Thermal stabilization of fungal ?-glucosidase through glutaraldehyde crosslinking

Baker, John O.; Oh, K. K.; Grohmann, K.; Himmel, M. E.

doi:10.1007/bf01026159

Cited by 21 publications

(3 citation statements)

References 7 publications

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“…Purification of fungal b-glucosidase from novozyme 188 Fungal b-glucosidase was purified by the method of Baker et al 59 with slight modification. Novozyme 188 (15mls) was dialysed overnight against 0.1M phosphate buffer pH 6.5 and applied to a Q-sepharose column and protein was eluted with a 0-1M NaCl gradient.…”

Section: Methodsmentioning

confidence: 99%

Linker-free covalent thermophilic β-glucosidase functionalized polymeric surfaces

et al. 2011

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The surface immobilization of enzymes is important for many biomedical and industrial applications; however, the choice of enzyme and immobilization method for best performance is often difficult. This paper demonstrates that Plasma Immersion Ion Implantation (PIII) provides high enzyme coverage and rapid covalent attachment (within the first minute) of incubation, and shows how this can be used to control the composition of the attached layer from an enzyme mixture. The use of a thermophilic enzyme combined with covalent immobilization via PIII-treatment significantly improves b-glucosidase activity. b-glucosidase is an important rate-limiting enzyme in the production of cellulosic biofuel and is useful in many other industrial applications. b-glucosidase immobilized on the PIII-treated polystyrene surface demonstrated significant improvements in reaction rate and glucose yields compared to the enzyme on the untreated surface. A thermophilic b-glucosidase immobilized with our PIII-treatment method shows an average glucose production rate more than twenty-fold higher, over five uses, compared to the commercially-available b-glucosidase immobilized by physisorption after purification.

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Section: Methodsmentioning

confidence: 99%

Linker-free covalent thermophilic β-glucosidase functionalized polymeric surfaces

et al. 2011

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“…It reduced the reversible deactivation without any eŠect on the irreversible one. The crosslinking produced by this substance prevents normal unfolding of the enzyme, 18) however in this case the eŠect is somewhat lower than that of the additives.…”

mentioning

confidence: 91%

Thermal Inactivation and Product Inhibition ofAspergillus terreusCECT 2663 α-L-Rhamnosidase and Their Role on Hydrolysis of Naringin Solutions

Soria

Ellenrieder

2002

Bioscience, Biotechnology, and Biochemistry

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“…It has been reported previously that entrapped uncross-linked BG had a higher thermal stability than the free enzyme [32]. It is also known that glutaraldehyde treated BG has higher thermostability than the corresponding free BG [29,33]. These examples indicate that the IMBG was likely stabilized by molecular interactions, which is the most widely accepted mechanism for stabilization for glutaraldehyde cross-linked immobilized enzymes.…”

Section: Resultsmentioning

confidence: 93%

Enzymatic Cellulose Hydrolysis: Enzyme Reusability and Visualization of β-Glucosidase Immobilized in Calcium Alginate

Tsai

Meyer

2014

Molecules

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Abstract:The high cellulase enzyme dosages required for hydrolysis of cellulose is a major cost challenge in lignocellulosic ethanol production. One method to decrease the enzyme dosage and increase biocatalytic productivity is to re-use β-glucosidase (BG) via immobilization. In the present research, glutaraldehyde cross-linked BG was entrapped in calcium alginate gel particles. More than 60% of the enzyme activity could be recovered under optimized conditions, and glutaraldehyde cross-linking decreased leakage of BG from the calcium alginate particles. The immobilized BG aggregates were visualized by confocal laser scanning microscopy (CLSM). The CLSM images, which we believe are the first to be published, corroborate that more BG aggregates were entrapped in the matrix when the enzymes were cross-linked by glutaraldehyde as opposed to when they are not cross-linked. The particles with the immobilized BG were recycled for cellulase catalyzed hydrolysis of Avicel. No significant loss in BG activity was observed for up to 20 rounds of reaction recycle steps of the BG particles of 48 h each, verifying a significant stabilization of the BG by immobilization. Similar high glucose yields were obtained by one round of enzymatic hydrolysis of hydrothermally pretreated barley straw during a 72 h reaction with immobilized BG and free BG.

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Thermal stabilization of fungal ?-glucosidase through glutaraldehyde crosslinking

Cited by 21 publications

References 7 publications

Linker-free covalent thermophilic β-glucosidase functionalized polymeric surfaces

Linker-free covalent thermophilic β-glucosidase functionalized polymeric surfaces

Thermal Inactivation and Product Inhibition ofAspergillus terreusCECT 2663 α-L-Rhamnosidase and Their Role on Hydrolysis of Naringin Solutions

Enzymatic Cellulose Hydrolysis: Enzyme Reusability and Visualization of β-Glucosidase Immobilized in Calcium Alginate

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