Peptide synthesis in aqueous–organic media catalyzed by proteases from latex of Araujia hortorum (Asclepiadaceae) fruits

Quiroga, Evelina; Priolo, Nora; Obregón, David; Marchese, José Abramo; Barberis, S

doi:10.1016/j.bej.2007.08.020

Cited by 22 publications

(24 citation statements)

References 38 publications

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“…The total protein content of araujiain was 5.4 mg protein/mL and the specific activity was 12.8 Ucas/ mg protein (68.4 Ucas/mL araujiain) when casein was used as substrate. Previous studies of Priolo and Obregón [9] reveal the presence of three fractions with proteolytic activity contained in this enzymatic extract [26,28]. Such fractions (called araujiain hI, hII and hIII) have synergistic activity and show better performance at different pH and temperatures in the proteolytic extract that when each working alone and isolated.…”

Section: Process Of Immobilizationmentioning

confidence: 99%

“…Enzymatic peptide synthesis catalyzed by immobilized araujiain was carried out in an aqueous-organic medium formed by Tris-HCl buffer (0.1 M, pH 8.5) and ethyl acetate at 1:1 ratio, according to conditions established in previous studies [9,25]. The condensation reaction was initiated by mixing the aqueous phase containing the immobilized enzyme (2.1 IU/g carrier) and 4mM Phe-OMe as amino component, with the organic phase containing the carboxylic component (Z-Ala or Z-Ala-pNo).…”

Section: Peptide Synthesis Catalyzed By Immobilized Araujiainmentioning

confidence: 99%

“…N,N-dimethylformamide (with low water content) and mixtures of the Tris-HCl buffer (0.1 M, pH 8.5) and hexane, ethyl acetate or propanone in 50:50 ratio were selected to perform the peptide synthesis catalyzed by araujiain. The maximum conversion (35%) was obtained using ethyl acetate as organic medium [9]. In later work, araujiain was immobilized on diverse supports: i) deposited onto polyamide araujiain demonstrated to be good catalyst for the condensation of coded and non-coded Cbz-amino acids and amines such as amino alcohols and amino acetals in acetonitrile containing 1% (v/v) water [13]; ii) the use of titanium dioxide as support for the immobilization of araujiain led to an immobilized biocatalyst with a high protein concentration but with partial deactivation with respect to the native enzyme [29]; iii) entrapped within alginate beads araujiain showed good performance in the peptide synthesis using aqueous-organic media and a secondary structure with a high α-helical character was responsible for the highest activity of entrapped araujiain [25,30].…”

Section: Introductionmentioning

confidence: 99%

“…In particular, alkaline proteases have applications in leather processing [3], laundry detergents [4], production of protein hydrolysates [5] and food processing [6][7][8]. The recent application of proteases to the production of certain peptides and peptides derivatives has received great attention as a viable alternative to the chemical approach [9][10][11][12][13]. This wide range of applications insures proteases the first place in the world market of enzymes.…”

Section: Introductionmentioning

confidence: 99%

“…This enzymatic preparation consisting on three papain-like cysteine peptidases was obtained from the latex of Araujia hortorum fruits (a climbing plant that grows in Brazil, Paraguay, Uruguay and Argentina) [26][27][28]. Araujiain has been demonstrated to be a successful biocatalyst for the synthesis of amide bonds in aqueous-organic media [9]. N,N-dimethylformamide (with low water content) and mixtures of the Tris-HCl buffer (0.1 M, pH 8.5) and hexane, ethyl acetate or propanone in 50:50 ratio were selected to perform the peptide synthesis catalyzed by araujiain.…”

Section: Introductionmentioning

confidence: 99%

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A Highly Stable Biocatalyst Obtained from Covalent Immobilization of a Non-Commercial Cysteine Phytoprotease

Ceccacci¹

2015

J Bioprocess Biotech

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In this work, araujiain (enzymatic preparation obtained from the latex of Araujia hortorum fruits) was successfully immobilized on glyoxyl-agarose via multipoint covalent attachment. Thus, good efficiency of immobilization and high operational stability of immobilized enzyme were obtained. The activity of araujiain at alkaline pH was significantly improved after immobilization. In addition, immobilized araujiain also showed high activity and good stability, without significant loss in its activity, at temperatures between 37 and 60°C and in the presence of immiscible organic solvents. Immobilized araujiain also showed good performance in a mixture of 50% ethyl acetate in buffer, used for peptide synthesis, with better results than when the free enzyme was used as catalyst. These results indicate that immobilized araujiain via multipoint covalent attachment can be highly stabilized and this method might be used for practical applications of araujiain in hydrolytic and synthetic processes.

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Section: Process Of Immobilizationmentioning

confidence: 99%

Section: Peptide Synthesis Catalyzed By Immobilized Araujiainmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

A Highly Stable Biocatalyst Obtained from Covalent Immobilization of a Non-Commercial Cysteine Phytoprotease

Ceccacci¹

2015

J Bioprocess Biotech

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Proteases as Powerful Catalysts for Organic Synthesis

Illanes

Guzmán

Barberis

2009

Amino Acids, Peptides and Proteins in Organic Chemistry

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Enzyme‐Catalyzed Synthesis of Polyamides and Polypeptides

Cheng

2010

Biocatalysis in Polymer Chemistry

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IntroductionThe synthesis of polypeptides and polyamides by chemical means is well known and well established [1 -4] . Nevertheless, there have been substantial efforts to use enzymes as catalysts for these reactions [5] . The motivation is to fi nd improved processes that are more environmentally friendly and that involve lower reaction temperatures, thereby decreasing energy usage. In general, enzymatic catalysis entails milder reaction conditions but can be more diffi cult for the synthesis of high -molecular -weight polymers. However, several promising reports have recently appeared. This review will be confi ned to the synthesis of polyamides and polypeptides using enzymes that are commercially available or isolated from appropriate organisms. Thus, production of proteins in vivo and in cell -free extracts is not covered, nor are polyesters and poly(ester -amides).Prior to 2000 enzymatic methods for polyamides and polypeptides have mostly been used for the synthesis of oligomers (with degree of polymerization , DP , about 2 -8) and condensation of large protein fragments. After 2000, several articles have appeared that reported the synthesis of higher -molecular -weight polymers. This fi eld is evolving, with new approaches and new methodologies still being developed.Three general approaches involving isolated enzymes have been used for polyamide or polypeptide synthesis. The fi rst approach uses protease and other proteolytic enzymes. The second approach uses lipases and esterases. These two approaches account for most of the papers in the literature. The proteases and the lipases used tend to have relatively broad substrate specifi city and can be applied to the synthesis of different types of polyamides and polypeptides. The third approach includes enzymes other than proteases and lipases. For example, in protein synthesis there has been much research into the use of cell -free extracts to produce proteins in vivo . In a few cases, the enzyme(s) responsible for the synthesis have been isolated and used to produce the same or similar proteins in vitro . Selected publications have been included in this review.

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Peptide synthesis in aqueous–organic media catalyzed by proteases from latex of Araujia hortorum (Asclepiadaceae) fruits

Cited by 22 publications

References 38 publications

A Highly Stable Biocatalyst Obtained from Covalent Immobilization of a Non-Commercial Cysteine Phytoprotease

A Highly Stable Biocatalyst Obtained from Covalent Immobilization of a Non-Commercial Cysteine Phytoprotease

Proteases as Powerful Catalysts for Organic Synthesis

Enzyme‐Catalyzed Synthesis of Polyamides and Polypeptides

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