Stabilization by multipoint covalent attachment of a biocatalyst with polygalacturonase activity used for juice clarification

Tapias, Yuly A. Ramírez; Rivero, Cintia W.; López‐Gallego, Fernando; Guisán, José M.; Trelles, Jorge A.

doi:10.1016/j.foodchem.2016.03.086

Cited by 18 publications

(6 citation statements)

References 18 publications

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“…This treatment generates aldehyde groups on HRP sugar residues that could form Schiff´s bases with amino groups of the PEI used as a catalyst for the Si deposition. Similar to the chemistry used to immobilize proteins on glyoxyl activated supports [40], a further reducing step via Na 2 BH 4 , would transform the first reversible interaction between the enzyme and the matrix into a three dimensional multiple covalent attachment of HRP within the Si particles Fig 1. The strategy was followed in the presence of trehalose, a common additive used to gain protein stability [12].…”

Section: Resultsmentioning

confidence: 99%

Design of stable magnetic hybrid nanoparticles of Si-entrapped HRP

et al. 2019

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Hybrid and composite nanoparticles represent an attractive material for enzyme integration due to possible synergic advantages of the structural builders in the properties of the nanobiocatalyst. In this study, we report the synthesis of a new stable hybrid nanobiocatalyst formed by biomimetic silica (Si) nanoparticles entrapping both Horseradish Peroxidase (HRP) (EC 1.11.1.7) and magnetic nanoparticles (MNPs). We have demonstrated that tailoring of the synthetic reagents and post immobilization treatments greatly impacted physical and biocatalytic properties such as an unprecedented ~280 times increase in the half-life time in thermal stability experiments. The optimized nanohybrid biocatalyst that showed superparamagnetic behaviour, was effective in the batch conversion of indole-3-acetic acid, a prodrug used in Direct Enzyme Prodrug Therapy (DEPT). Our system, that was not cytotoxic per se , showed enhanced cytotoxic activity in the presence of the prodrug towards HCT-116, a colorectal cancer cell line. The strategy developed proved to be effective in obtaining a stabilized nanobiocatalyst combining three different organic/inorganic materials with potential in DEPT and other biotechnological applications.

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Section: Resultsmentioning

confidence: 99%

Design of stable magnetic hybrid nanoparticles of Si-entrapped HRP

et al. 2019

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“…Pectin is the third structural polysaccharide found in the primary cell wall and middle lamella of plants. It contributes to plant firmness and structure and consists mainly of linear chains of 1,4-a-D-galacturonic acids, which are partially methyl-or acetyl-esterified (Dam asio et al 2010;Tapias et al 2016). The pectin present in fruits and vegetables remains in the pulp during the extraction of the juice, causing turbidity.…”

Section: Introductionmentioning

confidence: 99%

Biotechnological potential of an exo‐polygalacturonase of the new strain Penicillium janthinellum VI2R3M: biochemical characterization and clarification of fruit juices

et al. 2019

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Aims The aim of this work was to characterize and apply a polygalacturonase of Penicillium janthinellum new strain VI2R3M. Methods and Results The polygalacturonase obtained from P. janthinellum VI2R3M was incubated in cultures of passion fruit peel and was partially purified by ion‐exchange chromatography and gel filtration. The enzyme showed a relative molecular mass of 102·0 kDa, maximum activity at pH 5·0, temperature of 50°C, 100% stablity at 50°C and 80% stablity at pH 3·0–5·0. The apparent Km, Vmax and Kcat values for hydrolyzing polygalacturonic acid were 2·56 mg ml−1, 163·1 U mg−1 and 277 s−1 respectively. The polygalacturonase presented exo activity and was activated by Mg2+. The juices treated with polygalacturonase presented increases in transmittance with reduction in colour. Conclusions The results suggest that the new lineage P. janthinellum VI2R3M presents a high yield of an exo‐polygalacturonase induced by agro‐industrial residues, with excellent activity and stability in acidic pH and at 50°C. Significance and Impact of the Study The use of agro‐industrial residue to obtain the polygalacturonase can contribute to a decrease enzyme production cost. The results of the activity, stability to acidic pH and excellent performance in the clarification of juices show that the enzyme is promising for industrial application.

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“…The immobilized xylanase retained about 50% of its initial activity after nine cycles of juice clarification [56]. Fe 3 O 4 @SiO 2 nanoparticles were prepared as supports for the immobilization of xylanase (from Thermomyces lanuginosus, ≥2500 units/g); the immobilized xylanase retained about 55% of its initial activity even after 10 clarification reactions in concentrated fruit juice [71]. A crude enzyme mixture (protein content: 1.175 ± 0.032 mg/mL) containing cellulase (3.96 ± 0.32 U/mg protein), pectinase (3.31 ± 0.24 U/mg protein), and xylanase (2.90 ± 0.12 U/mg protein) was produced with Aspergillus niger and was immobilized on magnetic nanoparticles (MNPs) by cross-linking them with glutaraldehyde.…”

Section: Xylanasementioning

confidence: 99%

Application of Immobilized Enzymes in Juice Clarification

Wang,

Xu,

Wang

et al. 2023

Foods

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Immobilized enzymes are currently being rapidly developed and are widely used in juice clarification. Immobilized enzymes have many advantages, and they show great advantages in juice clarification. The commonly used methods for immobilizing enzymes include adsorption, entrapment, covalent bonding, and cross-linking. Different immobilization methods are adopted for different enzymes to accommodate their different characteristics. This article systematically reviews the methods of enzyme immobilization and the use of immobilized supports in juice clarification. In addition, the mechanisms and effects of clarification with immobilized pectinase, immobilized laccase, and immobilized xylanase in fruit juice are elaborated upon. Furthermore, suggestions and prospects are provided for future studies in this area.

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Stabilization by multipoint covalent attachment of a biocatalyst with polygalacturonase activity used for juice clarification

Cited by 18 publications

References 18 publications

Design of stable magnetic hybrid nanoparticles of Si-entrapped HRP

Design of stable magnetic hybrid nanoparticles of Si-entrapped HRP

Biotechnological potential of an exo‐polygalacturonase of the new strain Penicillium janthinellum VI2R3M: biochemical characterization and clarification of fruit juices

Application of Immobilized Enzymes in Juice Clarification

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