On the Enzyme Specificity for the Synthesis of Prebiotic Galactooligosaccharides
On the Enzyme Specificity for the Synthesis of Prebiotic Galactooligosaccharides
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益生元低聚半乳糖合成的酶特异性
DOI:
10.1007/978-81-322-1094-8_3
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发表时间:
2013
期刊:
影响因子:
--
通讯作者:
F. Plou
中科院分区:
文献类型:
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作者:
Bárbara Rodriguez;L. Fernández;Miguel Teixeira de Abreu;Paulina Urrutia;M. Fernández;A. Ballesteros;F. Plou
β-Galactosidases catalyze transgalactosylation reactions in which lactose as well as the glucose and galactose released by hydrolysis serve as galactosyl acceptors yielding a series of galactooligosaccharides (GOS). GOS constitute the major part of oligosaccharides in human milk and are responsible of the formation of a Bifidus microbiota in the intestine of milk-fed babies. The bioactive properties of GOS depend on their chemical composition, structure, and polymerization degree. We have analyzed the product specificity of various β-galactosidases, namely, those from Kluyveromyces lactis, Bacillus circulans, and Aspergillus oryzae. The major products synthesized by B. circulans β-galactosidase contained only β-(1 → 4) bonds, whereas the enzyme from K. lactis synthesized GOS with major presence of β-(1 → 6) linkages. The A. oryzae β-galactosidase formed preferentially β-(1 → 6) bonds, with minor proportion of β-(1 → 3). B. circulans and K. lactis β-galactosidases produce nearly 45–50 % (w/w) GOS, whereas the A. oryzae enzyme produces less than 30 % (w/w). Another difference between the three enzymes was the polymerization degree of products; in particular, for a GOS mixture enriched in disaccharides, K. lactis and A. oryzae β-galactosidases are the best choices. In contrast, the B. circulans enzyme would be preferable for a GOS product with a high trisaccharides and tetrasaccharides content.