β-Galactosidase Immobilization on Chitosan-Hydroxyapatite Complex: Effects of Immobilization Conditions

Çabuk, Burcu; Tarı, Canan; Harsa, Şebnem

doi:10.15406/jnhfe.2014.01.00004

Cited by 6 publications

(4 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The literature reports present various examples of β-galactosidase immobilisation. Among them, κ-carrageenan beads [28], chitosan-hydroxyapatite beads [29], fibres composed of alginate and gelatin hardened with glutaraldehyde [30], cellulose acetate-polymethylmethacrylate membrane [31], and glass beads [32] have been proposed. The utilisation of sodium alginate in the dairy industry context is justified due to the natural source of the main compound and mild gelation conditions.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Encapsulated NOLA™ Fit 5500 Lactase—An Economically Beneficial Way to Obtain Lactose-Free Milk at Low Temperature

Czyżewska

Trusek-Hołownia

2021

Catalysts

View full text Add to dashboard Cite

The current requirements of industrial biocatalysis are related to economically beneficial and environmentally friendly processes. Such a strategy engages low-temperature reactions. The presented approach is essential, especially in food processes, where temperature affects the quality and nutritional value foodstuffs. The subject of the study is the hydrolysis of lactose with the commercial lactase NOLA™ Fit 5500 (NOLA). The complete decomposition of lactose into two monosaccharides gives a sweeter product, recommended for lactose intolerant people and those controlling a product’s caloric content. The hydrolysis reaction was performed at 15 °C, which is related to milk transportation and storage temperature. The enzyme showed activity over the entire range of substrate concentrations (up to 55 g/L lactose). For reusability and easy isolation, the enzyme was encapsulated in a sodium alginate network. Its stability allows carrying out six cycles of the complete hydrolysis of lactose to monosaccharides, lasting from two to four hours. During the study, the kinetic description of native and encapsulated NOLA was conducted. As a result, the model of competitive galactose inhibition and glucose mixed influence (competitive inhibition and activation) was proposed. The capsule size does not influence the reaction rate; thus, the substrate diffusion into capsules can be omitted from the process description. The prepared 4 mm capsules are easy to separate between cycles, e.g., using sieves.

show abstract

Section: Discussionmentioning

confidence: 99%

“…Additionally, the negative galactose effect is more substantial in fungal preparations than yeast and bacterial [18]. The available reports, which present encapsulated β-galactosidase into chitosan and alginate-gelatin with glutaraldehyde, can be characterised by K m values such as 3.25 and 16.7 g/L at 35-37 • C, respectively [30,38].…”

Section: Discussionmentioning

confidence: 99%

Encapsulated NOLA™ Fit 5500 Lactase—An Economically Beneficial Way to Obtain Lactose-Free Milk at Low Temperature

Czyżewska

Trusek-Hołownia

2021

Catalysts

View full text Add to dashboard Cite

show abstract

“…0.00E+00 A change in enzyme conformation due to overly high or low pH value can cause a loss of enzymatic activity [22]. Therefore, pH is an important parameter in determining the optimum conditions for immobilization.…”

Section: Effect Of Immobilization Time On Esterification Activitymentioning

confidence: 99%

The effect of ethanol solvent on thermostability and esterification activity of immobilized Candida rugosa lipase on celite

Yudhana,

Zamara,

Curie

et al. 2023

IOP Conf. Ser.: Earth Environ. Sci.

View full text Add to dashboard Cite

Lipase is an enzyme commonly applied as a catalyst in the food industry, the synthesis of bioplastics, and the production of biodiesel. Candida rugosa lipase (CRL) is one of the widely used lipases due to its high selectivity and activity. However, high operating temperatures can denature enzymes, affecting enzyme activity due to structural changes. An enzyme can be immobilized on a supporting matrix to improve stability. Ethanol as an immobilization solvent may also increase the thermostability and esterification activity. This study examines the effect of ethanol solvent on the thermostability of immobilized Candida rugosa lipase. Immobilization was carried out on the Celite-545 matrix in buffer/ethanol solution. Different operating conditions such as enzyme concentrations, immobilization temperatures, immobilization time, and immobilization pH were observed. The immobilized enzyme activity was determined by esterification reaction using butyric acid and 1-butanol as substrates and isooctane as reaction medium. The results showed that immobilization increased the esterification activity by 76% at 37°C. Thermostability of immobilized enzyme was also enhanced by 29-51%, depending on the esterification temperature.

show abstract

“…Enzymes have an optimal pH range at which they exhibit the highest activity, and deviations from this range can lead to changes in the enzyme's conformation, affecting its catalytic activity (Chen et al, 2013). Besides, the loss in enzymatic activity at highly acidic or alkaline conditions might be also contributed to the alterations in the conformation of the enzyme resulting in a decrease in immobilization efficiency for the crosslinking technique (Cabuk et al, 2014). Moreover, variations in βgalactosidase characteristics, depending on the source (fungi, yeast, or bacteria), contribute to the lack of a consistent optimal pH for the enzyme (Carević et al, 2015).…”

Section: Operational Stability Of β-Galactosidasepolymethacrylate Mon...mentioning

confidence: 99%

Enhancing stability and activity of β-galactosidase from Kluyveromyces lactis through immobilization on polymethacrylate monolith and optimisation using response surface methodology

Dahari, R. F.,

Misson, M.,

Ongkudon, C. M.

et al. 2023

MJM

View full text Add to dashboard Cite

Aims: This study investigates the potential of porous polymethacrylate monoliths as enzyme support materials for largescale enzyme commercialization. Methodology and results: It focuses on their preparation and various immobilization techniques, such as adsorption, covalent-binding and cross-linking, specifically applied to β-galactosidase for bioprocess applications. The research assesses immobilization performance, operational stability, reusability and optimization using response surface methodology (RSM). The results reveal that covalent-binding exhibited the highest enzyme activity recovery, while cross-linking showed superior performance at lower enzyme concentrations but decreased at higher concentrations. Covalent-bound enzymes demonstrated reusability for up to four cycles, with optimal pH ranging between 7 and 8 and optimal temperature ranging between 30 °C and 40 °C. Furthermore, RSM optimization highlighted the significant influence of substrate concentration on enzyme activity, with a reliable model (R 2 = 0.9163) and adequate precision (S/N = 13.1409). Conclusion, significance and impact of study: Overall, this study provides valuable guidelines for effectively employing porous monoliths in large-scale industrial bioprocessing, offering potential cost-saving benefits and enhanced efficiency in enzyme commercialization.

show abstract

β-Galactosidase Immobilization on Chitosan-Hydroxyapatite Complex: Effects of Immobilization Conditions

Cited by 6 publications

References 31 publications

Encapsulated NOLA™ Fit 5500 Lactase—An Economically Beneficial Way to Obtain Lactose-Free Milk at Low Temperature

Encapsulated NOLA™ Fit 5500 Lactase—An Economically Beneficial Way to Obtain Lactose-Free Milk at Low Temperature

The effect of ethanol solvent on thermostability and esterification activity of immobilized Candida rugosa lipase on celite

Enhancing stability and activity of β-galactosidase from Kluyveromyces lactis through immobilization on polymethacrylate monolith and optimisation using response surface methodology

Contact Info

Product

Resources

About