ORCID Profile
0000-0002-6102-1177
Current Organisation
University of Reading
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Publisher: Hindawi Limited
Date: 16-12-2021
DOI: 10.1111/JFBC.14030
Abstract: Quinoa (Chenopodium quinoa Willd) is a potential source of protein with ideal amino acid profiles which its bioactive compounds can be improved during germination and gastrointestinal digestion. The present investigation studies the impact of germination for 24 hr and simulated gastrointestinal digestion on α-glucosidase inhibitory activity of the quinoa protein and bioactive peptides against the novel homologue of human α-glucosidase, PersiAlpha-GL1. The sprouted quinoa after gastroduodenal digestion was the most effective α-glucosidase inhibitor showing 81.10% α-glucosidase inhibition at concentration 4 mg/ml with the half inhibition rate (IC
Publisher: Springer Science and Business Media LLC
Date: 21-02-2021
Publisher: Elsevier BV
Date: 12-2020
Publisher: Wiley
Date: 29-07-2021
Abstract: Starch‐degrading enzymes have gained particular importance in recent decades due to their crucial role in numerous industrial applications especially, in the bakery industry. In this study, a novel thermostable pullulanase (PersiPul1) is screened from the metagenomic data for improving the quality of functional bread. The novel PersiPul1 is active over a wide range of temperature (30–80 °C) and pH (4–9) and exhibits high thermal stability, retaining 58.70% of activity at 80 °C. A cocktail of thermostable pullulanase and α‐amylase (PersiPul1and PersiAmy2) is developed to be used in bread fortified with quinoa protein ( Chenopodium quinoa Willd). The bread fortified with 7% quinoa protein isolate possess the highest reducing power and ABTS (73.64%) and DPPH (72.27%) radical scavenging activities. The addition of the enzyme mixture decreases the hardness and chewiness of the bread. The porosity, specific volume, and browning index of bread with pullulanase and α‐amylase are higher than control. Also, sensory analysis of the functional bread reveals higher scores in the presence of enzymes. Based on the results, the novel starch‐degrading enzyme cocktail is a promising alternative for improving the physical and sensory characteristics of the antioxidant bread enriched with quinoa protein isolate to be used in the bakery industry as a potential bio‐additive.
Publisher: Frontiers Media SA
Date: 30-08-2021
DOI: 10.3389/FMICB.2021.713125
Abstract: α-Amylases are among the very critical enzymes used for different industrial purposes. Most α-amylases cannot accomplish the requirement of industrial conditions and easily lose their activity in harsh environments. In this study, a novel α-amylase named PersiAmy1 has been identified through the multistage in silico screening pipeline from the rumen metagenomic data. The long-term storage of PersiAmy1 in low and high temperatures demonstrated 82.13 and 71.01% activities after 36 days of incubation at 4 and 50°C, respectively. The stable α-amylase retained 61.09% of its activity after 180 min of incubation at 90°C and was highly stable in a broad pH range, showing 60.48 and 86.05% activities at pH 4.0 and pH 9.0 after 180 min of incubation, respectively. Also, the enzyme could resist the high-salinity condition and demonstrated 88.81% activity in the presence of 5 M NaCl. PersiAmy1 showed more than 74% activity in the presence of various metal ions. The addition of the detergents, surfactants, and organic solvents did not affect the α-amylase activity considerably. Substrate spectrum analysis showed that PersiAmy1 could act on a wide array of substrates. PersiAmy1 showed high stability in inhibitors and superb activity in downstream conditions, thus useful in detergent and baking industries. Investigating the applicability in detergent formulation, PersiAmy1 showed more than 69% activity after incubation with commercial detergents at different temperatures (30–50°C) and retained more than 56% activity after incubation with commercial detergents for 3 h at 10°C. Furthermore, the results of the wash performance analysis exhibited a good stain removal at 10°C. The power of PersiAmy1 in the bread industry revealed soft, chewable crumbs with improved volume and porosity compared with control. This study highlights the intense power of robust novel PersiAmy1 as a functional bio-additive in many industrial applications.
Publisher: Elsevier BV
Date: 10-2021
Publisher: Elsevier BV
Date: 04-2021
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Fatemeh Sadeghian-Motahar.