Hydrolysis of whey lactose by immobilized β-Galactosidase

Mariotti, Marcela P.; Yamanaka, Hideko; Araújo, Ângela R.; Trevisan, Henrique C.

doi:10.1590/s1516-89132008000600019

Cited by 29 publications

(17 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These results demonstrate that the immobilization process was effective in maintaining the operational stability of the immobilized enzyme. Comparable results with b-galactosidase from A. oryzae immobilized in silica are reported by Mariotti et al [57] where the operational stability studies were carried out in packed bed reactor for a flow rate of 0.5 mL/min and the activity was reduced by 24 % after 130 days of operation. Klein et al [58] reported that b-galactosidase from K. lactis immobilized on chitosan [59].…”

Section: Reactor Operational Efficiencysupporting

confidence: 76%

Immobilization of β-galactosidase from Lactobacillus plantarum HF571129 on ZnO nanoparticles: characterization and lactose hydrolysis

Ethiraj

Mohanasrinivasan

Devi

et al. 2015

Bioprocess Biosyst Eng

View full text Add to dashboard Cite

β-Galactosidase from Lactobacillus plantarum HF571129 was immobilized on zinc oxide nanoparticles (ZnO NPs) using adsorption and cross-linking technique. Immobilized β-galactosidase showed broad-spectrum pH optima at pH 5-7.5 and temperature 50-60 °C. Fourier transform infrared spectroscopy (FTIR) and field emission scanning electron microscopy (FESEM) showed that β-galactosidase successfully immobilized onto supports. Due to the limited diffusion of high molecular weight substrate, K m of immobilized enzyme slightly increased from 6.64 to 10.22 mM, while V max increased from 147.5 to 192.4 µmol min(-1) mg(-1) as compared to the soluble enzyme. The cross-linked adsorbed enzyme retained 90 % activity after 1-month storage, while the native enzyme showed only 74 % activity under similar incubation conditions. The cross-linked β-galactosidase showed activity until the seventh cycle and maintained 88.02 % activity even after the third cycle. The activation energy of thermal deactivation from immobilized biocatalyst was 24.33 kcal/mol with a half-life of 130.78 min at 35 °C. The rate of lactose hydrolysis for batch and packed bed was found to be 0.023 and 0.04 min(-1).

show abstract

Section: Reactor Operational Efficiencysupporting

confidence: 76%

Immobilization of β-galactosidase from Lactobacillus plantarum HF571129 on ZnO nanoparticles: characterization and lactose hydrolysis

Ethiraj

Mohanasrinivasan

Devi

et al. 2015

Bioprocess Biosyst Eng

View full text Add to dashboard Cite

show abstract

“…The advantages of immobilized enzymes in respect to their free counterpart are well known. There are various methods for immobilization of enzyme ␤-galactosidase on different carriers -on the graphite surface with glutaraldehyde (GA) as cross-linking agent [2], on silica gel using GA [3], on Al 2 O 3 by physical adsorption [4] and est.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of β-galactosidase on modified polypropilene membranes

Vasileva

Iotov

Ivanov

et al. 2012

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

“…Also here, immobilization improved continuous lactose hydrolysis [7]. Accordingly, Mariotti et al [69] indicated that the stability and the hydrolysis activity of whey lactose by a silica-immobilized beta-galactosidase from A. oryzae within a continuous reactor process increased compared to non-immobilized systems. This study confirms the advanced performance of the immobilized enzyme at long-term processes.…”

Section: Advantages and Disadvantages Of Immobilized Enzymesmentioning

confidence: 70%

“…This study confirms the advanced performance of the immobilized enzyme at long-term processes. The halflife of the biocatalyst in a lactose solution at 40°C was estimated to be 12 months [69].…”

Section: Advantages and Disadvantages Of Immobilized Enzymesmentioning

confidence: 99%

Current enzymatic milk fermentation procedures

Beermann

Hartung

2012

Eur Food Res Technol

View full text Add to dashboard Cite

Aside from bacteria, yeasts and moulds, enzymes from animal, vegetal and microbial sources are increasingly utilized for milk fermentation providing a broad spectrum of innovative product conceptions. In order to alter texture and flavour or to improve the nutritional value of milk-based products from different animal milks, microbial and enzymatic fermentation procedures are traditionally established worldwide. To date, genomic and proteomic approaches enable new selection strategies for precise enzymes for modern product applications. Hereby, generating beneficial health ingredients from milk is a main aspect. New insights into the biochemical mechanisms of enzymatic digestion and genetic engineering lead to enzymes with exact defined functions for explicit ripening flavour development or the improvement of texture of fermented milk products. The ability to synthesize complex exo-polysaccharides or to release bioactive peptides by accurate proteolytic activities of enzymes or to enzymatically cross-link the protein matrix in order to modify the texture characteristics of fermented milk products is a raising facet, especially for specific pharma-or nutraceutical applications. This review aimed at discussing the recent research activities on milk fermentative enzymes, with focus on the broad spectrum of enzyme origins and current aspects of genetic engineering. New approaches on proteolytic, lipolytic, glycolytic as well as milk clotting and protein cross-linking enzymatic activities are examined and associated with possible product applications. From technical prospective, advantages and disadvantages of immobilized enzymes within milk fermentation processes are critically discussed.

show abstract

Hydrolysis of whey lactose by immobilized β-Galactosidase

Abstract: ABSTRACT

Cited by 29 publications

References 12 publications

Immobilization of β-galactosidase from Lactobacillus plantarum HF571129 on ZnO nanoparticles: characterization and lactose hydrolysis

Immobilization of β-galactosidase from Lactobacillus plantarum HF571129 on ZnO nanoparticles: characterization and lactose hydrolysis

Immobilization of β-galactosidase on modified polypropilene membranes

Current enzymatic milk fermentation procedures

Contact Info

Product

Resources

About