Oligosaccharide synthesis by reversed catalysis using α-amylase from Bacillus licheniformis

Chitradon, Lerluck; Mahakhan, Polson; Bucke, C.

doi:10.1016/s1381-1177(00)00110-7

Cited by 10 publications

(12 citation statements)

References 25 publications

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“…Alkyl glucosides were synthesised from starch and alcohols using Aspergillus oryzae a-amylase as the catalyst (Larsson, Svensson, & Adlercreutz, 2005). Chitradon, Mahakhan, and Bucke (2000) reported the oligosaccharide synthesis by the reversed catalytic reaction using a-amylase in the presence of soluble starch and added b-methylglucoside, cellobiose and mannose. Moreno et al (2010) investigated the synthesis of neotrehalose by Thermotoga maritima a-amylase.…”

Section: Stevioside (13-[2-o-b-d-glucopyranosyl-b-d-glucopyranosyl) Oxy]mentioning

confidence: 99%

Modification of stevioside using transglucosylation activity of Bacillus amyloliquefaciens α-amylase to reduce its bitter aftertaste

Yang

Xiao

et al. 2013

LWT - Food Science and Technology

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Section: Stevioside (13-[2-o-b-d-glucopyranosyl-b-d-glucopyranosyl) Oxy]mentioning

confidence: 99%

Modification of stevioside using transglucosylation activity of Bacillus amyloliquefaciens α-amylase to reduce its bitter aftertaste

Yang

Xiao

et al. 2013

LWT - Food Science and Technology

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“…α-Amylases and related amylolytic enzymes are among the most important enzymes and of great significance in the present day biotechnology. They could be potentially useful in the semisynthetic chemistry for the formation of oligosaccharides by transglycosylation [ 16 ]. The spectrum of amylase application has widened in many other fields, such as clinical, medicinal and analytical chemistry; as well as their widespread application in starch saccharification and in the textile, food, paper and pharmaceutical industries [ 17 - 20 ].…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of α-Amylase from Miswak Salvadora persica

Mohamed

Almulaiky

Ahmed

et al. 2014

BMC Complement Altern Med

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BackgroundThe miswak (Salvadora persica) is a natural toothbrush. It is well known that very little information has been reported on enzymes in miswak as medicinal plant. Recently, we study peroxidase in miswak. In the present study, the main goal of this work is to purify and characterize α-amylase from miswak. The second goal is to study the storage stability of α-amylase in toothpaste.MethodThe purification method included chromatographaphy of miswak α-amylase on DEAE-Sepharose column and Sephacryl S-200 column. Molecular weight was determined by gel filtration and SDS-PAGE.ResultsFive α-amylases A1, A4a, A4b, A5a and A5b from miswak were purified and they had molecular weights of 14, 74, 16, 30 and 20 kDa, respectively. α-Amylases had optimum pH from 6 to 8. Affinity of the substrates toward all enzymes was studied. Miswak α-amylases A1, A4a, A4b, A5a and A5b had Km values for starch and glycogen of 3.7, 3.7, 7.1, 0.52, 4.3 mg/ml and 5.95, 5.9 4.16, 6.3, 6.49 mg/ml, respectively. The optimum temperature for five enzymes ranged 40°C- 60°C. Miswak α-amylases were stable up to 40°C- 60°C after incubation for 30 min. Ca+2 activated all the miswak α-amylases, while Ni2+, Co+2 and Zn+2 activated or inhibited some of these enzymes. The metal chelators, EDTA, sodium citrate and sodium oxalate had inhibitory effects on miswak α-amylases. PMSF, p-HMB, DTNB and 1,10 phenanthroline caused inhibitory effect on α-amylases. The analysis of hydrolytic products after starch hydrolysis by miswak α-amylases on paper chromatography revealed that glucose, maltose, maltotriose and oligosaccharide were the major products. Crude miswak α-amylase in the toothpaste retained 55% of its original activity after 10 months of storage at room temperature.ConclusionsFrom these findings, α-amylases from miswak can be considered as beneficial enzymes for pharmaceuticals. Therefore, we study the storage stability of the crude α-amylase of miswak, which contained the five α-amylases, in toothpaste. The enzyme in the toothpaste retained 55% of its original activity after 10 months of storage at room temperature.

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“…α‐Amylases can be found in microorganisms, plants and animals where they play a dominant role in carbohydrate metabolism. These enzymes and related amylolytic enzymes are widely used in biotechnology for starch degradation [4] and in synthetic chemistry for the formation of oligosaccharides by transglycosylation [5–7]. Furthermore, these enzymes are used as targets for drug design in attempts to treat diabetes, obesity, hyperlipemia and caries [8].…”

Section: Introductionmentioning

confidence: 99%

Action pattern and subsite mapping of Bacillus licheniformis α‐amylase (BLA) with modified maltooligosaccharide substrates

et al. 2002

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This study represents the first characterisation of the substrate-binding site of Bacillus licheniformis K K-amylase (BLA). It describes the first subsite map, namely, number of subsites, apparent subsite energies and the dual product specificity of BLA. The product pattern and cleavage frequencies were determined by high-performance liquid chromatography, utilising a homologous series of chromophore-substituted maltooligosaccharides of degree of polymerisation 4^10 as model substrates. The binding region of BLA is composed of five glycone, three aglycone-binding sites and a 'barrier' subsite.Comparison of the binding energies of subsites, which were calculated with a computer program, shows that BLA has similarity to the closely related Bacillus amyloliquefaciens K Kamylase. ß

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Oligosaccharide synthesis by reversed catalysis using α-amylase from Bacillus licheniformis

Cited by 10 publications

References 25 publications

Modification of stevioside using transglucosylation activity of Bacillus amyloliquefaciens α-amylase to reduce its bitter aftertaste

Modification of stevioside using transglucosylation activity of Bacillus amyloliquefaciens α-amylase to reduce its bitter aftertaste

Purification and characterization of α-Amylase from Miswak Salvadora persica

Action pattern and subsite mapping of Bacillus licheniformis α‐amylase (BLA) with modified maltooligosaccharide substrates

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