Improved biocatalysts based on Bacillus circulans β-galactosidase immobilized onto epoxy-activated acrylic supports: Applications in whey processing

Torres, Pedro; Batista‐Viera, Francisco

doi:10.1016/j.molcatb.2012.07.004

Cited by 36 publications

(37 citation statements)

References 37 publications

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“…Even though C‐EPI‐EPI 100 and Gx‐A have the same concentration of aldehydes groups, the SF obtained with C‐EPI‐EPI 100 was 3.8‐fold higher than the one achieved with its agarose counterpart. SF of C‐EPI‐EPI 100 biocatalyst was higher than values reported for the immobilization of B. circulans β‐galactosidase on acrylic resine and meso‐macroporous silica, both activated with short‐chain aliphatic aldehydes. These results highlight that chitosan activated with EPI in a two‐step process is a suitable carrier for obtaining a highly stable biocatalyst of immobilized B. circulans β‐galactosidase.…”

Section: Resultscontrasting

confidence: 62%

Influence of chitosan derivatization on its physicochemical characteristics and its use as enzyme support

Urrutia

Bernal

Escobar

et al. 2013

J of Applied Polymer Sci

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Chitosan was derivatized by two methodologies for analyzing their effect on chitosan physicochemical characteristics and its applicability as carrier for Bacillus circulans b-galactosidase immobilization. Glutaraldehyde (GA) and epichlorohydrin (EPI) were used for crosslinking and activation of chitosan, producing the corresponding supports (C-GA and C-EPI-EPI) after a one-step and a twostep process, respectively. The spherical shape and mean diameter of chitosan particles was not significantly affected by polymer derivatization, while Fourier transform infrared analysis showed that in both cases, chitosan polymer was chemically modified. TGA analysis indicated that C-EPI-EPI was the most thermally stable. The high degree of activation of C-EPI-EPI (586 lmol of aldehydes/g) resulted in the highest loss of activity during immobilization; hence a support with 100 lmol of aldehydes/g was produced (C-EPI-EPI 100 ). The highest expressed activity (89.3 IU/g) was obtained with the enzyme immobilized in C-GA, while the biocatalyst with highest thermal stability at 60 C was obtained with C-EPI-EPI 100 (half-life was 84-fold higher than the one of the soluble enzyme). The best compromise between biocatalyst expressed activity and thermal stability corresponded to b-galactosidase immobilized in C-EPI-EPI 100 . According to this study, chitosan derivatized with EPI is a thermally stable carrier appropriate for producing highly stable immobilized B. circulans b-galactosidase. V C 2013 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2014, 131, 40171.

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Section: Resultscontrasting

confidence: 62%

Influence of chitosan derivatization on its physicochemical characteristics and its use as enzyme support

Urrutia

Bernal

Escobar

et al. 2013

J of Applied Polymer Sci

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“…61 Table 3 shows the kinetic parameters of bgalactosidase immobilized in different materials. Pessela et al, 62 Torres and Batista-Viera, 63 Ansari et al, 38 and Ansari and Husain 64 observed the same behavior in relation to K M and V max . According to Matsuno et al, 65 mass transfer resistance and electrostatic and steric effects are the probable reasons for increased Michaelis constant after immobilization.…”

Section: Characterization Of Free and Immobilized B-galactosidasesmentioning

confidence: 74%

Modification of Immobead 150 support for protein immobilization: Effects on the properties of immobilized Aspergillus oryzae β‐galactosidase

Gennari

Mobayed

Rafael

et al. 2018

Biotechnology Progress

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We studied the modification of Immobead 150 support by either introducing aldehyde groups using glutaraldehyde (Immobead-Glu) or carboxyl groups through acid solution (Immobead-Ac) for enzyme immobilization by covalent attachment or ion exchange, respectively. These two types of immobilization were compared with the use of epoxy groups that are now provided on a commercial support. We used Aspergillus oryzae β-galactosidase (Gal) as a model protein, immobilizing it on unmodified (epoxy groups, Immobead-Epx) and modified supports. Immobilization yield and efficiency were tested as a function of protein loading (10-500 mg g support). Gal was efficiently immobilized on the Immobeads with an immobilization efficiency higher than 75% for almost all supports and protein loads. Immobilization yields significantly decreased when protein loadings were higher than 100 mg g support. Gal immobilized on Immobead-Glu and Immobead-Ac retained approximately 60% of its initial activity after 90 days of storage at 4°C. The three immobilized Gal derivatives presented higher half-lifes than the soluble enzyme, where the half-lifes were twice higher than the free Gal at 73°C. All the preparations were moderately operationally stable when tested in lactose solution, whey permeate, cheese whey, and skim milk, and retained approximately 50% of their initial activity after 20 cycles of hydrolyzing lactose solution. The modification of the support with glutaraldehyde provided the most stable derivative during cycling in cheese whey hydrolysis. Our results suggest that the Immobead 150 is a promising support for Gal immobilization. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:934-943, 2018.

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“…25,26 In addition, another difficulty in comparing the results of prior research is that enzymes from different sources have different microbial characteristics and properties.…”

Section: Figure 1 Contour Diagrams For the Immobilization Yield Basementioning

confidence: 99%

“…Moreover, because of the relatively high cost of Eupergit ® C, most of the studies involving this support used approximately 400 mg of Eupergit ® C. 9,25,26 Furthermore, β-galactosidase from yeast has a narrow working pH range, restricting this parameter to the previously studied range (pH between 6.5 and 7.5). In light of these findings, ionic strength is the most important variable to assess.…”

Section: Figure 1 Contour Diagrams For the Immobilization Yield Basementioning

confidence: 99%

A NEW APPROACH TO EVALUATE IMMOBILIZATION OF β-GALACTOSIDASE ON EUPERGIT^®C: STRUCTURAL, KINETIC, AND THERMAL CHARACTERIZATION

Braga¹,

Silva²,

Oliveira³

et al. 2014

Química Nova

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This study aimed to evaluate β-galactosidase immobilization. For this purpose, the ionic strength of the buffer, reaction time, amount of the immobilization support, and pH were evaluated by a central composite design. Assay 8, which consisted of 1.5 mol L −1 phosphate buffer (pH 7.5) and a reaction time of 2 h, produced the maximum yield. Eupergit ® C (400 mg) was subsequently used as an immobilization support. Immobilization kinetics wereinvestigated, and a significant increase in the yield was obtained after immobilization compared with that obtained from assay 8 (22.0 U mL −1 vs. 15.6 U mL −1). The enzyme efficiency of actuation was evaluated using o-nitrophenyl-β-d-galactopyranoside and lactose, with lactose providing better results. The reuse of β-galactosidase was evaluated, and more than 50% of the initial enzyme activity was maintained after five cycles of use. Enzyme characterization revealed that immobilization improved some aspects of the thermostability of β-galactosidase.

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Improved biocatalysts based on Bacillus circulans β-galactosidase immobilized onto epoxy-activated acrylic supports: Applications in whey processing

Cited by 36 publications

References 37 publications

Influence of chitosan derivatization on its physicochemical characteristics and its use as enzyme support

Influence of chitosan derivatization on its physicochemical characteristics and its use as enzyme support

Modification of Immobead 150 support for protein immobilization: Effects on the properties of immobilized Aspergillus oryzae β‐galactosidase

A NEW APPROACH TO EVALUATE IMMOBILIZATION OF β-GALACTOSIDASE ON EUPERGIT^®C: STRUCTURAL, KINETIC, AND THERMAL CHARACTERIZATION

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Improved biocatalysts based on Bacillus circulans β-galactosidase immobilized onto epoxy-activated acrylic supports: Applications in whey processing

Cited by 36 publications

References 37 publications

Influence of chitosan derivatization on its physicochemical characteristics and its use as enzyme support

Influence of chitosan derivatization on its physicochemical characteristics and its use as enzyme support

Modification of Immobead 150 support for protein immobilization: Effects on the properties of immobilized Aspergillus oryzae β‐galactosidase

A NEW APPROACH TO EVALUATE IMMOBILIZATION OF β-GALACTOSIDASE ON EUPERGIT®C: STRUCTURAL, KINETIC, AND THERMAL CHARACTERIZATION

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A NEW APPROACH TO EVALUATE IMMOBILIZATION OF β-GALACTOSIDASE ON EUPERGIT^®C: STRUCTURAL, KINETIC, AND THERMAL CHARACTERIZATION