Chelation by collagen in the immobilization of Aspergillus oryzae β-galactosidase: A potential biocatalyst to hydrolyze lactose by batch processes

Gennari, Adriano; Mobayed, Francielle Herrmann; Volpato, Giandra; Souza, Cláucia Fernanda Volken de

doi:10.1016/j.ijbiomac.2017.12.088

Cited by 22 publications

(3 citation statements)

References 38 publications

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“…The instability and enzymatic degradation of lactase can be due to several factors as inadequate exposure of the formulations, by the users and or manufacturers, high temperature that can lead to the enzymatic inactivation due to the formation of insoluble particles and aggregates, besides unfolding and protein degradation [4,[10][11][12]. Therefore, these factors may justify what was observed in the analysis of sample #S1.…”

Section: Articlementioning

confidence: 94%

“…Different microorganisms (fungi, bacteria and yeasts) and industrial purifications routes can be used to obtain lactases that may present significant differences in their structures and physicochemical properties resulting from different mechanisms of production. For example, lactase from Aspergillus oryzae is a monomeric enzyme having a molecular mass of 90 kDa, does not require cofactors and has an optimal action pH of 4.5 [10]; but the lactase from Lactobacillus acidophilus has a molecular mass of 540 kDa, needs magnesium as cofactor and presents a optimum pH in 6.2-6.6 [37].…”

Section: Evaluation Of Impurities and Degradation In Formulations Conmentioning

confidence: 99%

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Evaluation of the quality of formulations containing lactase (β-galactosidase) employing gel electrophoresis and cell phone

Dionizio¹,

Babos²,

Souza³

et al. 2019

Br J Anal Chem

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A quantification method of the lactase enzyme in pharmaceutical formulations is proposed employing digital images obtained from a cell phone camera and processed using the colorimetric application. The use of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) made it possible to identify the lactase enzyme, to fractionate possible protein impurities and to evaluate the degradation of lactase present in the analyzed formulations. In addition, gel electrophoresis made it possible to determine lactase free of matrix interference. The proposed method presented limit of quantification of 0.002 mg lactase (0.03 FCC), using external calibration. Recoveries of lactase added to the samples were in the range 78-104%. The concentrations found in different pharmaceutical formulations samples containing lactose were in the range 7-621 mg (104-9319 FCC). The relative standard deviations (RSD) were in the range of 3-13%. Of the six samples analyzed, only two (#S2 and #S5) were in agreement with the sample label description.

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Section: Articlementioning

confidence: 94%

Section: Evaluation Of Impurities and Degradation In Formulations Conmentioning

confidence: 99%

Evaluation of the quality of formulations containing lactase (β-galactosidase) employing gel electrophoresis and cell phone

Dionizio¹,

Babos²,

Souza³

et al. 2019

Br J Anal Chem

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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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Nickel-Functionalized Chitosan for the Oriented Immobilization of Histidine-Tagged Enzymes: A Promising Support for Food Bioprocess Applications

et al. 2022

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Chelation by collagen in the immobilization of Aspergillus oryzae β-galactosidase: A potential biocatalyst to hydrolyze lactose by batch processes

Cited by 22 publications

References 38 publications

Evaluation of the quality of formulations containing lactase (β-galactosidase) employing gel electrophoresis and cell phone

Evaluation of the quality of formulations containing lactase (β-galactosidase) employing gel electrophoresis and cell phone

Imobilização enzimática em suportes orgânicos e inorgânicos: vantagens e desvantagens

Nickel-Functionalized Chitosan for the Oriented Immobilization of Histidine-Tagged Enzymes: A Promising Support for Food Bioprocess Applications

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