Cyclodextrin Chemistry: Preparation And Application CDON

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First starch is liquified either by heat treatment or Cyklodextrin glucanotransferas (CGTase, EC 2.4.1.19) produktion med användning av ny alkalifil Microbacterium terrae KNR 9 undersöktes genom nedsänkt CGTase, a novel antimicrobial protein from Bacillus cereus YUPP-10, suppresses Verticillium dahliae and mediates plant defence responses Mol Plant Pathol. 2020 Nov 23. doi: 10.1111/mpp.13014. Online ahead of print. Cyclodextrin glycosyl transferase (also Cyclodextrin glucosyltransferase or Cyclodextrin glucanotransferase) or CGTase for short (EC 2.4.1.19) is a bacterial enzyme belonging to the same family of the α-amylase specifically known as glycosyl-hydrolase family 13.

Cgtase

2014-12-15 γ-CGTase activity increased, in both control cultures (from 71.7 to 97.0%) and cultures supplemented with β-cyclodextrin (from 56.3 to 91.8%). More importantly, the effect of β-cyclodextrin on total soluble γ-CGTase activity, as a multiple of the control value, increased 2008-08-26 The purified CGTase has a pI value of 4.2. The optimum pH of 6.0 and 60 °C temperature were found to be the best for CGTase activity. Purified CGTase showed 5.18 kcal/mol activation energy (Ea). 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 more. The cyclodextrin glucanotransferase (CGTase, EC 2.4.1.19) gene from Bacillus sp.

At 300mM Î±-CD, varied DDM concentration and 60Â°C, the reaction obeyed Michaelis-Menten kinetics with a K(m) value of 18mM and a V(max) value of 100U/mg enzyme.

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CGTase has been found in many bacteria, including Bacillus spp. (Chen et al., 2018; Gimenez et al., 2019; Yap et al., 2010) and Paenibacillus spp. (Castillo et al., 2018).

Molecular Characterization of Oil Degrading Bacteria Bacillus

1996-01-01 2009-07-08 Cyclodextrin glycosyl transferase (CGTase, EC 2.4.1.19) is an important industrial enzyme, unique in its ability to convert starch and related glycans into non-reducing, cyclic malto-oligosacchrarides called cyclodextrins (CDs) via a cyclization reaction, an intramolecular transglycosylation reaction [1]. 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.

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. However, the low specificity and activity of soluble γ-CGTase increase the production cost of γ-CD, thereby limiting its applications. 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.
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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.

Organism. Anaerobranca gottschalkii. Status. Unreviewed-Annotation score: -Protein inferred from homology i. Function i Cofactor i. Ca 2+ ARBA annotation.
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Actually, CGTase has been discovered in a great number of Bacillus, Thermoanaerobacter, Brevibacterium and Thermoanaerobacterium [8,9,10]. CGTase, a novel antimicrobial protein from Bacillus cereus YUPP-10, suppresses Verticillium dahliae and mediates plant defence responses. Mol Plant Pathol. 2020 Nov 23. doi: 10.1111/mpp.13014. Online ahead of print. The CGTase was eluted by adding 45 ml of CGTase buffer containing 0.05 g maltose and 0.6 g KCl to the starch and incubated at 50 °C for 1.5 h.

AU - Lundemo, Pontus. AU - Svensson, David. AU - Adlercreutz, Patrick. PY - 2011.
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Molecular Characterization of Oil Degrading Bacteria Bacillus

Function i Cofactor i. Ca 2+ ARBA annotation.