β-galactosidase and galactooligosaccharides production and applications

被引：5

作者：

Byfield J. ^{[1
]}

Cardenas S. ^{[1
]}

Alméciga-Diaz C.J. ^{[2
]}

Sánchez O.F. ^{[1
]}

机构：

[1] Chemical Engineering Department, Design Group of Process and Products, Universidad de Los Andes, Bogotá

[2] Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana, Bogotá

来源：

Recent Patents on Chemical Engineering | 2010年 / 3卷 / 01期

关键词：

β-galactosidase; Functional foods; Galactooligosaccharides; Prebiotics;

D O I：

10.2174/1874478811003010017

中图分类号：

学科分类号：

摘要：

Since early 1990s functional foods have presented important attention and demand from scientist and general population. Among the different components of functional foods, prebiotics have demonstrated a wide range of beneficial properties such as favoring of probiotic bacteria growth and intestinal mineral absorption. The most used prebiotics are inulin-type fructans and galactooligosaccharides (GOS). Although the former are widely used in nutritional supplements and functional foods and drinks, GOS have started to emerge as important prebiotic compounds since they share most of the prebiotic characteristic of inulin-type fructans but can be synthesized from cheaper substrates like whey. GOS are produced by the transgalactosylating activity ofβ-galactosidases (β-gal) derived from microorganisms, mainly fungi. In this paper, the recent patents inβ-gal and GOS production and their applications will be discussed. About 47 patents regardingβ-gal and GOS production and applications have been published since 2000, which are lower than those observed for other prebiotic compounds, like inulin-type fructans. Patents include the production of GOS with native or recombinant enzymes, the production ofβ-gal resistant to low or high temperatures and the development of functional foods and cosmetics.β-gal and GOS production represent an important but partially explored field for the development of new prebiotic compounds and their applications. © 2010 Bentham Science Publishers Ltd.

引用

页码：17 / 29

页数：12

共 65 条

[41]

Corral J.M., Banuelos O., Adrio J.L., Velasco J., Cloning and characterization of a beta β-galactosidase encoding region in Lactobacillus coryniformis CECT5711, Appl Microbiol Biotechnol, 73, 3, pp. 640-646, (2006)

[42]

Kim C.S., Ji E.S., Oh D.K., Characterization of a thermostable recombinant beta β-galactosidase from Thermotoga maritima, J Appl Microbiol, 97, 5, pp. 1006-1014, (2004)

[43]

Hung M., Xia Z., Hu N., Lee B., Molecular and biochemical analysis of two beta β-galactosidases from Bifidobacterium infantis HL96, Appl Environ Microbiol, 67, 9, pp. 4256-4263, (2001)

[44]

Ishikawa E., Sakai T., Ikemura H., Matsumoto K., Abe H., Identification, cloning, and characterization of a Sporobolomyces singularis beta β-galactosidase-like enzyme involved in galacto- oligosaccharide production, J Biosci Bioeng, 99, 4, pp. 331-339, (2005)

[45]

Chen W., Chen H., Xia Y., Zhao J., Tian F., Zhang H., Production, purification, and characterization of a potential thermostable galactosidase for milk lactose hydrolysis from Bacillus stearothermophilus, J Dairy Sci, 91, 5, pp. 1751-1758, (2008)

[46]

Jorgensen F., Hansen O., Stougaard P., (2002)

[47]

Tzortzis G., Goulas A., Goulas T., (2009)

[48]

Tzortzis G., Goulas A., Goulas T., (2009)

[49]

Mills D.A., Lebrilla C.B., Locascio R., Ninonuevo M., German B.J., Freeman S., (2009)

[50]

Gibson G.R., Kolida S., (2004)

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