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Journal ArticleDOI

hydrolysis of beta-galactosides using polymer-entrapped lactase: A study towards producing lactose-free milk.

Arne Dahlqvist, +2 more
- 01 Mar 1973 - 
- Vol. 15, Iss: 2, pp 395-402
TLDR
In this paper, a yeast lactase, Maxilact, was immobilized in crosslinked polyacrylamide using a bead-polymerization technique, and the polymer beads obtained, containing the entrapped enzyme, were used for the preparation of lactose-free milk.
Abstract
A yeast lactase, Maxilact, was immobilized in crosslinked polyacrylamide using a bead-polymerization technique. The polymer beads obtained, containing the entrapped enzyme, were used for the preparation of lactose-free milk. The binding yield of the enzyme and residual enzymic activity in the “enzyme beads” were studied as a function of the amounts of monomeric acrylamide and cysteine and bovine serum albumin present as protecting agents in the monomer-enzyme solution prior to polymerization. A maximum of about 75% of the enzyme could be immobilized using a 20% (w/v) solution of acrylamide plus N, N′-methylenebis-acrylamide, whereas the highest activity quotient (bound to free) of about 60% was observed on using a 25% solution. The presence of cysteine increased the activity by up to 30% and that of serum albumin up to about 15%.

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Citations
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Journal ArticleDOI

Beta‐galactosidase technology: A solution to the lactose problem

TL;DR: The enzyme can be used on a semi-continuous or continuous basis in bioreactors for large-scale reduction of lactose content of milk and other dairy products, and production of sweetener concentrates and food syrups.
Journal ArticleDOI

Kinetic Modeling of Lactose Hydrolysis by a β-Galactosidase from Kluyveromices Fragilis

TL;DR: The kinetic model of lactose hydrolysis by means of a commercial β-galactosidase from Kluyveromices fragilis provided by Novo nordisk has been determined using a wide range of the main variables: enzyme, substrate, and product concentrations and temperature.
Journal ArticleDOI

Beta-Galactosidase: Review of Recent Research Related to Technological Application, Nutritional Concerns, and Immobilization

TL;DR: The carbohydrase β -galactosidase is reviewed in this article, where a brief discussion of enzyme sources, isolation, purification, and assay techniques is presented, and potential commercial applications of lactose hydrolyzed products are described.
Journal Article

Beta-galactosidase: review of recent research related to technological application, nutritional concerns, and immobilization [Food science].

TL;DR: The carbohydrase β -galactosidase is reviewed, and various immobilized lactase systems are described in chronological order, and recent applications are discussed.
Journal ArticleDOI

Characterization of Galactosidases from Aspergillus niger: Purification of a Novel α-Galactosidase Activity

TL;DR: The existence of at least two different alpha-galactosidases in Aspergillus niger was confirmed, with one of them showing synergism with beta-mannanase and the other with a different mass after deglycosylation with N-glycanase F.
References
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