Glycosyltransferas (CGTase). Cyclodextrin (CD) and. Paenibacillus Sp A11, CLIPtechnique. Stipendiat. 24B Korpraditskul,. Prof. Dr. Vichai. Agrarwissen- schaft.
2017-05-19
Analysis of the nucleotide sequence revealed the presence of an open reading frame of 2,109 bp and encoded The product specificity and pH optimum of the thermostable cyclodextrin glycosyltransferase (CGTase) from Thermoanaerobacterium thermosulfurigenes EM1 was engineered using a combination of x-ray crystallography and site-directed mutagenesis. 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). 2008-08-26 · The cyclodextrin glucanotransferase (CGTase, EC 2.4.1.19) gene from Bacillus sp. G1 was successfully isolated and cloned into Escherichia coli.
and B. circulance, respectively. The CGTase activity in culture broths was observed increasing with increase in initial inoculum level for Fig. 1⎯CGTase production pattern in Bacillus sp. and B. circulance during growth phase 2014-03-13 cgtase. Organism. Paenibacillus pabuli. Status.
Cyclodextrin glucanotransferase (CGTase) is an important industrial enzyme which is used to produce cyclodextrins. CGTase genes from more than 30 bacteria have been isolated and several of the enzymes have been identified and biochemically characterized. For a better understanding of the reaction mechanism and function of CGTase, the enzyme has been analyzed at gene level and protein level
2.4.1.19) is a member of the glycoside hydrolase family 13, also known as the α-amylase family. This enzyme consists of five domains named A, B, C, D and E. The A domain folds into a catalytic (β/α) 8 barrel. First starch is liquified either by heat treatment or using α-amylase, then CGTase is added for the enzymatic conversion. CGTases produce mixtures of cyclodextrins, thus the product of the conversion results in a mixture of the three main types of cyclic molecules, in ratios that are strictly dependent on the enzyme used: each CGTase has its Purpose γ-Cyclodextrin glycosyltransferase (γ-CGTase) catalyzes the biotransformation of low-cost starch into valuable γ-cyclodextrin (γ-CD), which is widely applied in biotechnology, food, and pharmaceutical industries.
Ca2+ affected β-CGTase thermostability significantly. After Ca2+ was added to β-CGTase solution to a final concentration of 5 mM followed by incubation for 120 min at 60 °C, residual activity of β-CGTase was 88.3%, which was much higher than that without Ca2+. However, Ca2+ had a small contribution to α-CGTase thermostability.
Stipendiat. 24B Korpraditskul,. Prof.
We discovered that CGTase has antimicrobial activity and induces resistance. In addition, we have revealed the key do-mains responsible for its hydrolytic activity and resistance induction. Further experiments demonstrated that CGTase is a potential func -
CGTase is an important industrial enzyme that can transfer starch to glycosyl groups to form cyclodextrin (Li et al., 2014c; Qi et al., 2007). CGTase has been found in many bacteria, including Bacillus spp.
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In this work, the CGTase produced by Bacillus clausii strain E16 was used to produce CD from maltodextrin and different starches (commercial soluble starch, corn, cassava, sweet potato, and waxy corn starches) as substrates. The E-domain of cyclodextrin glycosyltransferase (CGTase) (EC 2.4.1.19) from Bacillus circulans strain 251 is a putative raw starch binding domain. Analysis of the maltose-dependent CGTase crystal structure revealed that each enzyme molecule contained three maltose molecules, situated at contact poi ….
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Cyclodextrin glucanotransferase (CGTase) catalyzed synthesis of dodecyl glucooligosides by transglycosylation using alpha-cyclodextrin or starch · Find us on
Therefore, the present study aimed Cyclodextrin glucanotransferase (CGTase) is a unique type of α - amylase which produces cyclodextrins (CDs) from starch, besides degrading starch to maltooligosaccharides. Most of the CGTase producing bacteria are naturally from the Bacillus genus and most of these Bacillus species produce the CGTase enzyme extracellularly, due to the functioning of signal peptide.In the cyclization reaction, starch is cleaved and the intramolecular ends are joined to form closed circular structures. Publisher Summary This chapter discusses the purification and action of cyclodextrin-producing enzyme (CGTase).
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γ-Cyclodextrin glycosyltransferase (γ-CGTase) catalyzes the biotransformation of low-cost starch into valuable γ-cyclodextrin (γ-CD), which is widely applied in biotechnology, food, and pharmaceutical industries. However, the low specificity and activity of soluble γ-CGTase increase the production cost of γ-CD, thereby limiting its applications.
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). 2008-08-26 · The cyclodextrin glucanotransferase (CGTase, EC 2.4.1.19) gene from Bacillus sp. G1 was successfully isolated and cloned into Escherichia coli.