Immobilization of Sporothrix schenckii 1099-18 exo-polygalacturonase in magnetic mesoporous silica yolk-shell spheres: Highly reusable biocatalysts for apple juice clarification

Karataş, Ersin; Tülek, Ahmet; Yıldırım, Deniz; Tamtürk, Faruk; Bi̇nay, Barış

doi:10.1016/j.fbio.2021.101324

Cited by 10 publications

(3 citation statements)

References 53 publications

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“…A heterologously expressed exo-polygalacturonase from Sporothrix schenckii was purified and immobilized on yolk-shellstructured magnetic mesoporous silica using the encapsulation and cross-linking methods, respectively. The two resulting magnetic immobilized enzymes (silica@Fe 3 O 4 /SsExo-PG and silica@Glu-Fe 3 O 4 /SsExo-PG) were further used for apple juice clarification [103]. The turbidity of the apple juice was reduced by 82% after a 1 h treatment for both biocatalysts and the immobilized enzyme retained 80% and 90% of its initial activity after 10 consecutive applications, respectively.…”

Section: Other Enzymesmentioning

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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Section: Other Enzymesmentioning

confidence: 99%

Application of Immobilized Enzymes in Juice Clarification

Wang,

Xu,

Wang

et al. 2023

Foods

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“…[2][3][4][5] Furthermore, enzyme immobilization enables industrial-scale use of enzymes, reduces operational cost, and prevents product contamination with proteins. 6,7 A series of immobilization techniques have been successfully developed including physical adsorption, covalent coupling, and entrapment in solid matrices. 8,9 Among them, the covalent enzyme immobilization has been proved to be more effective, leading to a more stable biocatalyst.…”

Section: Introductionmentioning

confidence: 99%

“…Enzyme immobilization is one of the most popular methods to permit the simple reuse of enzymes and modulation of the catalytic properties of enzyme such as specificity, selectivity, resistance to inhibitions, and organic solvents 2–5 . Furthermore, enzyme immobilization enables industrial‐scale use of enzymes, reduces operational cost, and prevents product contamination with proteins 6,7 . A series of immobilization techniques have been successfully developed including physical adsorption, covalent coupling, and entrapment in solid matrices 8,9 .…”

Section: Introductionmentioning

confidence: 99%

Effective immobilization of lactate dehydrogenase onto mesoporous silica

Alagöz

Toprak

Varan

et al. 2022

Biotech and App Biochem

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This study presents that covalent immobilization technique has been utilized for the immobilization of l-lactate dehydrogenase (l-LDH) from porcine on mesoporous silica. To develop mesoporous silica as support material for use in l-LDH immobilization, the particle surfaces were functionalized with 3aminopropyltrimethoxysilane and further conjugated with glutaraldehyde. The effect of some parameters such as glutaraldehyde concentration, immobilization pH, initial enzyme concentration, and immobilization time was investigated and the optimum conditions for these parameters were determined as 1% (w/v), pH 8.0, 1 mg/ml, and 120 min, respectively. The maximum working pH and temperature for the oxidation of lactate to pyruvate reaction were determined as 10.0 and 35 • C for free and 9.0 and 40 • C for immobilized l-LDH, respectively. The kinetic parameters (K m and V max ) of l-LDH for the oxidation of lactate to pyruvate reaction were examined as 1.02 mM and 7.58 U/mg protein for free and 0.635 mM and 1.7 U/mg protein for immobilized l-LDH, respectively. Moreover, the immobilized l-LDH was 1.3-fold more stable than free l-LDH at 25 • C according to calculated t 1/2 values. The immobilized l-LDH retained 80% of its initial activity in a batch reactor after 14 reuses.

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