Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose

Mörschbächer, Ana Paula; Volpato, Giandra; Souza, Cláucia Fernanda Volken de

doi:10.1590/0103-8478cr20150833

Cited by 21 publications

(8 citation statements)

References 25 publications

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“…Enzymatic hydrolysis of lactose is a highly selective procedure which maintains the characteristics of a raw material in the yielded product, as well have great potential for application in the food industry . Table illustrates hydrolysis of lactose by soluble and PANI‐CS‐NC‐ and PANI‐CS‐Ag‐NC‐adsorbed β‐gal for 10 h at 50 °C.…”

Section: Resultssupporting

confidence: 81%

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Elucidating the binding efficacy of β‐galactosidase on polyaniline–chitosan nanocomposite and polyaniline–chitosan–silver nanocomposite: activity and molecular docking insights

Khan

Husain

Ahmad

2018

J of Chemical Tech & Biotech

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BACKGROUND: Aspergillus oryzae -galactosidase ( -gal; EC 3.2.1.23) was physically adsorbed on polyaniline-chitosan nanocomposite (PANI-CS-NC) and polyaniline-chitosan-silver nanocomposite (PANI-CS-Ag-NC). Stability and kinetic studies were assessed, along with reusability and molecular docking interactions.RESULTS: According to transmission electron microscopy images, the sizes of the respective NCs were found to be in the range of 23-39 and 6-18 nm. The (effectiveness factor) values for PANI-CS-NC-and PANI-CS-Ag-NC-bound -gal were calculated to be 0.89 and 1.23, respectively, suggesting an enhancement in the activity of the enzyme in the presence of silver ions. Significant broadening was observed in pH and temperature profiles. Kinetic properties of PANI-CS-NC-and PANI-CS-Ag-NC-bound -gal showed lower K m , and two-and fourfold higher V max , respectively, compared to free enzyme. PANI-CS-Ag-NC-bound -gal was able to retain 94% of its initial activity after 10 repeated uses. Circular dichroism analysis revealed conformational changes in the secondary structure of protein upon immobilization. The genotoxic assessment revealed non-toxic behaviour of both free and enzyme-bound NC. The rate of lactose hydrolysis at 50 ∘ C exhibited by PANI-CS-Ag-NC bound -gal was 7% higher than that for the native enzyme. In-silico analysis showed efficient binding of -gal on PANI-CS-NCs due to interaction with residues that were exclusive of the active site of the enzyme. CONCLUSION: PANI-CS-Ag-NC-bound -gal preparation proved to be a robust nano-biocatalyst due to remarkable enhancement in catalytic activity along with excellent stability and reusability characteristics, which could be further utilized for efficient construction of nano-biosensors for producing lactose-free dairy products to feed lactose-intolerant patients. Lactose hydrolysis in batch processEnzymatic hydrolysis of lactose is a highly selective procedure which maintains the characteristics of a raw material in the J Chem Technol Biotechnol 2019; 94: 837-849

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Section: Resultssupporting

confidence: 81%

“…galactose. This phenomenon of inhibition of soluble β‐gal by its own product was explained earlier . Both immobilized β‐gal preparations were more resistant to inhibition‐mediated by‐product; thus they were able to hydrolyse more lactose on prolonged incubation.…”

Section: Resultsmentioning

confidence: 99%

Elucidating the binding efficacy of β‐galactosidase on polyaniline–chitosan nanocomposite and polyaniline–chitosan–silver nanocomposite: activity and molecular docking insights

Khan

Husain

Ahmad

2018

J of Chemical Tech & Biotech

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“…Proteolysis, lipolysis, and lactose decomposition were key factors in the formation of flavor precursor compounds and texture improvements in cheese (Ozcan and Kurdal, 2012;Mörschbächer et al, 2016;Ozturkoglu-Budak et al, 2016). Among the four types of cheeses, the contents of TFAA and Glu were the highest in WcC, which are extremely related to the high protease activity of W. confusa B14.…”

Section: Discussionmentioning

confidence: 99%

Investigation of the Lactic Acid Bacteria in Kazak Cheese and Their Contributions to Cheese Fermentation

Huang

Zheng

et al. 2020

Front. Microbiol.

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Kazak cheese is a traditional dairy product fermented by lactic acid bacteria (LAB) in Xinjiang. To investigate the LAB in Kazak cheese and their contributions to cheese fermentation, four representative LAB, Streptococcus thermophilus B8, Lactobacillus helveticus B6, Weissella confusa B14, and Lactobacillus rhamnosus B10, were isolated from Kazak cheese and subsequently used to ferment cheeses, which were named StC, LhC, WcC, and LrC, respectively. The result showed that most of the physical and chemical indicators had no significant difference, except for moisture and fat. W. confusa B14 was beneficial to the production of amino acids, whereas S. thermophilus B8 promoted the formation of organic acids and contributed to formation ideal texture property. Furthermore, the four cheeses all possessed a strong fruity aroma, with brandy, sweet, herbaceous, pungent, and fatty aromas being the most prominent in WcC. This is because L. helveticus B6 produced a high concentration of hexanal, nonanal, octanal, 3-methylbutanoic acid, ethyl acetate, ethyl butanoate, isoamyl acetate, and ethyl hexanoate in LhC. Research on the fermentation mechanism of LAB in cheese will provide a theoretical basis for the quality control and industrial production of Kazak cheese.

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“…Contudo, as enzimas apresentam desvantagens quanto a estabilidade operacional e de armazenamento, pois são moléculas complexas e altamente sensíveis. Porém, o avanço do processo de imobilização em vários tipos de suportes, por diferentes protocolos, permitiu melhorar sensivelmente a estabilidade térmica das enzimas (MÖRSCHBÄCHER, VOLPATO, SOUZA, 2016;GENNARI et al, 2018).…”

Section: Uso De Enzimas Imobilizadasunclassified

Imobilização enzimática em suportes orgânicos e inorgânicos: vantagens e desvantagens

Queissada

Silva²

2020

RHE

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O interesse na imobilização enzimática é alcançar um biocatalisador com atividade e estabilidade que não sejam afetadas durante o processo e que proporcione o máximo de reutilização da enzima frente aos parâmetros que podem inativar a mesma (temperatura, solventes orgânicos, etc.), cooperando com o meio ambiente e, ao mesmo tempo, otimizando a produção industrial. Este trabalho tem como objetivo principal descrever a imobilização enzimática em suportes orgânicos e inorgânicos, destacando as principais vantagens e desvantagens de cada sistema.Conclui-se que o uso da imobilização enzimática é menos prejudicial para o meio ambiente, contudo a escolha do melhor tipo de suporte, dependendo do objetivo da produção, é fundamental para o sucesso, tanto ambiental como industrial, do processo. Assim, deve-se levar em consideração as principais vantagens e desvantagens de cada técnica utilizada.

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Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose

Abstract: One of the greatest challenges for dairy industries is the correct destination of all the whey generated during cheese making, considering its high impact, the large volume created

Cited by 21 publications

References 25 publications

Elucidating the binding efficacy of β‐galactosidase on polyaniline–chitosan nanocomposite and polyaniline–chitosan–silver nanocomposite: activity and molecular docking insights

Elucidating the binding efficacy of β‐galactosidase on polyaniline–chitosan nanocomposite and polyaniline–chitosan–silver nanocomposite: activity and molecular docking insights

Investigation of the Lactic Acid Bacteria in Kazak Cheese and Their Contributions to Cheese Fermentation

Imobilização enzimática em suportes orgânicos e inorgânicos: vantagens e desvantagens

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