Preparation and Application of Immobilized β-Galactosidase of Saccharomyces Lactis

Woychik, J.H.; Wondolowski, M. V.; Dahl, K. J.

doi:10.1007/978-1-4684-2088-3_3

Cited by 11 publications

(4 citation statements)

References 2 publications

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“…The estimated space-time (ratio of the volume occupied by the milk to the volumetric flow rate) was less than 3 min, and 7 min for the 3 L/h and 1.5 L/h flow rates, respectively. The estimated capacity of lactose hydrolysis, defined as grams of hydrolized lactose per gram of immobilized-enzyme microbeads per hour, at 340C and 3 L/h flow rate was similar to the estimated capacity of the enzyme immobilized on collagen (Woychik, et al, 1973).…”

Section: And Discussionmentioning

confidence: 70%

Lactose hydrolysis by immobilized ?-galactosidase on nylon-6: A novel spin-basket reactor

et al. 1993

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Section: And Discussionmentioning

confidence: 70%

Lactose hydrolysis by immobilized ?-galactosidase on nylon-6: A novel spin-basket reactor

et al. 1993

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“…The maximal velocities for both the soluble and immobilized lactase were not significantly different. Galactose, one of the monosaccharides resulting from the hydrolysis of lactose by lactase, has been reported to act as a competitive inhibitor for lactase (Woychik et al 1974). Therefore, the inhibition of lactase activity by galactose was tested by increasing the concentrations of galactose in the assay mixture.…”

Section: Kinetic Studiesmentioning

confidence: 99%

The Kinetic Properties of Lactase, Papain and Lipase Immobilized on a Single Support

Kilara¹,

Shahani²,

Wagner

1978

J Food Biochemistry

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Lactase, papain and lipase enzymes were immobilized concomitantly on derivatized Sepharose 4‐B. Equal molar concentrations of each enzyme were allowed to react with activated Sepharose and a preferential binding of lipase and papain over lactase was observed. This preferential binding was explained by differences in diffusion rates of enzymes resulting in greater availability of binding sites within the beads to certain enzyme species. The effects of pH of assay, temperature of assay and substrate concentrations on each individual enzyme were determined. Soluble forms of each enzyme were used for comparison. There were some differences in pH and temperature optima for the immobilized enzymes. However, the affinity of the enzymes for their substrates was substantially the same.

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“…1973a,b; Ostergaard and Martiny 1973;Paine and Carlsonell 1975;Reagan et al 1974;Wondolowski and Woychik 1974), fungal ; Coughlin and Charles 1976;Coughlin et al 1974;Hasselberger e t al. 1974;Hyrkas et al 1976; Okos and Harper 1974;Okos et al 1978; Olson and Stanley 1973;Paruchuri 1976;Pitcher et al 1976;Weetall et al 1974a,b;Wierzbicki et al 1973;Woychik and Wondolowski 1972;, and yeast (Dahlquist et al 1973;Kilara et al 1977; Pastore e t 1976;Woychik et al 1974) sources have previously been immobilized on a number of support materials and used in the hydrolysis of lactose present in different solutions. A fungal lactase derived from A. n i g e r was used in this research.…”

Section: Introductionmentioning

confidence: 99%

Use of Immobilized Lactase in Processing Cheese Whey Ultrafiltrate

Roodpeyma

Hill

Amundson

1983

J Food Process Engineering

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Enzymatic hydrolysis of lactose in cottage cheese whey ultrafiltrate was investigated. Lactase of A. niger was immobilized on an alumina‐silica catalyst support by the linking agent tolylene‐2, 4‐diisocyanate. The resulting immobilized enzyme preparation had an activity of 3 standard international units of lactase per gram at pH 4 and 37 °C. The optimum pH and temperature for hydrolysis of lactose by immobilized lactase were 3.5 and 50°C, respectively. Immobilization of the enzyme resulted in reductions of 1.1 pH units and 15°C in optimum pH and temperature, respectively. The two constants of the simple Michaelis‐Menten rate expression were obtained from Lineweaver‐Burk plots of the initial reaction rate data obtained at 37°C. Estimated values for Vmax and the apparent Km were 7.8 (μmoles/min‐g) and 0.26 (M), respectively. Inhibition by the product galactose was measured by studying the hydrolysis reaction in a batch reactor. The inhibition constant Ki was estimated from batch reactor data to be 0.005 and 0.053 (M) at 35 and 50°C, respectively. Activation energies of 8.1 and 6.4 (kcal/gmole) were obtained for the immobilized and soluble enzyme reactions, respectively. The behavior of the batch reactor as measured in terms of a plot of conversion versus time was essentially the same for both conventional and deionized whey ultrafiltrate.

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Preparation and Application of Immobilized β-Galactosidase of Saccharomyces Lactis

Cited by 11 publications

References 2 publications

Lactose hydrolysis by immobilized ?-galactosidase on nylon-6: A novel spin-basket reactor

Lactose hydrolysis by immobilized ?-galactosidase on nylon-6: A novel spin-basket reactor

The Kinetic Properties of Lactase, Papain and Lipase Immobilized on a Single Support

Use of Immobilized Lactase in Processing Cheese Whey Ultrafiltrate

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