studies on glycosyltransferases other than CGTase, we are interested in the action of CGTase in producing cyclic glucans larger than CDs. In this paper, we investigated the initial action of CGTase from an alkalophilic Bacillus sp. A2-5a (25) on synthetic amylose and found that the CGTase also produced

In our work, the CGTase from Thermoanaerobacter sp. (Tor- uzyme 3.0 L) gave a higher yield than that from Bacil- lus macerans (CGTase Amano). In contrast with the CGTase from Bacillus macerans (the HPLC chroma- togram showed four different compounds with in- creasing concentration, indicating the formation of the so-called analogous series

The transglycosylation activity of CGTase is well reported, as it is able to glucosylate other phenolic compounds such as resveratrol [ 26, 27 ], catechin [ 28 ], hydroquinone [ 29 ], kaempferol [ 30] or genistein [ 31 ]. Table 1. Cyclodextrin glucanotransferase (CGTase) from Bacillus macerans was applied to produce the CDs from linear α- (1,4)-glucans, which were obtained by Neisseria polysaccharea amylosucrase (Np AS) treatment on sucrose. The greatest CD yield (21.1%, w/w) was achieved from a one-pot dual enzyme reaction at 40 °C for 24 h. Amyloglucosidase from Aspergillus niger (Spirizyme Fuel) and CGTase from Thermoanaerobacter sp. (Toruzyme 3.0 L) were kindly donated by Novozymes A/S. CGTase from Bacillus macerans (CGTase Amano) was kindly supplied by Amano Enzyme Inc. Pure amyloglucosidase from Aspergillus niger (ref.

Cgtase amano

Närproducerade, ekologiska råvaror och viner av högsta kvalité brinner vi för. Färsk gös direkt från Hjälmaren, lokalt plockad svamp och oljor från Julita är bara ett par exempel. A bacterium that secretes maltooligosaccharide-forming amylase in a medium containing 12.5% (vol/vol) dimethylsulfoxide (DMSO) was isolated and identified as Brachybacterium sp. strain LB25. The amylase of the strain was purified from the culture supernatant, and its molecular mass was 60 kDa. The enzyme was stable at pH 7.0–8.5 and active at pH 6.0–7.5.

Table 1. Cyclodextrin glucanotransferase (CGTase) from Bacillus macerans was applied to produce the CDs from linear α- (1,4)-glucans, which were obtained by Neisseria polysaccharea amylosucrase (Np AS) treatment on sucrose.

studies on glycosyltransferases other than CGTase, we are interested in the action of CGTase in producing cyclic glucans larger than CDs. In this paper, we investigated the initial action of CGTase from an alkalophilic Bacillus sp. A2-5a (25) on synthetic amylose and found that the CGTase also produced

Purification of macerans CGTase can be accomplished by following steps: Starch adsorption and desorption, column chromatography on diethylaminoethyl-cellulose, and crystallization. Cyclodextrin glycosyltransferases (CGTases) from Paenibacillus macerans, Thermoanaerobacter sp. ATCC 53627, Bacillus stearothermophilus and a Carboxydocella sp. (phylogenetically identified from genomic DNA) were characterized with respect to their catalytic activity in different reactions, with emphasis on reactions useful for the elongation of the carbohydrate group of alkyl glycosides.

The crude CGTase extract with the corn starch substrate showed a productivity of 0.38 mmol/L/h, which was 29 % lower than using the purified enzyme and the corn starch substrate but 7 % higher

In our work, the CGTase from Thermoanaerobacter sp. (Tor- uzyme 3.0 L) gave a higher yield than that from Bacil- lus macerans (CGTase Amano).

fraccionar las grandes moléculas en otras de tamaño mucho más reducido, 13 Mar 2014 The CGTase catalyzed reactions between the glucose and maltose Denmark) and CGTase from B. macerans was obtained from Amano 7 Nov 2017 Lesaffre 2017 – Direcciόn Comunicaciόn grupo – Derechos reservados. 4. Ciclomaltodextrin. Glucanotransferasa.
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Närproducerade, ekologiska råvaror och viner av högsta kvalité brinner vi för.

Substrate, hesperetin, was purchased from Sigma-Aldrich Co. CGTase was purchased from Amano Pharmaceutical Co. Ltd. The NMR spectra were recorded in CD 3 OD using a Varian XL-400 spectrometer. The chemical shifts were expressed in δ (ppm) referring to tetramethylsilane. The HRFABMS spectra were measured using a JEOL MStation JMS-700 spectrometer.
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A bacterium that secretes maltooligosaccharide-forming amylase in a medium containing 12.5% (vol/vol) dimethylsulfoxide (DMSO) was isolated and identified as Brachybacterium sp. strain LB25. The amylase of the strain was purified from the culture supernatant, and its molecular mass was 60 kDa. The enzyme was stable at pH 7.0–8.5 and active at pH 6.0–7.5. The optimum

The number of ~'-CD producing enzyme is increasing, partly because of ~'-CD's high solubility, its large cavity and its potential usefulness. In all of these CGTase producing bacteria, B. macerans was selected for our research, and cultivated to obtain the enzyme containing broth. Amano Enzyme was founded 120 years ago in Japan as a pharmaceutical business, expanding into specialty enzymes in 1948 with our first item—malt diastase.

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Synthesis of β-maltosides of resveratrol. CGTase (Paenibacillus macerans) was purchased from Amano Enzyme Inc. Resveratrol 3-maltoside (8) and resveratrol 4′-β-maltoside (9) were produced individually as fol-lows. To a solution containing resveratrol 3-β-glucoside (2) …

CGTase solution (1% v/v) and PVA (8 wt%) solution were mixed followed by electrospinning (-9 kV, 3 h). CGTase/PVA nanofibres with an average diameter of 176 ± 46 nm were successfully produced. Samce rosną zwykle do 3,5 cm długości, samice do 4 cm, chociaż spotyka się jeszcze większe osobniki.Ciało przezroczyste, na grzbiecie biegnie linia, na bokac Glucoamylase was from Toyobo Co., Ltd. (Osaka, Japan) and B. macerans CGTase was from Amano Enzyme Inc. (Aichi, Japan). The enzyme was further purified using DEAE Sepharose Fast Flow media (Amersham Biosciences Europe GmbH). The enzyme was eluted with a linear gradient between 0 and 0.5 M NaCl in Tris–HCl buffer, pH 7.8. この物質をつくる酵素をサイクロデキストリングルカノトランスフェラーゼ（CGTase）といいます。そこに空間があるから。この輪の中には、何が入れられるでしょうか？ studies on glycosyltransferases other than CGTase, we are interested in the action of CGTase in producing cyclic glucans larger than CDs. In this paper, we investigated the initial action of CGTase from an alkalophilic Bacillus sp. A2-5a (25) on synthetic amylose and found that the CGTase also produced CGTase A reaction mixture (300 µL) containing 0.15 mg nerol, 30 mg maltose, 20 mM potassium phosphate buﬀer (pH 7.0), and 2 units of transglucosidase or 0.03 units of CGTase were incubated at 30°C for 24 h.

Bacillus macerans CGTase, here called Amano, (EC.2.4.1.19) was kindly provided by Amano enzyme Europe Ltd. (Milton Keynes, UK) and Thermoanaerobacter sp. ATCC 53627 CGTase (Toruzyme 3.0L,) from Novozymes (Bagsvaerd, Denmark). These enzymes have been

Isolation of CNF support The isolation process of CNF consists of several steps of alkaline process and high-intensity ultrasonication. Kenaf A produção de CDs foi feita usando a enzima ciclodextrina glucosiltransferase (CGTase E. C. 2.4.1.19), proveniente de Bacillus macerans, da Amano Intemational Enzyme, a 50°C e a avaliação dos resultados foi feito através de HPLC (High Performance Chromatography Liquid).

The optimum Tesque, Amano Enzyme, or Sigma-Aldrich. PaGT-3 was expressed and purified as described previously [7, 8]. LC analysis was performed on either a Shimadzu or a Hitachi HPLC system. Quercetin and its glycoside products were separated on reverse phase columns using acetonitrile/water. Mass spectra were obtained Munich, Germany. CGTase derived from Bacillus macerans was obtained as a kind gift from Amano Enzyme, Inc., Nagoya, Japan, in a stock solution that was used as supplied and stored at 5 °C.