Dataset Information

Improving Bread Quality with the Application of a Newly Purified Thermostable ?-Amylase from Rhizopus oryzae FSIS4.

ABSTRACT: A new thermostable ?-amylase from Rhizopus oryzae FSIS4 was purified for first time and recovered in a single step using a three-phase partitioning (TPP) system. The fungal ?-amylase, at a concentration of 1.936 U per kg of flour, was used in bread-making and compared to the commercial enzyme. The results showed a significant effect of the recovered ?-amylase in the prepared bread and allowed us to improve the quality of the bread. The study indicated clearly that the recovered ?-amylase is a potential candidate for future applications in the bread-making industry and in other food biotechnology applications.

SUBMITTER: Ait Kaki El-Hadef El-Okki A

PROVIDER: S-EPMC5296670 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature

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Improving Bread Quality with the Application of a Newly Purified Thermostable α-Amylase from Rhizopus oryzae FSIS4.

Ait Kaki El-Hadef El-Okki Amel A Gagaoua Mohammed M Bourekoua Hayat H Hafid Kahina K Bennamoun Leila L Djekrif-Dakhmouche Shahrazed S El-Hadef El-Okki Mohamed M Meraihi Zahia Z

Foods (Basel, Switzerland) 20170101 1

A new thermostable α-amylase from <i>Rhizopus oryzae</i> FSIS4 was purified for first time and recovered in a single step using a three-phase partitioning (TPP) system. The fungal α-amylase, at a concentration of 1.936 U per kg of flour, was used in bread-making and compared to the commercial enzyme. The results showed a significant effect of the recovered α-amylase in the prepared bread and allowed us to improve the quality of the bread. The study indicated clearly that the recovered α-amylase ...[more]

PMID: 28231081

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Project description:BackgroundChinese Nong-flavor (NF) liquor is continuously and stably produced by solid-state fermentation technology for 1000 years, resulting in enrichment of special microbial community and enzymes system in its starter. Based on traditional culture-dependent methods, these functional enzymes are hardly obtained. According to our previous metatranscriptomic analysis, which identifies plenty of thermostable carbohydrate-active enzymes in NF liquor starter, the aim of this study is to provide a direct and efficient way to mine these thermostable enzymes.ResultsIn present study, an alpha-amylase (NFAmy13A) gene, which showed the highest expression level of enzymes in starch degradation at high temperature stage (62 °C), was directly obtained by functional metatranscriptomics from Chinese Nong-flavor liquor starter and expressed in Pichia pastoris. NFAmy13A had a typical signal peptide and shared the highest sequence identity of 64% with α-amylase from Aspergillus niger. The recombinant enzyme of NFAmy13A showed an optimal pH at 5.0-5.5 and optimal temperature at 60 °C. NFAmy13A was activated and stabilized by Ca2+, and its half-lives at 60 and 70 °C were improved significantly from 1.5 and 0.4 h to 16 and 0.7 h, respectively, in the presence of 10 mM CaCl2. Meanwhile, Hg2+, Co2+ and SDS largely inhibited its activity. NFAmy13A showed the maximum activity on amylopectin, followed by various starches, amylose, glycogen, and pullulan, and its specificity activity on amylopectin was 200.4 U/mg. Moreover, this α-amylase efficiently hydrolyzed starches (from corn, wheat, and potato) at high concentrations up to 15 mg/ml.ConclusionsThis study provides a direct way to mine active enzymes from man-made environment of NF liquor starter, by which a fungal thermostable α-amylase (NFAmy13A) is successfully obtained. The good characteristics of NFAmy13A in degrading starch at high temperature are consistent with its pivotal role in solid-state fermentation of NF liquor brewing. This work would stimulate mining more enzymes from NF liquor starter and studying their potentially synergistic roles in NF liquor brewing, thus paving the way toward the optimization of liquor production and improvement of liquor quality in future.

Dataset Information

Improving Bread Quality with the Application of a Newly Purified Thermostable ?-Amylase from Rhizopus oryzae FSIS4.

Publications

Improving Bread Quality with the Application of a Newly Purified Thermostable α-Amylase from Rhizopus oryzae FSIS4.

Similar Datasets

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