A comparison of different methods of β-galactosidase immobilization

Bódalo, A.; Gómez, E.; Gómez, José L.; Bastida, Jaume; Máximo, M.F.; Diaz, Franchesca

doi:10.1016/0032-9592(91)85025-j

Cited by 48 publications

(27 citation statements)

References 12 publications

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“…Dierent con®gurations of the immobilized enzyme reactor have been advanced for the hydrolysis of lactose in whey or milk, both in research and industry (Bakken et al, 1989(Bakken et al, , 1990(Bakken et al, , 1992Baret, 1987;BoÂ dalo et al, 1991;Dohan et al, 1980;Gekas and LoÂ pez-Leiva, 1985;Greenberg and Mahon-ey, 1981;Mahoney, 1985;Peterson et al, 1989;Pitcher et al, 1976;Pivarnik et al, 1995;Richmond et al, 1981;Van Griethuysen-Dilber et al, 1988). Of the carrier/ enzyme pairs described, none is ideal for commercial practice in regard to technological or economic criteria, and, therefore, new supports with speci®cally tailored properties and improved``lactases'' continue to appear in the literature.…”

Section: Immobilized Enzyme Reactors For Lactose Conversionmentioning

confidence: 97%

Development of an ultrahigh‐temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable β‐glycosidases and optimization of a packed‐bed reactor for lactose conversion

Petzelbauer

Kühn

Splechtna

et al. 2002

Biotech & Bioengineering

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Recombinant hyperthermostable beta-glycosidases from the archaea Sulfolobus solfataricus (Ss beta Gly) and Pyrococcus furiosus (CelB) were covalently attached onto the insoluble carriers chitosan, controlled pore glass (CPG), and Eupergit C. For each enzyme/carrier pair, the protein-binding capacity, the immobilization yield, the pH profiles for activity and stability, the activity/temperature profile, and the kinetic constants for lactose hydrolysis at 70 degrees C were determined. Eupergit C was best among the carriers in regard to retention of native-like activity and stability of Ss beta Gly and CelB over the pH range 3.0-7.5. Its protein binding capacity of approximately 0.003 (on a mass basis) was one-third times that of CPG, while immobilization yields were typically 80% in each case. Activation energies for lactose conversion by the immobilized enzymes at pH 5.5 were in the range 50-60 kJ/mol. This is compared to values of approximately 75 kJ/mol for the free enzymes. Immobilization expands the useful pH range for CelB and Ss beta Gly by approximately 1.5 pH units toward pH 3.5 and pH 4.5, respectively. A packed-bed enzyme reactor was developed for the continuous conversion of lactose in different media, including whey and milk, and operated over extended reaction times of up to 14 days. The productivities of the Eupergit C-immobilized enzyme reactor were determined at dilution rates between 1 and 12 h(-1), and using 45 and 170 g/L initial lactose. Results of kinetic modeling for the same reactor, assuming plug flow and steady state, suggest the presence of mass-transfer limitation of the reaction rate under the conditions used. Formation of galacto-oligosaccharides in the continuous packed-bed reactor and in the batch reactor using free enzyme was closely similar in regard to yield and individual saccharide components produced.

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Section: Immobilized Enzyme Reactors For Lactose Conversionmentioning

confidence: 97%

Development of an ultrahigh‐temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable β‐glycosidases and optimization of a packed‐bed reactor for lactose conversion

Petzelbauer

Kühn

Splechtna

et al. 2002

Biotech & Bioengineering

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“…Numbers of other supports for adsorption of β-galactosidase were tested; e.g. adsorption on celite (Gaur et al 2006), on zeolite pellets (Poletto et al 2005), on hydrophobic cotton cloth (Sharma & Yamazaki 1984), on chromosorb W (Bodalo et al 1991), etc.…”

Section: Immobilisation Of β-Galactosidasementioning

confidence: 99%

Perspectives and applications of immobilised β-galactosidase in food industry - a review

Grosová¹,

Rosenberg²,

Rebroš³

2008

Czech J. Food Sci.

116

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Grosová Z., Rosenberg M., Rebroš M. (2008): Perspectives and applications of immobilised β-galactosidase in food industry -a review. Czech J. Food Sci., 26: 1-14.β-Galactosidase is an important industrial enzyme in the hydrolysis of milk and whey lactose. The enzymatic hydrolysis of lactose allows to avoid health and environmental problems posed by this disaccharide. In addition, this enzyme catalyses the formation of galacto-oligosaccharides, which are prebiotic additives for the so-called "healthy foods". β-Galactosidase is one of the relatively few enzymes that have been used in large-scale processes in both free and immobilised forms. This article presents a review of recent trends in immobilisation of β-galactosidase and their application in food industry.

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“…Our research group has wide experience in enzyme immobilization on this support [29], which has also been used for phenol removal [30]. One of the immobilized derivatives and the corresponding free enzyme were tested for the inactivation by both substrates in order to demonstrate that immobilization prevents peroxidase inactivation.…”

Section: Introductionmentioning

confidence: 99%

A comparative study of free and immobilized soybean and horseradish peroxidases for 4-chlorophenol removal: protective effects of immobilization

Bódalo

Bastida

Máximo

et al. 2008

Bioprocess Biosyst Eng

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Horseradish peroxidase (HRP) and soybean peroxidase (SBP) were covalently immobilized onto aldehyde glass through their amine groups. The activity yield and the protein content for the immobilized SBP were higher than for the immobilized HRP. When free and immobilized peroxidases were tested for their ability to remove 4-chlorophenol from aqueous solutions, the removal percentages were higher with immobilized HRP than with free HRP, whereas immobilized SBP needs more enzyme to reach the same conversion than free enzyme. In the present paper the two immobilized derivatives are compared. It was found that at an immobilized enzyme concentration in the reactor of 15 mg l(-1), SBP removed 5% more of 4-chlorophenol than HRP, and that a shorter treatment was necessary. Since immobilized SBP was less susceptible to inactivation than HRP and provided higher 4-chlorophenol elimination, this derivative was chosen for further inactivation studies. The protective effect of the immobilization against the enzyme inactivation by hydrogen peroxide was demonstrated.

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A comparison of different methods of β-galactosidase immobilization

Cited by 48 publications

References 12 publications

Development of an ultrahigh‐temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable β‐glycosidases and optimization of a packed‐bed reactor for lactose conversion

Development of an ultrahigh‐temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable β‐glycosidases and optimization of a packed‐bed reactor for lactose conversion

Perspectives and applications of immobilised β-galactosidase in food industry - a review

A comparative study of free and immobilized soybean and horseradish peroxidases for 4-chlorophenol removal: protective effects of immobilization

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