Continuous production of lactulose by immobilized thermostable β-glycosidase from Pyrococcus furiosus

Mayer, Jürgen; Kranz, Bertolt; Fischer, Lutz

doi:10.1016/j.jbiotec.2009.12.017

Cited by 71 publications

(44 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The enzymatic synthesis of lactulose is usually performed with β-galactosidase and glucosidase enzyme classes (Adamczak et al, 2009;Mayer et al, 2010;Zimmer et al, 2017). β-galactosidase is a biocatalyst used in the transgalactosylation reaction which may bioconvert lactose and fructose in lactulose (Panesar & Kumari, 2011;Tang et al, 2011).…”

Section: Enzymatic Methodsmentioning

confidence: 99%

Obtainment, quantification and use of lactulose as a functional food – a review

et al. 2017

View full text Add to dashboard Cite

Whey (milk serum) is produced by the dairy industry during the manufacture of cheese. In addition to being a valuable source of functional and nutritional proteins, whey also presents almost all the lactose from the original whole milk. However, many industries still consider the whey as an effluent, which can cause serious environmental problems when not properly treated. Therefore, it is important to develop alternatives for the adequate use of whey. The lactose obtained from whey permeate can be converted into lactulose, a prebiotic which may be metabolized in the intestine by probiotic bacteria, such as Lactobacillus sp. and Bifidobacterium sp., through enzymatic isomerization or by using alkaline catalysts, with minimal secondary reactions and high yield. This manuscript provides information about various techniques used to produce lactulose, its purification and analysis, as well as its mechanisms of action and alternative applications in food products and medicines.Keywords: lactose isomerization; lactulose; prebiotics; reuse of industrial byproducts; whey permeate.Practical Application: Synthesizing and quantifying lactulose from whey permeate, and use in the dairy industry.

show abstract

Section: Enzymatic Methodsmentioning

confidence: 99%

Obtainment, quantification and use of lactulose as a functional food – a review

et al. 2017

View full text Add to dashboard Cite

show abstract

“…Since b-galactosidase genes have been successfully expressed in recombinant E. coli and the purified enzymes have been used in lactulose production [8,11], the expressing of b-galactosidases genes from other microbes such as Arthrobacter sp. LAS in E. coli might change the condition for lactulose production and minimize the byproducts.…”

Section: Purification Of B-galactosidasementioning

confidence: 99%

“…Although b-galactosidases from different sources either in the form of whole cells or purified enzymes are described, the promising ones are limited to those from Kluyveromyces lactis, Sulfolobus solfataricus, and Pyrococcus furiosus [8,9,11] whose optimum temperatures for lactulose production are relatively high (60, 80, and 75°C, respectively). High temperature with the high concentration of reducing sugars (lactose, fructose) induces nonenzymatic browning [10].…”

Section: Introductionmentioning

confidence: 99%

Lactulose biosynthesis by β-galactosidase from a newly isolated Arthrobacter sp.

Tang¹,

Li²,

Dong³

et al. 2010

J Ind Microbiol Biotechnol

View full text Add to dashboard Cite

Lactulose, a ketose disaccharide, is used in both pharmaceutical and food industries. This study was undertaken to screen and isolate potent β-galactosidase-producing bacteria and to evaluate their enzymatic production of lactulose. Soil samples from fruit gardens were collected. One isolate designated LAS was identified whose cell extract could convert lactose and fructose into lactulose. The 16S rDNA gene analysis of LAS revealed its phylogenetic relatedness to Arthrobacter sp. The β-galactosidase produced by LAS was purified 15.7-fold by ammonium sulfate precipitation and subsequent Phenyl-Sepharose hydrophobic chromatography. The optimum pH and temperature for lactulose synthesis by this β-galactosidase were 6.0 and 20 °C, respectively. The low optimum temperature of this enzyme compared to the currently used ones for lactulose production has the advantage of reducing the nonenzymatic browning in biotransformations. The results indicated that Arthrobacter could be used as a novel bacterial β-galactosidase source for lactulose production.

show abstract

“…Any sugar present throughout the reaction can be the nucleophile to accept the transferred galactosyl moiety, yielding a mixture of glucose, galactose, unreacted lactose and fructose, trans-D-galactosylated oligosaccharides indicating that the transgalactosylation catalyzed by b-galactosidase is a very complex reaction. b-Galactosidases from different sources, including Kluyveromyces lactis (K. lactis), the major source of bgalactosidase, have been described as catalysts for the transgalactosylation from lactose to fructose, directing towards the formation (Kim, Park, & Oh, 2006;Lee, Kim, & Oh, 2004;Mayer et al, 2004;Mayer, Kranz, & Fischer, 2010). However, little information about other transgalactosylation products has been previously reported, probably due to the fact that the physicochemical properties of these formed oligosaccharides were so similar, that the analytical methods used, could not distinguish them or they were not isolated and identified successfully.…”

Section: Introductionmentioning

confidence: 99%