Binding of Tris to Bacillus licheniformis &amp;#945;-Amylase Can Affect Its Starch Hydrolysis Activity

Ghalanbor, Zahra; Ghaemi, Nasser; Marashi, Sayed-Amir; Amanlou, Massoud; Habibi-Rezaei, Mehran; Khajeh, Khosro; Ranjbar, Bijan; Chan, Yau Sang; Wong, Jack Ho; Ng, Tzi Bun

doi:10.2174/092986608783489616

Cited by 29 publications

(16 citation statements)

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“…The inhibition of the enzymatic activity by 2-amino-2-hydroxymethyl-propane-1,3-diol (Tris) was also reported for β-glucosidase from Agrobacterium faecalis [20]. In both cases, the inhibition caused by Tris is consistent with that seen for other enzymes such as β-galactosidase [7,21], α-amylase [22], and α-galactosidase [23] and is presumably the reflection of the general affinity of glycosidases for hydroxylated amines [20,24]. …”

Section: Resultssupporting

confidence: 58%

Cloning and characterization of a novel cold-active glycoside hydrolase family 1 enzyme with β-glucosidase, β-fucosidase and β-galactosidase activities

et al. 2013

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BackgroundCold-active enzymes, sourced from cold-adapted organisms, are characterized by high catalytic efficiencies at low temperatures compared with their mesophilic counterparts, which have poor activity. This property makes them advantageous for biotechnology applications as it: (i) saves energy costs, (ii) shortens the times for processes operated at low temperatures, (iii) protects thermosensitive substrates or products of the enzymatic reaction, (iv) prevents undesired chemical transformations, and (v) prevents the loss of volatile compounds.ResultsA bglMKg gene that encodes a monomeric cold-active glycoside hydrolase family 1 enzyme with an apparent molecular mass of 50 kDa was isolated by the functional screening of a marine metagenomic library. The BglMKg enzyme was expressed in E. coli, purified by FPLC and characterized. The recombinant BglMKg could effectively hydrolyze various chromogenic substrates and β-linked oligosaccharides, and had remarkably high β-galactosidase, β-glucosidase and β-fucosidase activities. Because of the lack of information about the usefulness of β-fucosidases in industry, further characterization of the enzymatic properties of BglMKg was only carried out with substrates specific for β-glucosidase or β-galactosidase. The BglMKg had maximal β-galactosidase and β-glucosidase activities at approximately 40°C and 45°C, respectively. The optimum pH for β-galactosidase activity was 6.5, whereas the optimum pH for β-glucosidase activity was 7.5. In general, the enzyme was stable below 30°C and from pHs 6.0 to 8.0. The results of the kinetic studies revealed that BglMKg more efficiently hydrolyzed β-glucosidase substrates than β-galactosidase ones.ConclusionsBglMKg is a small, monomeric, cold-active β-glucosidase with additional enzymatic activities. It was efficiently expressed in E. coli indicating that BglMKg might be a candidate for industrial applications.

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Section: Resultssupporting

confidence: 58%

Cloning and characterization of a novel cold-active glycoside hydrolase family 1 enzyme with β-glucosidase, β-fucosidase and β-galactosidase activities

et al. 2013

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“…The authors showed a competitive inhibition by Tris with inhibition constants of 13–14 m m . A competitive inhibition of an α‐amylase from Bacillus licheniformis by Tris with a K i of 13.12 m m has also been reported . Accompanying docking studies indicated a high binding potential of Tris at the active site of the enzyme.…”

Section: Discussionmentioning

confidence: 88%

“…The corresponding K i values (Table ) for both buffers were determined by replotting the slopes calculated from the Lineweaver–Burk plots against the concentration of Tris and MOPS . The results showed that MOPS is the stronger inhibitor of both enzymes with significantly lower K i values compared to Tris.…”

Section: Resultsmentioning

confidence: 99%

Effect of Tris, MOPS, and phosphate buffers on the hydrolysis of polyethylene terephthalate films by polyester hydrolases

et al. 2016

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The enzymatic degradation of polyethylene terephthalate (PET) occurs at mild reaction conditions and may find applications in environmentally friendly plastic waste recycling processes. The hydrolytic activity of the homologous polyester hydrolases LC cutinase (LCC) from a compost metagenome and TfCut2 from Thermobifida fusca KW3 against PET films was strongly influenced by the reaction medium buffers tris(hydroxymethyl)aminomethane (Tris), 3‐(N‐morpholino)propanesulfonic acid (MOPS), and sodium phosphate. LCC showed the highest initial hydrolysis rate of PET films in 0.2 m Tris, while the rate of TfCut2 was 2.1‐fold lower at this buffer concentration. At a Tris concentration of 1 m, the hydrolysis rate of LCC decreased by more than 90% and of TfCut2 by about 80%. In 0.2 m MOPS or sodium phosphate buffer, no significant differences in the maximum initial hydrolysis rates of PET films by both enzymes were detected. When the concentration of MOPS was increased to 1 m, the hydrolysis rate of LCC decreased by about 90%. The activity of TfCut2 remained low compared to the increasing hydrolysis rates observed at higher concentrations of sodium phosphate buffer. In contrast, the activity of LCC did not change at different concentrations of this buffer. An inhibition study suggested a competitive inhibition of TfCut2 and LCC by Tris and MOPS. Molecular docking showed that Tris and MOPS interfered with the binding of the polymeric substrate in a groove located at the protein surface. A comparison of the Ki values and the average binding energies indicated MOPS as the stronger inhibitor of the both enzymes.

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“…Studies suggest that Tris inhibits the function of enzymes such as aminopeptidase and alpha-amylase (Desmarais et al, 2002; Ghalanbor et al, 2008). In addition, Tris, TES and related buffer compounds have been shown to react with nerve agents to form new products (Gab et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

Allosteric modulation of alpha4beta2 nicotinic acetylcholine receptors by HEPES

Weltzin

Huang

Schulte

2014

European Journal of Pharmacology

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A number of new positive allosteric modulators (PAMs) have been reported that enhance responses of neuronal alpha7 and alpha4beta2 nicotinic acetylcholine receptor subtypes to orthosteric ligands. PAMs represent promising new leads for the development of therapeutic agents for disorders involving alterations in nicotinic neurotransmission including Autism, Alzheimer's and Parkinson's disease. During our recent studies of alpha4beta2 PAMs, we identified a novel effect of 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES). The effects of HEPES were evaluated in a phosphate buffered recording solution using two-electrode voltage clamp techniques and alpha4beta2 and alpha7 nicotinic acetylcholine receptor subtypes expressed in Xenopus laevis oocytes. Acetylcholine induced responses of high-sensitivity alpha4beta2 receptors were potentiated 190% by co-exposure to HEPES. Responses were inhibited at higher concentrations (bell-shaped concentration/response curve). Coincidentally, at concentrations of HEPES typically used in oocyte recording (5–10 mM), the potentiating effects of HEPES are matched by its inhibitory effects, thus producing no net effect. Mutagenesis results suggest HEPES potentiates the high-sensitivity stoichiometry of the alpha4beta2 receptors through action at the beta2+/beta2− interface and is dependent on residue beta2D218. HEPES did not potentiate low-sensitivity alpha4beta2 receptors and did not produce any observable effect on acetylcholine induced responses on alpha7 nicotinic acetylcholine receptors.

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Binding of Tris to Bacillus licheniformis α-Amylase Can Affect Its Starch Hydrolysis Activity

Cited by 29 publications

References 0 publications

Cloning and characterization of a novel cold-active glycoside hydrolase family 1 enzyme with β-glucosidase, β-fucosidase and β-galactosidase activities

Cloning and characterization of a novel cold-active glycoside hydrolase family 1 enzyme with β-glucosidase, β-fucosidase and β-galactosidase activities

Effect of Tris, MOPS, and phosphate buffers on the hydrolysis of polyethylene terephthalate films by polyester hydrolases

Allosteric modulation of alpha4beta2 nicotinic acetylcholine receptors by HEPES

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