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In Depth Study of a New Highly Efficient Raw Starch Hydrolyzing alpha-Amylase from Rhizomucor sp

Abstract : A new alpha-amylase from Rhizomucor sp. (RA) was studied in detail due to its very efficient hydrolysis of raw starch granules at low temperature (32 degrees C). RA contains a starch binding domain (SBD) connected to the core amylase catalytic domain by a O-glycosylated linker. The mode of degradation of native maize starch granules and, in particular, the changes in the starch structure during the hydrolysis, was monitored for hydrolysis of raw starch at concentrations varying between 0.1 and 31%. RA was compared to porcine pancreatic alpha-amylase (PPA), which has been widely, studied either on resistant starch or as a model enzyme in solid starch hydrolysis studies. RA is particularly efficient on native maize starch and release glucose only. The hydrolysis rate reaches 75% for a 31% starch solution and is complete at 0.1% starch concentration. The final hydrolysis rate was dependent on both starch concentration and enzyme amount applied. RA is also very efficient in hydrolyzing the crystalline domains in the maize starch granule. The major A-type crystalline structure is more rapidly degraded than amorphous domains in the first stages of hydrolysis. This is in agreement with the observed preferential hydrolysis of amylopectin, the starch constituent that forms the backbone of the crystalline part of the granule. Amy lose lipid complexes present in most cereal starches are degraded in a second stage, yielding amylose fragments that then reassociate into B-type crystalline structures, forming the final resistant fraction.
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Submitted on : Friday, May 29, 2020 - 4:43:47 AM
Last modification on : Wednesday, December 9, 2020 - 5:58:05 PM

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Georges Tawil, Anders Vikso-Nielsen, Agnès Rolland-Sabaté, Paul Colonna, Alain Buleon. In Depth Study of a New Highly Efficient Raw Starch Hydrolyzing alpha-Amylase from Rhizomucor sp. Biomacromolecules, American Chemical Society, 2011, 12 (1), pp.34 - 42. ⟨10.1021/bm100913z⟩. ⟨hal-02646404⟩

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