A novel transglycosylating β-galactosidase from Enterobacter cloacae B5

Lu, Lili; Xiao, Min; Li, Zhengyi; Li, Yumei; Wang, Fengshan

doi:10.1016/j.procbio.2008.10.010

Cited by 35 publications

(33 citation statements)

References 23 publications

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“…32cB ␤-dgalactosidase catalyzed the synthesis of heterooligosaccharides, namely lactulose, galactosyl-xylose or galactosyl-arabinose, and glycosylated salicin. ␤-d-Galactosidases from Enetrobacter agglomerans B1 and E. cloacae B5 catalyze glycosyl transfer from ONPG to various acceptors such as hexoses (glucose, galactose, mannose, fructose, sorbose), pentoses (arabinose, xylose), disaccharides (cellobiose, sucrose, trehalose), hexahydroxyalcohols (mannitol, sorbitol), cyclitol (inositol) and aromatic glycoside (salicin) [33,34]. The enzymatic synthesis, by Aspergillus oryzae ␤-d-galactosidase, of galactosyl-xylose from ONPG and xylose as substrates has been also reported [35].…”

Section: Discussionmentioning

confidence: 99%

“…However, this process leads to the formation of a certain amount of by-products as a result of sugar degradation under harsh conditions, namely a pH 10.5-11.5 and temperatures of between 70 and 100 • C. The enzymatic synthesis of lactulose offers much milder conditions and can be conducted in crude lactose materials such as whey or whey permeate [32]. Heterologous galactosyl transfer catalyzed by ␤-d-galactosidase yields a virtually unlimited diversity of oligosaccharides [33][34][35][36][37][38][39]. However, none of cold-active ␤-d-galactosidases have yet been used for this purpose.…”

Section: Introductionmentioning

confidence: 99%

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A novel cold-active β-d-galactosidase with transglycosylation activity from the Antarctic Arthrobacter sp. 32cB – Gene cloning, purification and characterization

Pawlak-Szukalska

Wanarska

Popinigis

et al. 2014

Process Biochemistry

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a b s t r a c tA gene encoding a novel ␤-d-galactosidase from the psychrotolerant Antarctic bacterium Arthrobacter sp. 32cB was isolated, cloned and expressed in Escherichia coli. The active form of recombinant ␤-dgalactosidase consists of two subunits with a combined molecular weight of approximately 257 kDa. The enzyme's maximum activity towards o-nitrophenyl-␤-d-galactopyranoside was determined as occurring at 28 • C and pH 8.0. However, it exhibited 42% of maximum activity at 10 • C and was capable of hydrolyzing both lactose and o-nitrophenyl-␤-d-galactopyranoside at that temperature, with K m values of 1.52 and 16.56 mM, and k cat values 30.55 and 31.84 s −1 , respectively. Two units of the enzyme hydrolyzed 90% of the lactose in 1 mL of milk at 10 • C in 24 h. The transglycosylation activity of Arthrobacter sp. 32cB ␤-d-galactosidase was also examined. It synthesized galactooligosaccharides in a temperature range from 10 to 30 • C. Moreover, it catalyzed the synthesis of heterooligosaccharides such as lactulose, galactosyl-xylose and galactosyl-arabinose, alkyl glycosides, and glycosylated salicin from lactose and the appropriate acceptor at 30 • C. The properties of Arthrobacter sp. 32cB ␤-d-galactosidase make it a candidate for use in the industrial removal of lactose from milk and a promising tool for the glycosylation of various acceptors, especially those which are thermosensitive.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A novel cold-active β-d-galactosidase with transglycosylation activity from the Antarctic Arthrobacter sp. 32cB – Gene cloning, purification and characterization

Pawlak-Szukalska

Wanarska

Popinigis

et al. 2014

Process Biochemistry

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“…b-Galactosidases have been also used to produce heterooligosaccharides (HeOSs); e.g., lactulose was enzymatically synthesized by a Sulfolobus solfataricus b-galactosidase from lactose and fructose (Kim, Park, & Oh, 2006), whereas Kluyveromyces lactis b-galactosidase galactosylated aromatic primary alcohols (Bridiau, Taboubi, Marzouki, Legoy, & Maugard, 2006). A wide range of sugar alcohols and mono-and disaccharides have been shown to act as an acceptor carbohydrate for a b-galactosidase of Enterobacter cloacae B5 (Lu, Xiao, Li, & Wang, 2009). The choice of acceptor carbohydrate and enzyme allows the formation of tailor-made HeOSs with potential application as food additives or therapeutics.…”

Section: Introductionmentioning

confidence: 99%

Production of galactooligosaccharides and heterooligosaccharides with disrupted cell extracts and whole cells of lactic acid bacteria and bifidobacteria

Schwab

Lee

Sørensen

et al. 2011

International Dairy Journal

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“…Recently novel β‐galactosidase capable of glycosyl transfer was purified from a strain of Enterobacter cloacae B5 isolated from soil. This strain synthesizes GOS with a high yield of 55% from 275 g/L lactose at 50 °C for 12 h. A gene encoding the enzyme was cloned in E. coli and the recombinant enzyme was found to have similar transglycosylation activity to the natural enzyme (Lu and others 2009). …”

Section: Biotechnological Methods For Enhanced Gos Productionmentioning

confidence: 99%

Galactooligosaccharides: Novel Components of Designer Foods

Sangwan¹,

Tomar²,

Singh³

et al. 2011

Journal of Food Science

196

149

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Since introduction of functional foods, commercialization of the traditionally used probiotics has ushered in more followers into the new fraternity of sophisticated, health-conscious consumers. In 1995, this was followed by the first introduction of prebiotics. Prebiotics are defined as "a non-digestible feed supplement, beneficially affecting the host by selectively stimulating growth and/or activity in one or a limited number of bacteria in the colon." The number of new product introductions with prebiotics has steeply increased over the last few years. Paradoxically, probiotics have limited applications as these cannot be used in wide range of food products because of their viability issue. Fortunately, prebiotics do not suffer from any such constraint and can be used in a wide range of food products. Probiotics do not have a long shelf life in their active form. In most cases, refrigeration is required to maintain the shelf life. While probiotics are predominantly used in fermented dairy products, the use of prebiotics has expanded into other food categories. Prebiotics have successfully been incorporated in a wide variety of human food products such as baked goods, sweeteners, yoghurts, nutrition bars, and meal replacement shakes. For instance, the introduction of galacto-oligosaccharides (GOS) into baby foods has been very successful. GOS, which are identical to the human milk oligosaccharides, has emerged with strong clinical support for both digestive and immune health. Various aspects related to GOS such as types and functions of functional food constituents with special reference to GOS, their role as prebiotics, and enhanced industrial production through microbial intervention are dealt in this review.

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A novel transglycosylating β-galactosidase from Enterobacter cloacae B5

Cited by 35 publications

References 23 publications

A novel cold-active β-d-galactosidase with transglycosylation activity from the Antarctic Arthrobacter sp. 32cB – Gene cloning, purification and characterization

A novel cold-active β-d-galactosidase with transglycosylation activity from the Antarctic Arthrobacter sp. 32cB – Gene cloning, purification and characterization

Production of galactooligosaccharides and heterooligosaccharides with disrupted cell extracts and whole cells of lactic acid bacteria and bifidobacteria

Galactooligosaccharides: Novel Components of Designer Foods

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