Effect of temperature and enzyme origin on the enzymatic synthesis of oligosaccharides

Boon, M.A.; Janssen, A.E.M.; Riet, K. van ’t

doi:10.1016/s0141-0229(99)00167-2

Cited by 169 publications

(150 citation statements)

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“…In biotechnology, bgalactosidases are mainly employed for the hydrolysis of lactose to D-glucose and D-galactose in various products of the dairy industry (Gekas & Lopez-Leiva, 1985;Holsinger & Kligerman, 1991). In addition, b-galactosidases catalyse transgalactosylation reactions, which have attracted considerable interest because of suggested beneficial effects on human health (Boon et al, 2000;Nakayama & Amachi, 1999).…”

Section: Introductionmentioning

confidence: 99%

Induction of extracellular β-galactosidase (Bga1) formation by d-galactose in Hypocrea jecorina is mediated by galactitol

et al. 2007

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The ability of Hypocrea jecorina (Trichoderma reesei) to grow on lactose strongly depends on the formation of an extracellular glycoside hydrolase (GH) family 35 b-galactosidase, encoded by the bga1 gene. Previous studies, using batch or transfer cultures of pregrown cells, had shown that bga1 is induced by lactose and D-galactose, but to a lesser extent by galactitol. To test whether the induction level is influenced by the different growth rates attainable on these carbon sources, bga1 expression was compared in carbon-limited chemostat cultivations at defined dilution (=specific growth) rates. The data showed that bga1 expression by lactose, D-galactose and galactitol positively correlated with the dilution rate, and that galactitol and D-galactose induced the highest activities of b-galactosidase at comparable growth rates. To know more about the actual inducer for b-galactosidase formation, its expression in H. jecorina strains impaired in the first steps of the two D-galactose-degrading pathways was compared. Induction by D-galactose and galactitol was still found in strains deleted in the galactokinase-encoding gene gal1, which is responsible for the first step of the Leloir pathway of D-galactose catabolism. However, in a strain deleted in the aldose/D-xylose reductase gene xyl1, which performs the reduction of D-galactose to galactitol in a recently identified second pathway, induction by D-galactose, but not by galactitol, was impaired. On the other hand, induction by D-galactose and galactitol was not affected in an L-arabinitol 4-dehydrogenase (lad1)-deleted strain which is impaired in the subsequent step of galactitol degradation. These results indicate that galactitol is the actual inducer of Bga1 formation during growth on D-galactose in H. jecorina.

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Section: Introductionmentioning

confidence: 99%

Induction of extracellular β-galactosidase (Bga1) formation by d-galactose in Hypocrea jecorina is mediated by galactitol

et al. 2007

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“…In the case of acidic whey hydrolysis, fungal β-galactosidase with pH optima of 3.0-5.0 is suitable. Thus the selection of β-galactosidase depends on the final application of the enzyme or industry (53,54 (55). In industrial applications, two major classes of β-galactosidase are of prime importance.…”

Section: Lactase (β-Galactosidase)mentioning

confidence: 99%

Applications of Microbial Enzymes in Food Industry

Sindhu

Binod

Ummalyma

et al. 2018

Food Technol. Biotechnol.

525

230

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SUMMARYThe use of enzymes or microorganisms in food preparations is an age-old process. With the advancement of technology, novel enzymes with wide range of applications and specificity have been developed and new application areas are still being explored. Microorganisms such as bacteria, yeast and fungi and their enzymes are widely used in several food preparations for improving the taste and texture and they offer huge economic benefits to industries. Microbial enzymes are the preferred source to plants or animals due to several advantages such as easy, cost-effective and consistent production. The present review discusses the recent advancement in enzyme technology for food industries. A comprehensive list of enzymes used in food processing, the microbial source of these enzymes and the wide range of their application are discussed.

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“…For avoiding these undesirable products long protection -deprotection steps for selective control are required, as well as low final yields are achieved (11). In the last years GOS has been produced through employing the transgalactosylation activity of various β-galactosydases (lactase, EC.3.2.1.23) (3,19). β-Galactosydases can catalyze the transgalactosyl reaction as well as the hydrolysis of lactose.…”

Section: Introductionmentioning

confidence: 99%