexane as solvent, (R)-pentyl 2-methylbutyrate was prepared in 2 h with c 40%, ee p 90%, and E = 35, while Thermomyces lanuginosus leads to c 18%, ee p 91%, and E = 26.The (S)-enantiomer was obtained by the use of Candida rugosa or Rhizopus oryzae (2-h reaction, c 34% and 35%, ee p 75 and 49%, and E = 10 and 4, respectively). Under optimal conditions, the effect of the solvent, the molar ratio, and the nucleophile were evaluated.

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Immobilization of phenylalanine dehydrogenase onto Eupergit CM for the synthesis of (S)-2-amino-4-phenylbutyric acid

Cited by 14 publications

References 28 publications

Metal ions coordinated immobilization of phenylalanine dehydrogenase by GO‐PEI with high activity recovery and enhanced stability

Metal ions coordinated immobilization of phenylalanine dehydrogenase by GO‐PEI with high activity recovery and enhanced stability

Production of α‐Ketoisocaproate and α‐Keto‐β‐Methylvalerate by Engineered L‐Amino Acid Deaminase

Convenient enzymatic resolution of (R,S)‐2‐methylbutyric acid catalyzed by immobilized lipases

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