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通过用糊精(含8-12个D-葡萄糖残基)做底物,以碘显色,在460nm监测光吸收的变化,测定淀粉麦芽四糖酶活力的结果表明:测活体系中含有一定量的钙离子.酶的测活曲线(在A_(460)<0.08的吸收范围)有较好的线性,该方法比间断法简便,快速,并且在测定淀粉麦芽四糖酶盐酸胍变性的失活动力学过程中.具有较好的重复性,可能成为淀粉麦芽寡糖酶测活的常用方法. 相似文献
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淀粉麦芽寡糖酶的连续测活 总被引:1,自引:0,他引:1
通过用糊精(含8-12个D-葡萄糖残基)做底物,以碘显色,在460nm监测光吸收的变化,测定淀粉麦芽四糖酶活力的结果表明:测活体系中含有一定量的钙离子.酶的测活曲线(在A_(460)<0.08的吸收范围)有较好的线性,该方法比间断法简便,快速,并且在测定淀粉麦芽四糖酶盐酸胍变性的失活动力学过程中.具有较好的重复性,可能成为淀粉麦芽寡糖酶测活的常用方法. 相似文献
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Immobilization of glucoamylase by adsorption on carbon supports and its application for heterogeneous hydrolysis of dextrin 总被引:1,自引:0,他引:1
Glucoamylase (GA) was immobilized by adsorption on carbon support: on Sibunit, on bulk catalytic filamentous carbon (bulk CFC) and on activated carbon (AC). This was used to prepare heterogeneous biocatalysts for the hydrolysis of starch dextrin. The effect of the texture characteristics and chemical properties of the support surface on the enhancement of the thermal stability of the immobilized enzyme was studied, and the rates of the biocatalyst's thermal inactivation at 65-80 degrees C were determined. The thermal stability of glucoamylase immobilized on different carbon supports was found to increase by 2-3 orders of magnitude in comparison with the soluble enzyme, and decrease in the following order: GA on Sibunit>GA on bulk CFC>GA on AC. The presence of the substrate (dextrin) was found to have a significant stabilizing effect. The thermal stability of the immobilized enzyme was found to increase linearly when the concentration of dextrin was increased from 10 wt/vol % to 50 wt/vol %. The total stabilization effect for glucoamylase immobilized on Sibunit in concentrated dextrin solutions was about 10(5) in comparison with the enzyme in a buffer solution. The developed biocatalyst, 'Glucoamylase on Sibunit' was found to have high operational stability during the continuous hydrolysis of 30-35 wt/vol % dextrin at 60 degrees C, its inactivation half-time (t1/2) exceeding 350 h. To improve the starch saccharification productivity, an immersed vortex reactor (IVR) was designed and tested in the heterogeneous process with the biocatalyst 'Glucoamylase on Sibunit'. The dextrin hydrolysis rate, as well as the process productivity in the vortex reactor, was found to increase by a factor of 1.2-1.5 in comparison with the packed-bed reactor. 相似文献
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Xavier Roussel Christine Lancelon-Pin Anders Viksø-Nielsen Agnès Rolland-Sabaté Florent Grimaud Gabrielle Potocki-Véronèse Alain Buléon Jean-Luc Putaux Christophe D'Hulst 《Biochimica et Biophysica Acta (BBA)/General Subjects》2013
Background
Glycogen and starch branching enzymes catalyze the formation of α(1 → 6) linkages in storage polysaccharides by rearrangement of preexisting α-glucans. This reaction occurs through the cleavage of α(1 → 4) linkage and transfer in α(1 → 6) of the fragment in non-reducing position. These enzymes define major elements that control the structure of both glycogen and starch.Methods
The kinetic parameters of the branching enzyme of Rhodothermus obamensis (RoBE) were established after in vitro incubation with different branched or unbranched α-glucans of controlled structure.Results
A minimal chain length of ten glucosyl units was required for the donor substrate to be recognized by RoBE that essentially produces branches of DP 3–8. We show that RoBE preferentially creates new branches by intermolecular mechanism. Branched glucans define better substrates for the enzyme leading to the formation of hyper-branched particles of 30–70 nm in diameter (dextrins). Interestingly, RoBE catalyzes an additional α-4-glucanotransferase activity not described so far for a member of the GH13 family.Conclusions
RoBE is able to transfer α(1 → 4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new α(1 → 4) linkages yielding to the elongation of linear chains subsequently used for further branching. This result is a novel case for the thin border that exists between enzymes of the GH13 family.General significance
This work reveals the original catalytic properties of the thermostable branching enzyme of R. obamensis. It defines new approach to produce highly branched α-glucan particles in vitro. 相似文献5.
Starch dextrins of different molecular sizes (DPn 311, 142 and 39) were prepared by hydrolyzing a high amylose maize starch in acidic alcohol solutions. The dextrins were dissolved in an aqueous dimethyl sulfoxide solution (90% DMSO), and then the solution was allowed to migrate down into n-butanol separated by a membrane filter. The complex was gradually formed between the dextrin and butanol, and precipitated in the butanol layer. The dextrin–butanol complex yielded V6-I type crystals with broad reflections (d-spacings 1.123, 0.657 and 0.429 nm) under X-ray diffractograms. Platelets of average length less than 100 nm, interspersed in amorphous matrices, were observed in complexes of DPn 311 and 142, but that of DPn 39 showed different morphology, and the formation of complexes was limited. By hydrolyzing the complex of DPn 311 with α-amylase, amorphous matrices were selectively removed, and crystallites of 23–72 nm showing a V6-I X-ray diffraction pattern were obtained. However, crystallites in complexes of DPn 142 and 39 were eroded by amylolysis, forming large aggregates. 相似文献
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A rapid method was developed to determine the molecular weight (Mn) of β-limit dextrin and dextrans (Leuconostoc mesenteroides) using a reducing power approach. The Mn of the β-limit dextrin was also estimated from high performance liquid chromatography (HPLC). Chromatograms were pre-calibrated with the dextrans. The three dextrins had a Mn of 2.09, 2.40 and 2.63 × 105 using the reducing method and 4.80, 5.90 and 2.80 × 105 by HPLC. The method could be employed to estimate Mn of dextrins where chromatographic systems were not available. 相似文献
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