Influence of molecular structure on the susceptibility of starch to α-amylase

Autor: Marcia Maria de Souza Moretti, Flávia Villas-Boas, Célia Maria Landi Franco, Yasmin Yamauti
Přispěvatelé: Universidade Estadual Paulista (Unesp)
Rok vydání: 2019
Předmět:
Zdroj: Scopus
Repositório Institucional da UNESP
Universidade Estadual Paulista (UNESP)
instacron:UNESP
ISSN: 1873-426X
Popis: Made available in DSpace on 2019-10-06T15:43:01Z (GMT). No. of bitstreams: 0 Previous issue date: 2019-06-01 Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) The effect of the molecular structure of sweet potato (SPS), cassava (CAS)and high amylose maize (HAS)starches on the susceptibility to fungal and maltogenic α-amylases was investigated. The logarithm of the slope (LOS)and non-linear least-squares (NLLS)methods were used for fitting hydrolysis kinetics data. The malto-oligosaccharides released during hydrolysis were quantified and the hydrolysis residues were analyzed. The hydrolysis kinetic curves were well fitted to the LOS and NLLS models. SPS, CAS and HAS were hydrolyzed in one single phase by fungal α-amylase while two hydrolysis phases were identified for the root starches and a single phase for HAS, when maltogenic α-amylase was used. The lowest percentage of residual starch was found for CAS, independent of enzyme source, due to the high proportion of amylopectin short chains in this starch. On the other hand, the high proportion of HAS long chains contributed to its increased starch degradation rate coefficient during fungal α-amylase hydrolysis, while the high amylose content favored the endo-action pattern of maltognic α-amylase. Independent of starch source, malto-oligosaccharides of different sizes, especially G2-G5, were released after the fungal α-amylase action which hydrolyzes mainly inner and long amylopectin chains. Mainly maltose was produced in the maltogenic α-amylase hydrolysis which breaks the outer amylopectin chains by exo-action and amylose chains by endo-action. The starch molecular structure strongly interferes in both enzyme susceptibility and the action mechanism, as well as in the distribution and amount of products released. UNESP –– São Paulo State University Department of Food Engineering and Technology UNESP –– São Paulo State University Department of Food Engineering and Technology FAPESP: 2017/19521-1 CNPq: 307942/2015-5
Databáze: OpenAIRE
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