Improvement of thermal stability of β-galactosidase from Bacillus circulans by multipoint covalent immobilization in hierarchical macro-mesoporous silica

Bernal, Claudia; Sierra, Ligia; Mesa, Mónica

doi:10.1016/j.molcatb.2012.05.023

Cited by 65 publications

(52 citation statements)

References 24 publications

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“…The β–gal B. circulans has been immobilized by adsorption or covalent attachment in organic and inorganic supports . However, each technique has its own advantages and drawbacks, for example the high enzyme lixiviation by the adsorption pathway and the increase of the immobilization costs by covalent attachment due to the synthesis and functionalization of the supports before the immobilization process . Furthermore, in the case the immobilization on organic supports, the biocatalysts have low thermal and mechanic stability, low tolerance towards organic solvents and they are prone to microbial attack .…”

Section: Introductionmentioning

confidence: 99%

In situ immobilization of β‐galactosidase from Bacillus circulans in silica by sol‐gel process: Application in prebiotic synthesis

Escobar

Illanes

Wilson

et al. 2016

Engineering in Life Sciences

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In situ immobilization of β-galactosidase from Bacillus circulans in silica by sol-gel process: Application in prebiotic synthesisThe enzyme encapsulation is a very well-known stabilization pathway. However, there are some challenges in order to avoid the enzyme denaturation under encapsulation conditions. The β-galactosidase from Bacillus circulans was immobilized through sol-gel encapsulation route assisted by Triton X-100 surfactant and sugars. The effects of sugar presence in the immobilization process and the gelation time on the biocatalyst activity/stability were explained taking into account the characteristics of the formed silica matrix and the changes of the enzyme environment. The enzyme was effectively immobilized by this strategy, with high immobilization yield in terms of activity (29%) and expressed activity (47 IU/g). The immobilization through silica sol-gel in the presence of 1×10 −3 M Triton X-100 and fructose conferred 28.4-fold higher stability to the enzyme compared with the soluble form. This is an advantage for its use in the synthesis of the galacto-oligosaccharides at 50˚C. The total lactose conversion to galacto-oligosaccharides was 26%wt, which is comparable with that reported in the literature. The obtained biocatalyst is useful for the synthesis of galacto-oligosaccharides and its catalytic behavior is rationalized in this work. IntroductionThe β-galactosidase from Bacillus circulans is a hydrolase (E.C.

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Section: Introductionmentioning

confidence: 99%

In situ immobilization of β‐galactosidase from Bacillus circulans in silica by sol‐gel process: Application in prebiotic synthesis

Escobar

Illanes

Wilson

et al. 2016

Engineering in Life Sciences

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“…The best balance between these parameters is obtained when the silica modified with 1.0 mmol glyoxyl g −1 is used as support. The enzyme stiffening caused by covalent attachment in the supports with different activation degree explains the best thermal stability of the B. circulans β‐gal in this support . Multipoint attachment and stiffness increase as the glyoxyl content increases, improving IY and thermal stability (S‐Gx 1.0 ).…”

Section: Resultsmentioning

confidence: 97%

Design of β‐galactosidase/silica biocatalysts: Impact of the enzyme properties and immobilization pathways on their catalytic performance

Bernal

Sierra

Mesa

2013

Engineering in Life Sciences

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The use of heterogeneous biocatalysis in industrial applications is advantageous and the enzyme stability improvement is a continuous challenge. Therefore, we designed β‐galactosidase heterogeneous biocatalysts by immobilization, involving the support synthesis and enzyme selection (from Bacillus circulans, Kluyveromyces lactis, and Aspergillus oryzae). The underivatized, tailored, macro‐mesoporous silica exhibited high surface area, offered high enzyme immobilization yields and activity. Its chemical activation with glyoxyl groups bound the enzyme covalently, which suppressed lixiviation and conferred higher pH and thermal stability (120‐fold than for the soluble enzyme), without observable reduction of activity/stability due to the presence of silica. The best balance between the immobilization yield (68%), activity (48%), and stability was achieved for Bacillus circulans β‐galactosidase immobilized on glyoxyl‐activated silica, without using stabilizing agents or modifying the enzyme. The enzyme stabilization after immobilization in glyoxyl‐activated silica was similar to that observed in macroporous agarose‐glyoxyl support, with the reported microbiological and mechanical advantages of inorganic supports. The whey lactolysis at pH 6.0 and 25°C by using this catalyst (1 mg ml−1, 290 UI g−1) was still 90%, even after 10 cycles of 10 min, in batch process but it could be also implemented on continuous processes at industrial level with similar results.

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“…The inorganic materials with a controlled porous structure, for example, mesoporous silica, often give remarkable characteristics as support for enzyme immobilization based on a large surface area, chemical inertness, mechanical stability, and resistance against microbial contamination [24]. Bernal et al demonstrated that mesoporous silica activated with glyoxyl groups was suitable to immobilize and stabilize protein.…”

Section: Chemical Immobilization On Nanoscale Support Materialsmentioning

confidence: 99%

“…Finally, β-galactosidase was immobilized in the modified mesoporous silica by Schiff-base formation between glyoxyl groups in the support and neutral amino groups in the enzyme. The immobilized β-galactosidase exhibited a 370-fold higher stability than the free counterpart at pH 6 and 55 o C [24]. Recently, Khoobi et al reported the synthesis of functionalized polyethylenimine-grafted mesoporous silica spheres (MCM-41@PEI) for lipase immobilization.…”

Section: Chemical Immobilization On Nanoscale Support Materialsmentioning

confidence: 99%

Recent progress in nanobiocatalysis for enzyme immobilization and its application

Min

Yoo

2014

Biotechnol Bioproc E

146

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Recent advances in nanotechnology have provided various nanoscale materials that can be used as support for enzyme immobilization. Nanobiocatalysis integrating the biocatalyst and nanoscale materials is drawing great attention as innovative technology. Nanobiocatalysis could achieve not only a much higher enzyme loading capacity and a significantly enhanced mass transfer efficiency, but also unbelievable stabilization. In this review, we will present and discuss the recent progress in nanobiocatalysis and its applications in the fields of bioelectronics, bioconversion, and proteomics.

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Improvement of thermal stability of β-galactosidase from Bacillus circulans by multipoint covalent immobilization in hierarchical macro-mesoporous silica

Cited by 65 publications

References 24 publications

In situ immobilization of β‐galactosidase from Bacillus circulans in silica by sol‐gel process: Application in prebiotic synthesis

In situ immobilization of β‐galactosidase from Bacillus circulans in silica by sol‐gel process: Application in prebiotic synthesis

Design of β‐galactosidase/silica biocatalysts: Impact of the enzyme properties and immobilization pathways on their catalytic performance

Recent progress in nanobiocatalysis for enzyme immobilization and its application

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