Performance improvement of araujiain, a cystein phytoprotease, by immobilization within calcium alginate beads

Quiroga, Evelina; Illanes, Cristián Omar; Ochoa, Nelio Ariel; Barberis, S

doi:10.1016/j.procbio.2011.01.012

Cited by 50 publications

(36 citation statements)

References 30 publications

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Section: Process Of Immobilizationmentioning

confidence: 93%

“…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%

“…When araujiain is entrapped into alginate beads, 78% of the initial enzymatic activity is maintained after twenty cycles [25]. Thus, it was demonstrated better operational stability unlike to previous case or some examples in the literature where some entrapped enzymes in alginate show a minor possibility of reuse [25]. Comparing these results with those obtained when agarose was used as support, it can be concluded that the formation of araujiain-agarose covalent bonds improved the performance of the immobilized enzyme and allowed its use without loss of activity in successive cycles of hydrolytic reactions.…”

Section: Process Of Immobilizationmentioning

confidence: 99%

“…Among the immobilization methods available, multipoint covalent attachment is the most effective in terms of thermal stabilization [23], although gel-entrapped has also been reported to provides thermal stabilization [24,25].…”

Section: Introductionmentioning

confidence: 99%

“…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]. Although, it has been proved the remarkable enzymatic activity of araujiain immobilized on diverse supports, there are no studies in the literature reporting the multipoint covalent immobilization of 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: 93%

Section: Peptide Synthesis Catalyzed By Immobilized Araujiainmentioning

confidence: 99%

Section: Process Of Immobilizationmentioning

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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Carboxymethyl starch/alginate microspheres containing diamine oxidase for intestinal targeting

Blémur

Marcocci

et al. 2015

Biotech and App Biochem

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The association of carboxymethyl starch (CMS) and alginate is proposed as a novel matrix for the entrapment of bioactive agents in microspheres affording their protection against gastrointestinal degradation. In this study, the enzyme diamine oxidase (DAO) from white pea (Lathyrus sativus) was immobilized by inclusion in microspheres formed by ionotropic gelation of CMS/alginate by complexation with Ca2+. The association of CMS to alginate generated a more compact structure presenting a lesser porosity, thus decreasing the access of gastric fluid inside the microspheres and preventing the loss of entrapped enzyme. Moreover, the immobilized enzyme remained active and was able to oxidize the polyamine substrates even in the presence of degrading proteases of pancreatin. The inclusion yield in terms of entrapped protein was of about 82%–95%. The DAO entrapped in calcium CMS/alginate beads retained up to 70% of its initial activity in simulated gastric fluid (pH 2.0). In simulated intestinal fluid (pH 7.2) with pancreatin, an overall retention of 65% of activity for the immobilized DAO was observed over 24 H, whereas in similar conditions the free enzyme was totally inactivated. Our project proposes the vegetal DAO as an antihistaminic agent orally administered to treat food histaminosis and colon inflammation.

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Strawberry Protease as a Laundry Detergent Additive Candidate: Immobilization, Compatibility Study with Detergent Ingredients, and Washing Performance Test

Alici,

Arabaci

2023

Global Challenges

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The potential of strawberry‐derived protease as a component of laundry detergent is investigated. The compatibility of the enzyme with various surfactants, oxidizing agents, and commercial detergents is tested. The immobilized enzyme prepared by immobilizing Co2+ ions together with the enzyme is also tested. Strawberry crude protease shows high stability in the presence of surfactants frequently used in detergents. The enzyme is found to be relatively stable to oxidizing agents. In addition, it is determined that strawberry protease works in excellent compatibility with different commercial solid and liquid detergents in the Turkish market and also maintains its stability very well. Washing tests based on visual examination also reveal that the enzyme improves the washing performance of the tested detergent. All these properties and high activity at alkaline pH make this enzyme a very strong candidate for use in laundry detergent formulations.

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Performance improvement of araujiain, a cystein phytoprotease, by immobilization within calcium alginate beads

Cited by 50 publications

References 30 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

Carboxymethyl starch/alginate microspheres containing diamine oxidase for intestinal targeting

Strawberry Protease as a Laundry Detergent Additive Candidate: Immobilization, Compatibility Study with Detergent Ingredients, and Washing Performance Test

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