Concentrated beta-galactosidase and cell permeabilization from Saccharomyces fragilis IZ 275 for beta-galactosidase activity in the hydrolysis of lactose

被引:5
作者
Ito Morioka, Luiz Rodrigo [1 ]
Viana, Caroline dos Santos [1 ]
Alves, Erika de Padua [1 ]
Paiao, Fernanda Gonzales [1 ]
Takihara, Anderson Massaro [2 ]
Senoo Kakuno, Amanda Sayuri [3 ]
Suguimoto, Helio Hiroshi [1 ]
机构
[1] Univ Pitagoras Unopar UNOPAR, Londrina, PR, Brazil
[2] Univ Tecnolg Fed Parana UTFPR, Londrina, PR, Brazil
[3] Colegio Interat, Londrina, PR, Brazil
来源
FOOD SCIENCE AND TECHNOLOGY | 2019年 / 39卷 / 03期
关键词
enzyme activity; microbial biotechnology; cell permeabilization; lactose hydrolysis; enzyme extraction; STABILITY; SUPPORTS; ETHANOL;
D O I
10.1590/fst.06017
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The cheese whey shows an organic nutrient charge that can be used to obtain metabolites of interest by biotechnology of microorganisms. Thus, fermentative processes for enzyme production, in particular beta-galactosidase becomes feasible. The enzyme plays an important role in the biotech food industry to obtain milk and dairy products with low lactose content for consumption by intolerant individuals. The objective of this work was to determine the enzyme activity of the concentrated beta-galactosidase (CBG) and the permeabilized cells (PC) both obtained from Saccharomyces fragilis IZ 275. The enzyme beta-galactosidase obtained from the fermentation of Saccharomyces fragilis IZ 275 in cheese whey was used to determine the optimal conditions for the hydrolysis of lactose solution at 1% (w/v). Response Surface Methodology (RSM) by Box-Behnken Design (BBD) was employed to determine beta-galactosidase activity for such factors pH, temperature and enzyme concentration suitable for the lactose hydrolysis. Based on the statistical analysis, the optimum operational conditions for maximizing lactose hydrolysis thus optimizing the enzyme activity for CBG were, temperature 30 degrees C, pH 6.0 and enzyme concentration 3% (v/v and for PC was temperature 44 degrees C, pH 7.0 and enzyme concentration 4% (v/v).
引用
收藏
页码:524 / 530
页数:7
相关论文
共 18 条
[1]   Recombinant β-galactosidases - Past, present and future: A mini review [J].
Ansari, Shakeel Ahmed ;
Satar, Rukhsana .
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2012, 81 :1-6
[2]  
Box G.E.P., 1960, Technometrics, V2, P455, DOI [10.1080/00401706.1960.10489912, DOI 10.1080/00401706.1960.10489912]
[3]  
Colognesi G. de O. da S., 2017, African Journal of Biotechnology, V16, P2043, DOI 10.5897/ajb2016.15705
[4]   Optimization of β-galactosidase production using Kluyveromyces lactis NRRL Y-8279 by response surface methodology [J].
Dagbagli, Seval ;
Goksungur, Yekta .
ELECTRONIC JOURNAL OF BIOTECHNOLOGY, 2008, 11 (04)
[5]   A modelling study on hydrolysis of whey lactose and stability of β-galactosidase [J].
Demirhan, Elcin ;
Apar, Dilek Kilic ;
Ozbek, Belma .
KOREAN JOURNAL OF CHEMICAL ENGINEERING, 2010, 27 (02) :536-545
[6]   Lactose hydrolysis by immobilized β-galactosidase:: the effect of the supports and the kinetics [J].
Di Serio, M ;
Maturo, C ;
De Alteriis, E ;
Parascandola, P ;
Tesser, R ;
Santacesaria, E .
CATALYSIS TODAY, 2003, 79 (1-4) :333-339
[7]  
Domingues Lucilia, 2010, Bioeng Bugs, V1, P164, DOI 10.4161/bbug.1.3.10619
[8]   Production of ethanol from industrial whey [J].
Florencio, Isanna M. ;
Florentino, Eliane R. ;
da Silva, Flavio L. H. ;
Martins, Ricardo S. ;
Cavalcanti, Monica T. ;
Gomes, Josivanda P. .
REVISTA BRASILEIRA DE ENGENHARIA AGRICOLA E AMBIENTAL, 2013, 17 (10) :1088-1092
[9]   Use of highly efficient Draper-Lin small composite designs in the formal optimisation of both operational and chemical crucial variables affecting a FIA-chemiluminescence detection system [J].
Gámiz-Gracia, L ;
Cuadros-Rodríguez, L ;
Almansa-López, E ;
Soto-Chinchilla, JJ ;
García-Campaña, AM .
TALANTA, 2003, 60 (2-3) :523-534
[10]   Modeling of the simultaneous hydrolysis-ultrafiltration of whey permeate by a thermostable β-galactosidase from Aspergillus niger [J].
Hatzinikolaou, DG ;
Katsifas, E ;
Mamma, D ;
Karagouni, AD ;
Christakopoulos, P ;
Kekos, D .
BIOCHEMICAL ENGINEERING JOURNAL, 2005, 24 (02) :161-172