Acceptor specificity of amylomaltase from Corynebacterium glutamicum and transglucosylation reaction to synthesize palatinose glucosides

Naumthong, Wachiraporn; K, Ito; Pongsawasdi, Piamsook

doi:10.1016/j.procbio.2015.07.003

Cited by 6 publications

(2 citation statements)

References 52 publications

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“…The CAZyme families identified in both C. pseudotuberculosis biovars revealed the GH families involved in α-glucan metabolism, such as GH13, GH15 and GH77. The CAZymes responsible for α-glucan synthesis, which were all found in every genome of the analyzed dataset regardless of biovar, were represented by trehalose synthase (treS, GH13 subfamily 44), maltokinase (pep2, GT4), malosyltranferase (glgE, GH13 subfamily 3), 1,4-α-glucan branching enzyme (glgB, CBM48 + GH13 subfamily 9) [38,39] and GH77 corresponding to amylomaltase malQ with the ability to convert linear α-glucans into cyclic α-1,4-glucans [40].…”

Section: Detection Of Carbohydrate Active Enzymesmentioning

confidence: 99%

Ovine and Caprine Strains of Corynebacterium pseudotuberculosis on Czech Farms—A Comparative Study

Markova,

Langova,

Babak

et al. 2024

Microorganisms

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Caseous lymphadenitis (CLA) is a worldwide disease of small ruminants caused by Corynebacterium pseudotuberculosis, a facultative intracellular pathogen that is able to survive and multiply in certain white blood cells of the host. In this study, 33 strains of C. pseudotuberculosis were isolated from sheep and goats suffering from CLA on nine farms in the Czech Republic. All these strains were tested for their antibiotic susceptibility, ability to form a biofilm and resistance to the effects of commonly used disinfectant agents. To better understand the virulence of C. pseudotuberculosis, the genomes of strains were sequenced and comparative genomic analysis was performed with another 123 genomes of the same species, including ovis and equi biovars, downloaded from the NCBI. The genetic determinants for the virulence factors responsible for adherence and virulence factors specialized for iron uptake and exotoxin phospholipase D were revealed in every analyzed genome. Carbohydrate-Active Enzymes were compared, revealing the presence of genetic determinants encoding exo-α-sialidase (GH33) and the CP40 protein in most of the analyzed genomes. Thirty-three Czech strains of C. pseudotuberculosis were identified as the biovar ovis on the basis of comparative genome analysis. All the compared genomes of the biovar ovis strains were highly similar regardless of their country of origin or host, reflecting their clonal behavior.

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Section: Detection Of Carbohydrate Active Enzymesmentioning

confidence: 99%

Ovine and Caprine Strains of Corynebacterium pseudotuberculosis on Czech Farms—A Comparative Study

Markova,

Langova,

Babak

et al. 2024

Microorganisms

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“…Syrups from IMOs, which have a low viscosity and reduced sweetness including non digestable, can be applied as a substitute sugar for diabetics, to improve the intestinal microflora, or to prevent dental caries (Lee et al, 2002) e.g. palatinose glucosides (PGs) synthesis using as sucrose or palatinose in food products for health benefits (Naumthong et al, 2015).…”

Section: Applications Of Amylomaltasementioning

confidence: 99%

Enzymatic and computational analysis of large-ring cyclodextrin production by Corynebacterium glutamicum amylomaltase

Ngawiset

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Amylomaltase is a well-known glucanotransferase enzyme that can produce large-ring cyclodextrins (LR-CDs) via cyclization reaction. To determine important amino acid residues involved in LR-CDs production of amylomaltase from Corynebacterium glutamicum (CgAM), mutations at CA I and CA II subdomains were introduced by site-directed mutagenesis. P228Y, E231Y, A413F and G417F CgAM mutants were constructed from CgAM recombinant plasmid. The optimum pH and temperature of WT and mutants were around pH 6.0 - 7.5 and 25 - 35°C. The mutations did not affect the pH and temperature stability. In addition, WT and all mutated enzymes have Maltotriose (G3) as the best substrate for disproportionation activity. A413F possessed much lower specific activities of transglycosylation, starch degradation, disproportionation and cyclization activities than the WT enzyme. P228Y, E231Y and G417F exhibited similar specific activities of starch transglycosylation and starch degradation to the wild-type CgAM. P228Y had much lower disproportionation activity than the wild-type enzyme, while E231Y displayed higher disproportionation activity. This suggested that P228 and E231 of CgAM may play an important role in disproportionation. At 12 h, wild-type CgAM gave the principle CD of 27, whilst the principal product of P228Y, E231Y, A413F and G417F were CD36, CD25, CD38, and CD32, respectively. Molecular dynamic (MD) simulation showed that Y418, M474, L510, F534, Y23, R458, Q423, T666, Q475, L236, Q421, E231, Q420, N419 and Y235 might interact with LR-CDs.

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Highly efficient enzymatic preparation of isomalto-oligosaccharides from starch using an enzyme cocktail

Niu

Jian

et al. 2017

Electronic Journal of Biotechnology

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Acceptor specificity of amylomaltase from Corynebacterium glutamicum and transglucosylation reaction to synthesize palatinose glucosides

Cited by 6 publications

References 52 publications

Ovine and Caprine Strains of Corynebacterium pseudotuberculosis on Czech Farms—A Comparative Study

Ovine and Caprine Strains of Corynebacterium pseudotuberculosis on Czech Farms—A Comparative Study

Enzymatic and computational analysis of large-ring cyclodextrin production by Corynebacterium glutamicum amylomaltase

Highly efficient enzymatic preparation of isomalto-oligosaccharides from starch using an enzyme cocktail

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