We have determined the 2.0 and 2.5 Å X-ray structures of E257A/D229A CGTase in complex with The extracellular enzyme cyclodextrin glucanotransferase (CGTase) synthesizes cyclic malto-oligosaccharides called cyclodextrins (CDs) from starch and related α-1,4-glucans. CGTases are produced by a variety of bacteria, mainly Bacillus species, by submerged culture in complex medium. CGTases differ in the amount and types of CDs produced. In addition, CGTase production is highly dependent on Information on EC 22.214.171.124 - cyclomaltodextrin glucanotransferase. cyclomaltodextrins (Schardinger dextrins) of various sizes (6,7,8, etc.
The main chain of the γ-cyclodextrin-complexed CGTase superimposes very well on that of unliganded CGTase (root mean square deviation, 0.16 Å for 686 Cα atoms). The only exceptions occur in the loops comprising residues 324–334 (involved in catalysis around subsite −1 ( 7 )) and 144–151 (involved in altered crystal contacts). Expression vectors encoding N-terminal PelB, DacD, and the native Bacillus sp. G825-6 CGTase signal peptides (SP) were constructed for the recombinant CGTase.
を経て、 さらに、デンプンを糖供与体とした CGTase に. よるカプサイシンオリゴ サッカライド CYCLODEXTRIN의 기술 동향. 임번삼.
CGTase / sucrose ester / glycosyl transfer reaction / glucose / surfactant / lauric acid / sucrose laurate / non-ionic surfactant: 研究概要: CGTaseはデキストリンから水酸基への糖転移を触媒するが、これまでの実施例から、その水酸基結合する化合物が比較的水溶性が高い事が重要である。 The novel CGTase (CspCGT13) was also subjected to multiple sequence alignment with other well-characterized CGTases. From the alignment, the CGTase-specific sequence conservation was found in the four conserved regions identified for amylolytic enzymes (regions I, II, III and IV) (Table II) (MacGregor et al. 2001). The enzymes from the α-amylase family all share a similar α-retaining catalytic mechanism but can have different reaction and product specificities. One family member, cyclodextrin glycosyltransferase (CGTase), has an uncommonly high transglycosylation activity and is able to form cyclodextrins. We have determined the 2.0 and 2.5 Å X-ray structures of E257A/D229A CGTase in complex with C1a-8* CI 生産菌Paenibacillus sp.
For CGTase this mechanism can easily be imagined with the aid of a maltononaose substrate bound in the active site , as derived from the X‐ray structure of the enzyme complexed with a maltononaose inhibitor . From this complex, either a cyclization or a disproportionation reaction can …
CGTase activity decreased 20 fiold when incubation temperature was increased from 28 to 37 degreesC, and decreased 2.1- fold when the initial pH was lowered from 10.3 to 7.4. 2012-12-12
Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.) Expired - Lifetime Application number US07/927,316 Inventor Gerhard Schmid CGTase (EC 126.96.36.199) produced by mesophilic, thermophilic, alkaliphilic, and halophilic bacilli were used for transglycosylating stevioside and rebaudiosides A with the use of starch or cyclo-dextrine as donor. CGTases produced by Bacillus stearothermophilus B-5076 B. … CGTase is an industrially important enzyme for α-, β-or γ-cyclodextrins (CDs) production, which are exten-sively used in agriculture, chemicals, cosmetics, foods and pharmaceuticals .
Objectives: Cyclodextrin glucanotransferase (CGTase) is a multifunctional industrial enzyme, which undergoes cyclization reaction to converts starch into Cyclodextrin (CD). Due to their potential properties, CDs had been discovered to have numerous application in food industries, pharmaceutical, agriculture and also environmental engineering.
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CI 生産菌 Paenibacillus sp. 598K 株における CGTase 遺伝子の発見および CITase と CGTase. の生産制御機構.
AU - Svensson, David. AU - Adlercreutz, Patrick.
598K 株における CGTase 遺伝子の発見および CITase と CGTase. の生産制御機構.