Hydrolysis of lactose in whole milk catalyzed by β-galactosidase from Kluyveromyces fragilis immobilized on chitosan-based matrix

Vieira, Danielle Cristina; Lima, Lionete Nunes de; Mendes, Adriano A.; Adriano, Wellington Sabino; Giordano, Roberto; Giordano, Raquel de Lima Camargo; Tardioli, Paulo Waldir

doi:10.1016/j.bej.2013.10.007

Cited by 41 publications

(15 citation statements)

References 46 publications

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“…Exemplos de β-galactosidases comercialmente disponíveis são as que estão sob o nº 072-04141 do catálogo da Wako Pure Chemical Industries, Ltd., e G1875 da Sigma-Aldrich. Em relação ao pH, as lactases podem ser classificadas em dois grandes grupos: β-galactosidases de pH ótimo neutro (ZHOU; CHEN, 2001;VIEIRA et al, 2013;SRIVASTAVA;MISHRA;CHAND, 2015) e β-galactosidases com máxima atividade em pH ácido (VERA; GUERRERO;ILLANES, 2011;CHIBA;YAMADA;ISOBE, 2015;CAREVIĆ et al, 2016;NIU et al, 2017). β-galactosidases neutras são geralmente utilizadas em produtos alimentícios neutros, como o leite (WOLF; GASPARIN; PAULINO, 2018), enquanto as β-galactosidases ácidas são empregadas em suplementos nutricionais (WANG et al, 2009).…”

Section: Enzima β-Galactosidaseunclassified

Ciência e Tecnologia de Leite e Produtos Lácteos Sem Lactose

Dantas¹,

Verruck²,

Prudêncio³

2019

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Section: Enzima β-Galactosidaseunclassified

Ciência e Tecnologia de Leite e Produtos Lácteos Sem Lactose

Dantas¹,

Verruck²,

Prudêncio³

2019

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“…Immobilized β‐galactosidase was 3‐ to 5‐fold more stable than the soluble enzyme at 40 and 20°C, respectively. The immobilized biocatalyst was capable of efficiently hydrolyzing lactose into the whole milk at 25°C, and showed similar performance even after four consecutive batches (Vieira et al, ).…”

Section: Cell and Enzyme Immobilization And Process Optimizationmentioning

confidence: 97%

β-galactosidase: Biotechnological applications in food processing

2018

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β‐Galactosidases produced by microorganisms are being used in food technology for hydrolysis of lactose in milk and milk by‐products. The enzyme has attracted much attention in view of lactose intolerance in human population and due to importance of milk in human diet. β‐Galactosidase hydrolyze β‐galactopyranosides, that is, lactose, and form a range of trans‐galactosylation products or galactooligosaccharides (GOS) capable of providing several health benefits as prebiotics. In addition, the enzyme also finds applications in production of lactose based sweeteners from high lactose containing effluents of cheese manufacturing industries. Currently, the enzyme is mainly obtained from Aspergillus niger and Kluyveromyces lactis, however, they are thermolabile with optimum pH between 4.0 and 6.0 accompanied by low chemical resistance and high product inhibition properties. Thermostable enzymes are suitable to perform the hydrolytic process at relatively high temperatures, minimizing pathogen contamination, psychrophilic β‐galactosidases are preferred for treatment of milk under refrigerated conditions (<15°C), without heating and maintenance of temperature. Lactic acid bacteria (LAB) are a potential source of food grade enzymes and other metabolites. Although reports on the use of β‐galactosidase of LAB in pure form is reported for hydrolysis of lactose in milk and production of fermented milk products for reduced lactose content, methods of immobilization for use in continuous bioreactors are less explored. Recombinant DNA technology has attained much significance to reveal molecular aspects of enzyme catalysis, protein structure, gene organization for expression, and enhancement of thermophilic, psychrophilic, and mesophilic β‐galactosidases. Heterologous expression of extremozymes with β‐galactosidase would help in overcoming the limitations faced within the bioprocess technology. Practical applications Lactic acid bacteria (LAB) producing extracellular cell bound β‐galactosidase have been isolated and enzyme production was carried out using modified MRS medium incorporating lactose as enzyme inducer. Process for growing probiotic lactic acid bacteria for β‐galactosidase from fermented milk products has been patented (Indian Patent No. 247904). Thermostable β‐galactosidases were also extracted from Kluyveromyces lactis a yeast, isolated from curd samples and Bacillus sp. MTCC 864. An Indian patent has been granted for a simple, cost effective perforated two compartment immobilized enzyme bioreactor was designed and fabricated for lactose hydrolysis (Indian Patent No. 264609). The bioreactor can be operated continuously at temperature between 5.0 and 75.0°C, employing different immobilized enzyme preparations for different operational temperatures. β‐galactosidase of cell confined LAB and yeast have been immobilized in agarose and galactooligosaccharides (GOS) production was observed at 40% lactose concentration in 0.05M phosphate buffer at pH 6.5. Immobilized bioreactor preparation could be used for lactos...

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“…Activities of the biocatalysts CALB-SMMP-octyl and CALB-SMMPoctyl-glu were similar, although recovered activities were different for those biocatalysts. This difference indicates mass transfer delays into the internal surface of the biocatalyst, very common for highloaded biocatalysts [1,2,4,21].…”

Section: Characterization Of the Smmpsmentioning

confidence: 99%

Mono- and heterofunctionalized silica magnetic microparticles (SMMPs) as new carriers for immobilization of lipases

Lima

Vieira

Kopp

et al. 2016

Journal of Molecular Catalysis B: Enzymatic

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a b s t r a c tIn order to improve economic viability of an enzymatic process, the use of an operationally stable and low-cost biocatalyst is encouraged. Although the immobilization of lipases is widely reported, the search for new supports and immobilization protocols with better properties is still important. In this study, mono-and heterofunctionalized silica magnetic microparticles (SMMPs) were synthetized for immobilization of lipase B from Candida antarctica (CALB). The SMMPs were prepared in a micro-emulsion system containing sodium silicate and superparamagnetic iron oxide nanoparticles, followed by chemical modification with octyl groups and octyl plus aldehyde groups. These supports allowed the immobilization of CALB by hydrophobic adsorption or hydrophobic/covalent linkages, achieving immobilization yield of 88% and recovered activities of 128% and 59%, respectively. The performance of the magnetic biocatalysts was evaluated in the synthesis of xylose fatty acid esters (laurate or oleate) in tert-butyl alcohol medium, yielding around 60% conversion after 48 h under optimized conditions (xylose/fatty acid molar ratio of 1:0.2, 55 • C, and activity load of 37.5 U/g). The magnetic biocatalyst was used in 10 reaction cycles of 48 h at 46 • C maintaining high xylose conversions. Besides, the biocatalyst might be easily and quickly recovered from the reaction medium by an external magnetic field, an operational advantage in the case of viscous and complex media, e.g., medium containing insoluble sugars and molecular sieves.

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Hydrolysis of lactose in whole milk catalyzed by β-galactosidase from Kluyveromyces fragilis immobilized on chitosan-based matrix

Cited by 41 publications

References 46 publications

Ciência e Tecnologia de Leite e Produtos Lácteos Sem Lactose

Ciência e Tecnologia de Leite e Produtos Lácteos Sem Lactose

β-galactosidase: Biotechnological applications in food processing

Mono- and heterofunctionalized silica magnetic microparticles (SMMPs) as new carriers for immobilization of lipases

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