Transglycosylation reactions of Thermotoga maritima α-amylase

Moreno, A.; Damián-Almazo, Juanita Yazmin; Miranda-Molina, Alfonso; Saab‐Rincón, Gloria; González, Fernando; Munguía, Agustín López

doi:10.1016/j.enzmictec.2009.12.002

Cited by 20 publications

(14 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Preliminary tests showed that the α-amylases were able to synthesise glycosides by reverse hydrolysis reaction using starch as the glycosyl donor and phenol as the glycosyl acceptor. The ability of α-amylases from other sources to synthesise glycoside had previously been reported (Park et al, 1999;Larson et al, 2005;Sugimoto et al, 2007;Moreno et al, 2010). It seems that the glycosyl residues transferred in this study were the maltose, maltotriose and probably maltotetraose.…”

Section: Discussionmentioning

confidence: 55%

“…In general, these reactions proceed via a glycosylenzyme intermediate, which is deglycosylated either by water (hydrolysis) or another glycosyl acceptor (transglycosylation). Thus, many α-amylases have been examined as catalysts for glycosylation of various phenolic compounds (Nishimura et al, 1994;Park et al, 1999) and alcohols (Moreno et al, 2010;Santamaria et al, 1999;Larsson et al, 2005). Concerning particularly insect digestive tract, some glycosidases were explored in tranglycosylation reaction (Kouamé et al, 2001;Yapi et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

“…3.2.1.1) are enzymes that catalyze the hydrolysis of internal α-1,4 linkages of starch molecules acting through a "retaining mechanism" (Sinnott, 1990) and belong to family 13 of glycosyl hydrolases (GH13). The α-amylases are widely distributed in nature and have found multiple applications in industry (Thippeswamy et al, 2006;Moreno et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Novel α-Amylases Amy A1 and Amy A2 from digestive tract of tropical house cricket Gryllodes sigillatus (Orthoptera: Gryllidae): hydrolysis and transglycosylation reactions

Kouadio¹,

Konan²,

Tetchi³

et al. 2012

ABJNA

View full text Add to dashboard Cite

The aim of the study was to investigate the ability of Amy A1 and Amy A2 α-amylases from digestive tract of the tropical house cricket Gryllodes sigillatus to hydrolyse the gelatinized starches of some tropical crops and their potentiality to catalyze tranglycosylation reactions. The Amy A1 and Amy A2 α-amylases hydrolyzed efficiently the starches from tubers (yam, cocoyam) and roots (cassava) to obtain reducing sugars content ranging from 22.2 µg to 62.1 µg after 6 hours incubation. However, the both α-amylases hydrolyzed less the starches from cereal (maize, millet). Otherwise, they catalyzed the transglycosylation reactions with soluble starch as donor and phenol as acceptor. The optimisation of the transfer product yield was studied as functions of pH, incubation time, concentration of donor and acceptor. Indeed, the obtained yield in experimental optimum conditions were 63.1 ± 0.27 % and 51.6 ± 0.03 % for Amy A1 and Amy A2 α-amylases respectively. On the basis of these results, α-amylases from the digestive tract of the cricket G. sigillatus appear to be a valuable tool for the glycosylation of phenolic compounds.

show abstract

Section: Discussionmentioning

confidence: 55%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Novel α-Amylases Amy A1 and Amy A2 from digestive tract of tropical house cricket Gryllodes sigillatus (Orthoptera: Gryllidae): hydrolysis and transglycosylation reactions

Kouadio¹,

Konan²,

Tetchi³

et al. 2012

ABJNA

View full text Add to dashboard Cite

show abstract

“…It can hydrolyze internal -1-4-glycosidic bonds in various -glucans, such as starch, amylose, amylopectin and glycogen, to yield mainly glucose and maltose as final products. Because AmyA has the advantage of being a saccharifying enzyme in a stable scaffold, we explored its properties in the transglycosylation and alcoholysis reactions (Damián-Almazo et al, 2008;Damian-Almazo et al, 2008;Moreno et al, 2010). In addition to the characterization reported by Lieb et al, we found that AmyA is capable of using small oligosaccharides (G2 to G7) as substrates for the transglycoslation reactions at short reaction times.…”

Section: Transglycosylation Reactions In Alpha-amylasesmentioning

confidence: 92%

“…When compared to other saccharifiyng -amylases, AmyA has a high transfer capacity. The enzyme generates 7.5 mg/ml of methyl-glucoside (Moreno et al, 2010), almost three times the maximum amount found for the A. niger -amylase and almost eight times the maximum amount found for the A. oryzae -amylase .…”

Section: Transglycosylation Reactions In Alpha-amylasesmentioning

confidence: 99%

Site-Directed Mutagenesis as Applied to Biocatalysts

Damián-Almazo¹,

Saab‐Rincón²

2013

Genetic Manipulation of DNA and Protein - Examples From Current Research

View full text Add to dashboard Cite

β-Mannanase-catalyzed synthesis of alkyl mannooligosides

Morrill

Månberger

Rosengren

et al. 2018

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

β-Mannanases catalyze the conversion and modification of β-mannans and may, in addition to hydrolysis, also be capable of transglycosylation which can result in enzymatic synthesis of novel glycoconjugates. Using alcohols as glycosyl acceptors (alcoholysis), β-mannanases can potentially be used to synthesize alkyl glycosides, biodegradable surfactants, from renewable β-mannans. In this paper, we investigate the synthesis of alkyl mannooligosides using glycoside hydrolase family 5 β-mannanases from the fungi Trichoderma reesei (TrMan5A and TrMan5A-R171K) and Aspergillus nidulans (AnMan5C). To evaluate β-mannanase alcoholysis capacity, a novel mass spectrometry-based method was developed that allows for relative comparison of the formation of alcoholysis products using different enzymes or reaction conditions. Differences in alcoholysis capacity and potential secondary hydrolysis of alkyl mannooligosides were observed when comparing alcoholysis catalyzed by the three β-mannanases using methanol or 1-hexanol as acceptor. Among the three β-mannanases studied, TrMan5A was the most efficient in producing hexyl mannooligosides with 1-hexanol as acceptor. Hexyl mannooligosides were synthesized using TrMan5A and purified using high-performance liquid chromatography. The data suggests a high selectivity of TrMan5A for 1-hexanol as acceptor over water. The synthesized hexyl mannooligosides were structurally characterized using nuclear magnetic resonance, with results in agreement with their predicted β-conformation. The surfactant properties of the synthesized hexyl mannooligosides were evaluated using tensiometry, showing that they have similar micelle-forming properties as commercially available hexyl glucosides. The present paper demonstrates the possibility of using β-mannanases for alkyl glycoside synthesis and increases the potential utilization of renewable β-mannans.Electronic supplementary materialThe online version of this article (10.1007/s00253-018-8997-2) contains supplementary material, which is available to authorized users.

show abstract

Transglycosylation reactions of Thermotoga maritima α-amylase

Cited by 20 publications

References 32 publications

Novel α-Amylases Amy A1 and Amy A2 from digestive tract of tropical house cricket Gryllodes sigillatus (Orthoptera: Gryllidae): hydrolysis and transglycosylation reactions

Novel α-Amylases Amy A1 and Amy A2 from digestive tract of tropical house cricket Gryllodes sigillatus (Orthoptera: Gryllidae): hydrolysis and transglycosylation reactions

Site-Directed Mutagenesis as Applied to Biocatalysts

β-Mannanase-catalyzed synthesis of alkyl mannooligosides

Contact Info

Product

Resources

About