Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose
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چکیده
منابع مشابه
Bioaffinity Based Immobilization of Almond (Amygdalus communis) b-galactosidase on Con A-layered Calcium Alginate-cellulose Beads: Its Application in Lactose Hydrolysis in Batch and Continuous Mode
In this study, immobilization of partially purified almond (Amygdalus communis) β-galactosidase on Con A layered calcium alginate-cellulose beads was investigated. Immobilized β-galactosidase retained 72% of theinitial activity after crosslinking by glutaraldehyde. Both soluble and immobilized enzyme exhibited the samepH and temperature optima at pH 5.5 and 50ºC, respectively. Howev...
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This work aimed at evaluating the influence of enzyme concentration, temperature, and reaction time in the lactose hydrolysis process in milk, cheese whey, and whey permeate, using two commercial β-galactosidases of microbial origins. We used Aspergillus oryzae (at temperatures of 10 and 55°C) and Kluyveromyces lactis (at temperatures of 10 and 37°C) β-galactosidases, both in 3, 6, and 9 U/mL c...
متن کاملRegulation of lactose transport in Kluyveromyces lactis
Kluyveromyces lactis is able to ferment lactose and it is considered as an alternative model for biochemical, physiological and genetic studies in nonSaccharomyces yeasts. Understanding the mechanisms of lactose uptake and the regulation involved in the transport is an important step towards better biotechnological applications. The transport of lactose in K. lactis is mediated by a membrane pe...
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The present study demonstrates the immobilization of Aspergillus oryzae β-galactosidase on cellulose acetate-polymethylmethacrylate (CA-PMMA) membrane and its application in hydrolyzing lactose in dairy industries. The effect of physical and chemical denaturants like pH, temperature, product inhibition by galactose, storage stability, and reuse number of the enzyme immobilized on CA-PMMA membra...
متن کاملA new kinetic model proposed for enzymatic hydrolysis of lactose by a -galactosidase from Kluyveromyces fragilis
We study the enzymatic hydrolysis of lactose by a commercial enzyme from a selected strain of Kluyveromyces fragilis. The variables analyzed were: temperature (25–40 ◦C), enzyme concentration (0.1–3.0 g l−1), lactose concentration (0.0278–0.208 M), and initial galactose concentration (0.0347 M). On the basis of the data analyzed, both published and in the present work, we propose a Michaelis–Me...
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ژورنال
عنوان ژورنال: Ciência Rural
سال: 2016
ISSN: 0103-8478
DOI: 10.1590/0103-8478cr20150833