Starch‐Processing Enzymes

Maarel, Marc J. E. C. van der

doi:10.1002/9781444309935.ch14

Cited by 4 publications

(3 citation statements)

References 35 publications

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“…In addition, no differences were shown due to the type of enzyme added. It has been reported that the new branched structure of starches treated with branching enzyme leads to weakening of the interactions among amylopectin molecules, giving rise to solutions with relatively low viscosity [26]. The same flat pasting profile was reported when treating extruded flours with amylolytic and cyclodextrin glucanotransferase enzymes [19,27].…”

Section: Pasting Propertiessupporting

confidence: 56%

Changes in physicochemical properties and in vitro starch digestion of native and extruded maize flours subjected to branching enzyme and maltogenic α-amylase treatment

Román

Martínez

Rosell

et al. 2017

International Journal of Biological Macromolecules

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Extrusion is an increasingly used type of processing which combined with enzymatic action could open extended possibilities for obtaining clean label modified flours. In this study, native and extruded maize flours were modified using branching enzyme (B) and a combination of branching enzyme and maltogenic α-amylase (BMA) in order to modulate their hydrolysis properties. The microstructure, pasting properties, in vitro starch hydrolysis and resistant starch content of the flours were investigated. Whereas BMA treatment led to greater number of holes on the granule surface in native samples, B and BMA extruded samples showed rougher surfaces with cavities. A reduction in the retrogradation trend was observed for B and BMA native flours, in opposition to the flat pasting profile of their extruded counterparts. The glucose release increased gradually for native flours as the time of reaction did, whereas for extruded flours a fast increase of glucose release was observed during the first minutes of reaction, and kept till the end, indicating a greater accessibility to their porous structure. After 16 hours of hydrolysis, resistant starch content was lower for treated extruded samples. These results suggested that, in enzymatically treated extruded samples, changes produced at larger hierarchical levels in their starch structure could have masked a slowdown in the starch digestion properties.

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Section: Pasting Propertiessupporting

confidence: 56%

Changes in physicochemical properties and in vitro starch digestion of native and extruded maize flours subjected to branching enzyme and maltogenic α-amylase treatment

Román

Martínez

Rosell

et al. 2017

International Journal of Biological Macromolecules

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“…This limitation leads to the use of high-concentration α-amylase, which is not economically viable. Various strategies have been applied to improve α-amylase performance [2,15,16,17], including discovery of thermostable enzymes and protein modifications that have resulted in several commercial products [18,19]. Immobilization is another possible way to improve current starch-processing methods [16].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of α-Amylase from Anoxybacillus sp. SK3-4 on ReliZyme and Immobead Supports

et al. 2016

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α-Amylase from Anoxybacillus sp. SK3-4 (ASKA) is a thermostable enzyme that produces a high level of maltose from starches. A truncated ASKA (TASKA) variant with improved expression and purification efficiency was characterized in an earlier study. In this work, TASKA was purified and immobilized through covalent attachment on three epoxide (ReliZyme EP403/M, Immobead IB-150P, and Immobead IB-150A) and an amino-epoxide (ReliZyme HFA403/M) activated supports. Several parameters affecting immobilization were analyzed, including the pH, temperature, and quantity (mg) of enzyme added per gram of support. The influence of the carrier surface properties, pore sizes, and lengths of spacer arms (functional groups) on biocatalyst performances were studied. Free and immobilized TASKAs were stable at pH 6.0-9.0 and active at pH 8.0. The enzyme showed optimal activity and considerable stability at 60 • C. Immobilized TASKA retained 50% of its initial activity after 5-12 cycles of reuse. Upon degradation of starches and amylose, only immobilized TASKA on ReliZyme HFA403/M has comparable hydrolytic ability with the free enzyme. To the best of our knowledge, this is the first report of an immobilization study of an α-amylase from Anoxybacillus spp. and the first report of α-amylase immobilization using ReliZyme and Immobeads as supports.

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“…Although the double helical structures mostly due to exterior chains of amylopectin are common to all types, packing profiles of double helices are different between A-and B-types; A-type has a compact structure with a low water content, while B-type has a more open structure with a hydrated helical center. Industrial enzymatic decomposition of starch proceeds through gelatinization (30-40% starch slurry, heating for 5 min at 105°C), liquefaction (1-2 h at 95-100°C) and saccharification (72 h at 60°C) to glucose whose concentration was 97% in the saccharified products (Van Der Maarel, 2010). Production of glucose from starch has economically superiority but has a defect in competition with supply of food from starchy polysaccharides.…”

Section: Storage Polysaccharidementioning

confidence: 99%