Purification and characterization of an aminopeptidase A from<i>Staphylococcus chromogenes</i>and its use for the synthesis of amino‐acid derivatives and dipeptides

Yoshpe-Besancon, Iris; Auriol, Daniel; Paul, F.; Monsan, Pierre; Gripon, J.C.; Ribadeau‐Dumas, B.

doi:10.1111/j.1432-1033.1993.tb19875.x

Cited by 13 publications

(3 citation statements)

References 30 publications

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“…Some studies suggest the high enzyme activity and/or stability in aqueous glymes. Yoshpe-Besancon et al 322 observed that a 55% triglyme solution could shi the equilibrium of aminopeptidase A from amide bond hydrolysis to peptide bond formation, which allowed a selective a-amino protection of derivatives of many amino acids (except glycine and proline) by the malyl group. Rosell et al 323 found that 50% (v/v) aqueous solutions of diglyme (G2) or tetraglyme (G4) depressed the hydrolytic activity of penicillin acylase by roughly 65%, but boosted its synthetic activity by $4.8 times.…”

Section: (Co-)solvents For Biocatalysismentioning

confidence: 99%

Glymes as versatile solvents for chemical reactions and processes: from the laboratory to industry

2014

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Glymes, also known as glycol diethers, are saturated non-cyclic polyethers containing no other functional groups. Most glymes are usually less volatile and less toxic than common laboratory organic solvents; in this context, they are more environmentally benign solvents. However, it is also important to point out that some glymes could cause long-term reproductive and developmental damages despite their low acute toxicities. Glymes have both hydrophilic and hydrophobic characters that common organic solvents are lack of. In addition, they are usually thermally and chemically stable, and can even form complexes with ions. Therefore, glymes are found in a broad range of laboratory applications including organic synthesis, electrochemistry, biocatalysis, materials, and Chemical Vapor Deposition (CVD), etc. In addition, glyme are used in numerous industrial applications, such as cleaning products, inks, adhesives and coatings, batteries and electronics, absorption refrigeration and heat pumps, as well as pharmaceutical formulations, etc. However, there is a lack of comprehensive and critical review on this attractive subject. This review aims to accomplish this task by providing an in-depth understanding of glymes’ physicochemical properties, toxicity and major applications.

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Section: (Co-)solvents For Biocatalysismentioning

confidence: 99%

Glymes as versatile solvents for chemical reactions and processes: from the laboratory to industry

2014

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“…35 A few studies suggested the high enzyme activity and/or stability in aqueous glymes. 36–39 Our group 40 found that long-chain glymes are highly compatible with immobilized Candida antarctica lipase B.…”

Section: Introductionmentioning

confidence: 99%

DNA-based asymmetric catalysis: role of ionic solvents and glymes

Zhao

Shen

2014

RSC Adv.

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Recently, DNA has been evaluated as a chiral scaffold for metal complexes to construct so called ‘DNA-based hybrid catalysts’, a robust and inexpensive alternative to enzymes. The unique chiral structure of DNA allows the hybrid catalysts to catalyze various asymmetric synthesis reactions. However, most current studies used aqueous buffers as solvents for these asymmetric reactions, where substrates/products are typically suspended in the solutions. The mass transfer limitation usually requires a long reaction time. To overcome this hurdle and to advance DNA-based asymmetric catalysis, we evaluated a series of ionic liquids (ILs), inorganic salts, deep eutectic solvents (DES), glymes, glycols, acetonitrile and methanol as co-solvents/additives for the DNA-based asymmetric Michael addition. In general, these additives induce indistinguishable changes to the DNA B-form duplex conformation as suggested by circular dichroism (CD) spectroscopy, but impose a significant influence on the catalytic efficiency of the DNA-based hybrid catalyst. Conventional organic solvents (e.g. acetonitrile and methanol) led to poor product yields and/or low enantioselectivities. Most ILs and inorganic salts cause the deactivation of the hybrid catalyst except 0.2 M [BMIM][CF3COO] (95.4% ee and 93% yield) and 0.2 M [BMIM]Cl (93.7% ee and 89% yield). Several other additives have also been found to improve the catalytic efficiency of the DNA-based hybrid catalyst (control reaction without additive gives >99% ee and 87% yield): 0.4 M glycerol (>99% ee and 96% yield at 5 °C or 96.2% ee and 83% yield at room temperature), 0.2 M choline chloride/glycerol (1:2) (92.4% ee and 90% yield at 5 °C or 94.0% ee and 88% yield at room temperature), and 0.5 M dipropylene glycol dimethyl ether (>99% ee and 87% yield at room temperature). The use of some co-solvents/additives allows the Michael addition to be performed at a higher temperature (e.g. room temperature vs 5 °C) and a shorter reaction time (24 h vs 3 days). In addition, we found that a brief pre-sonication (5 min) of DNA in MOPS buffer prior to the reaction could improve the performance of the DNA-based hybrid catalyst. We have also shown that this DNA-based catalysis method is suitable for a variety of different substrates and relatively large-scale reactions. In conclusion, a judicious selection of benign co-solvents/additives could improve the catalytic efficiency of DNA-based hybrid catalyst.

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“…Consequently, deprotection is necessary to obtain a dipeptide. In contrast, aminopeptidase from Staphylococcus chromogenes was reported as useful for dipeptide synthesis in a one-step reaction (Yoshpe-Besancon et al 1993).…”

Section: Introductionmentioning

confidence: 97%

A mutant leucine aminopeptidase from Streptomyces cinnamoneus with enhanced l-aspartyl l-amino acid methyl ester synthetic activity

et al. 2012

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L-aspartyl L-amino acid methyl ester was synthesized using a mutant of a thermostable leucine aminopeptidase from Streptomyces cinnamoneus, D198 K SSAP, obtained in previously. A peptide of high-intensity sweetener, L-aspartyl-L-phenylalanine methyl ester, was selected as a model for demonstrating the synthesis of L-aspartyl L-amino acid methyl ester. The hydrolytic activities of D198 K SSAP toward L-aspartyl-L-phenylalanine and its methyl ester were, respectively, 74-fold and fourfold higher than those of wild type. Similarly, the initial rate of the enzyme for L-aspartyl-L-phenylalanine methyl ester synthesis was over fivefold higher than that of wild-type SSAP in 90% methanol (v/v) in a one-pot reaction. Furthermore, other L-aspartyl L-amino acid methyl esters were synthesized efficiently using D198 K SSAP. Results show that the substitution of Asp198 of SSAP with Lys is effective for synthesizing L-aspartyl L-amino acid methyl ester.

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Purification and characterization of an aminopeptidase A fromStaphylococcus chromogenesand its use for the synthesis of amino‐acid derivatives and dipeptides

Cited by 13 publications

References 30 publications

Glymes as versatile solvents for chemical reactions and processes: from the laboratory to industry

Glymes as versatile solvents for chemical reactions and processes: from the laboratory to industry

DNA-based asymmetric catalysis: role of ionic solvents and glymes

A mutant leucine aminopeptidase from Streptomyces cinnamoneus with enhanced l-aspartyl l-amino acid methyl ester synthetic activity

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