Shohreh Ariaeenejad - Academia.edu (original) (raw)

Papers by Shohreh Ariaeenejad

Research paper thumbnail of Identification and characterization of a novel thermostable xylanase from camel rumen metagenome

International Journal of Biological Macromolecules, Apr 1, 2019

Metagenomics has emerged to isolate novel enzymes from the uncultured microbiota in the environme... more Metagenomics has emerged to isolate novel enzymes from the uncultured microbiota in the environment. In this study, the metagenomic data obtained from camel rumen was considered as the potential source of microbial xylanase enzymes with proper activity in extreme conditions. The metagenomic data were assembled and contigs were used for in-silico identification of candidate thermostable enzyme. A novel thermostable xylanase enzyme, named PersiXyn1, with 1146 bp full-length gene which encodes a 381 amino acid protein was identified. Using the DNA template extracted from camel rumen metagenomic samples, the candidate enzyme genes were cloned and expressed in proper E. coli strains. The phylogenetic analysis showed the evolutionary position of PersiXyn1 among the known thermostable xylanases. The results of the CD analysis and determining the secondary structure of the enzyme, confirmed the presence of a high percentage of β-sheets as an important characteristic of thermophilic xylanases. The PersiXyn1 was active at a broad range of pH (6-11) and temperature (25-90 °C). The optimum pH and temperature were 8 and 40 °C respectively, and the enzyme maintained 80% of its maximum activity in the pH 8 and temperature 40 °C for 1 h. The Scanning electron microscope (SEM) micrograph of enzyme treated pulp clearly showed that the effective use of enzymes in fiber separation may reduce the cost of carton paper production. The novelty of this enzyme lies in the fact that it is highly active and stable in a broad range of pH and temperature. This study highlights the potential importance of camel microbiome for discovering novel thermostable enzymes with applications in agriculture and industries.

Research paper thumbnail of Improved saccharification of rice straw by removing phenolic compounds using a stable immobilized metagenome-derived laccase on sodium alginate-based hydrogel

Biochemical Engineering Journal

Research paper thumbnail of Effects of agro-waste resources on characteristics of Fe/nanocellulose hybrids and their applications as novel Fenton-like catalysts in dye removal from wastewater

Process Safety and Environmental Protection

Research paper thumbnail of Lignocellulose degradation by rumen bacterial communities: New insights from metagenome analyses

Research paper thumbnail of The impact of immobilizing two metagenome-derived α-amylases by cellulose nanocrystals, on enhancing the functional properties by experimental and computational approaches

Zenodo (CERN European Organization for Nuclear Research), Mar 17, 2023

Research paper thumbnail of Enhancing the ethanol production by exploiting a novel metagenomic-derived bifunctional xylanase/β-glucosidase enzyme with improved β-glucosidase activity by a nanocellulose carrier

Frontiers in Microbiology

Some enzymes can catalyze more than one chemical conversion for which they are physiologically sp... more Some enzymes can catalyze more than one chemical conversion for which they are physiologically specialized. This secondary function, which is called underground, promiscuous, metabolism, or cross activity, is recognized as a valuable feature and has received much attention for developing new catalytic functions in industrial applications. In this study, a novel bifunctional xylanase/β-glucosidase metagenomic-derived enzyme, PersiBGLXyn1, with underground β-glucosidase activity was mined by in-silico screening. Then, the corresponding gene was cloned, expressed and purified. The PersiBGLXyn1 improved the degradation efficiency of organic solvent pretreated coffee residue waste (CRW), and subsequently the production of bioethanol during a separate enzymatic hydrolysis and fermentation (SHF) process. After characterization, the enzyme was immobilized on a nanocellulose (NC) carrier generated from sugar beet pulp (SBP), which remarkably improved the underground activity of the enzyme up...

Research paper thumbnail of Efficiency of an alkaline, thermostable, detergent compatible, and organic solvent tolerant lipase with hydrolytic potential in biotreatment of wastewater

Science of The Total Environment

Research paper thumbnail of Enzymatically triggered delignification through a novel stable laccase: A mixed in-silico /in-vitro exploration of a complex environmental microbiota

International Journal of Biological Macromolecules

Research paper thumbnail of Author Correction: In vitro bioprocessing of corn as poultry feed additive by the influence of carbohydrate hydrolyzing metagenome derived enzyme cocktail

Research paper thumbnail of A computational learning paradigm to targeted discovery of biocatalysts from metagenomic data: A case study of lipase identification

Biotechnology and Bioengineering, 2022

The growing adoption of enzymes as biocatalysts in various industries has accentuated the demand ... more The growing adoption of enzymes as biocatalysts in various industries has accentuated the demand for acquiring access to the great natural diversity and, in the meantime, the advent and advancements of metagenomics and high‐throughput sequencing technologies have offered an unprecedented opportunity to explore this extensive resource. Lipases, enzymes responsible for the biological turnover of lipids, are among the most commercialized biocatalysts with numerous applications in different domains and therefore are of high industrial value. The relatively costly and time‐consuming wet‐lab experimental pipelines commonly used for novel enzyme discovery, highlight the necessity of agile in silico approaches to keep pace with the exponential growth of available sequencing data. In the present study, an in‐depth analysis of a tannery wastewater metagenome, including taxonomic and enzymatic profiling, was performed. Using sequence homology‐based screening methods and supervised machine learning‐based regression models aimed at prediction of lipases' pH and temperature optima, the metagenomic data set was screened for lipolytic enzymes, which led to the isolation of alkaline and highly thermophilic novel lipase. Moreover, MeTarEnz (metagenomic targeted enzyme miner) software was developed and made freely accessible (at https://cbb.ut.ac.ir/MeTarEnz) as a part of this study. MeTarEnz offers several functions to automate the process of targeted enzyme mining from high‐throughput sequencing data. This study highlights the competence of computational approaches in exploring vast biodiversity within environmental niches, while providing a set of practical in silico tools as well as a generalized methodology to facilitate the sequence‐based mining of biocatalysts.

Research paper thumbnail of Additional file 1 of A novel high performance in-silico screened metagenome-derived alkali-thermostable endo-β-1,4-glucanase for lignocellulosic biomass hydrolysis in the harsh conditions

Research paper thumbnail of Highly efficient removal of dyes from wastewater using nanocellulose from quinoa husk as a carrier for immobilization of laccase

Bioresource Technology, 2022

In this study, the synthesis of nanocellulose (NC) from an agro-waste of quinoa husks (QS) was re... more In this study, the synthesis of nanocellulose (NC) from an agro-waste of quinoa husks (QS) was reported for the first time. The NC nano-carrier was utilized for immobilization of a model laccase enzyme (PersiLac1) providing an innovative, green, and practical nano-biocatalyst for efficient two different model dyes removal (malachite green (MG) and congo red (CR)) from water.This nano-biocatalyst developed a synergistic adsorption-degradation approach leading the dye molecules easily gathered near the nano-carrier by adsorption and then degraded effectively by the enzyme. Upon enzyme immobilization, the dye removals (%) were remarkably improved for both 150 mg/L of dyes (from 54% and 12%, for MG and CR respectively, in case of the pristine NCs, to 98% and 60% for the immobilized enzyme). The immobilized PersiLac1 could decolorize the concentrated dye solutions and showed superior reusability (up to 83% dye removal after 18th runs for MG) and remarkable performance from complex real textile effluents.

Research paper thumbnail of Synthesis of two novel bio-based hydrogels using sodium alginate and chitosan and their proficiency in physical immobilization of enzymes

Scientific Reports, 2022

Herein, four novel and bio-based hydrogel samples using sodium alginate (SA) and chitosan (CH) gr... more Herein, four novel and bio-based hydrogel samples using sodium alginate (SA) and chitosan (CH) grafted with acrylamide (AAm) and glycidyl methacrylate (GMA) and their reinforced nanocomposites with graphene oxide (GO) were synthesized and coded as SA-g-(AAm-co-GMA), CH-g-(AAm-co-GMA), GO/SA-g-(AAm-co-GMA), and GO/CH-g-(AAm-co-GMA), respectively. The morphology, net charge, and water absorption capacity of samples were entirely changed by switching the biopolymer from SA to CH and adding a nano-filler. The proficiencies of hydrogels were compared in the immobilization of a model metagenomic-derived xylanase (PersiXyn9). The best performance was observed for GO/SA-g-poly(AAm-co-GMA) sample indicating better stabilizing electrostatic attractions between PersiXyn9 and reinforced SA-based hydrogel. Compared to the free enzyme, the immobilized PersiXyn9 on reinforced SA-based hydrogel showed a 110.1% increase in the released reducing sugar and almost double relative activity after 180 min...

Research paper thumbnail of The novel homologue of the human α‐glucosidase inhibited by the non‐germinated and germinated quinoa protein hydrolysates after in vitro gastrointestinal digestion

Journal of Food Biochemistry, 2021

Quinoa (Chenopodium quinoa Willd) is a potential source of protein with ideal amino acid profiles... more 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 (IC50 ) of 0.07 mg/ml. Based on the kinetic analysis, both the germinated and non-germinated samples before and after digestion were competitive-type inhibitors of α-glucosidase. Results of this study showed the improved α-glucosidase inhibitory activity of the quinoa bioactive peptides after germination and gastrointestinal digestion and highlighted the potential of metagenome-derived PersiAlpha-GL1 as a novel homologue of the human α-glucosidase for developing the future anti-diabetic drugs. PRACTICAL APPLICATIONS: This study aimed to evaluate the effect of germination and gastrointestinal digestion of the quinoa protein and bioactive peptides on α-glucosidase inhibitory activity against the novel PersiAlpha-GL1. Metagenomic data were used to identify the novel α-glucosidase structurally and functionally homologue of human intestinal. The results showed the highest inhibition on PersiAlpha-GL1 by a germinated quinoa after gastroduodenal digestion and confirmed the potential of PersiAlpha-GL1 to enhance the effectiveness of the anti-diabetic drugs for industrial application.

Research paper thumbnail of Lack of Antioxidant Effect of Selenium on Interaction of Methyl Tert-butyl Ether (MTBE) with Cytochrome c

Antioxidants are of great importance because they can protect the body from oxidation agents. Rea... more Antioxidants are of great importance because they can protect the body from oxidation agents. Reactive oxygen species (ROS) are constantly producing as a result of metabolic processes. However, environmental factors such as methyl tert-butyl ether (MTBE) can enhance oxidation stress. MTBE is a widely used fuel oxygenation liquid that has been shown to cause potential cancer. The use of antioxidants may help to reduce the oxidation condition caused by MTBE. Selenium is an essential element with antioxidant property. In this study, the interaction between Cyt C and MTBE has been investigated in the absence and presence of Se. Molecular level examinations are extremely important to investigate the structural change of proteins by MTBE. In this research, molecular behaviour of Cyt c as an important model of protein, in the presence and absence of MTBE and Se is detected by biophysical methods such as UV-vis, fluorescence and FTIR spectroscopy, chemiluminescence and molecular docking. Th...

Research paper thumbnail of Synergistic Effect of Metagenome‐Derived Starch‐Degrading Enzymes on Quality of Functional Bread with Antioxidant Activity

Starch - Stärke, 2021

Starch‐degrading enzymes have gained particular importance in recent decades due to their crucial... more 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 ...

Research paper thumbnail of Efficient removal of various textile dyes from wastewater by novel thermo-halotolerant laccase

Bioresource Technology, 2021

A novel thermostable/halotolerant metagenome-derived laccase (PersiLac2) from tannery wastewater ... more A novel thermostable/halotolerant metagenome-derived laccase (PersiLac2) from tannery wastewater was purified to remove textile dyes in this study. The enzyme was highly active over a wide temperature and pH range and maintained 73.35% of its initial activity after 30 days, at 50 °C. The effect of various metal and organic-solvent tolerance on PersiLac2 showed, retaining greater than 53% activity at 800 mM of metal ions, 52.12% activity at 6 M NaCl, and greater than 44.09% activity at 20% organic solvents. PersiLac2 manifested effective removal of eight different textile dyes from azo, anthraquinone, and triphenylmethane families. It decolorized 500 mg/L of Alizarin yellow, Carmine, Congo red and Bromothymol blue with 99.74-55.85% efficiency after 15 min, at 50 °C, without mediator. This enzyme could practically remove dyes from a real textile effluent and it displayed significant detoxification in rice seed germination tests. In conclusion, PersiLac2 could be useful in future for decolorization/detoxification of wastewater.

Research paper thumbnail of Immobilization of enzyme cocktails on dopamine functionalized magnetic cellulose nanocrystals to enhance sugar bioconversion: A biomass reusing loop

Carbohydrate Polymers, 2021

Research paper thumbnail of A Novel High Glucose-Tolerant β-Glucosidase: Targeted Computational Approach for Metagenomic Screening

Frontiers in Bioengineering and Biotechnology, 2020

Research paper thumbnail of Improving the quality of gluten-free bread by a novel acidic thermostable α-amylase from metagenomics data

Food Chemistry, 2021

Development of gluten-free products is important due to their role in gluten related disorders an... more Development of gluten-free products is important due to their role in gluten related disorders and health improvement. α-Amylase enzymes have shown to have a positive effect on wheat bread quality. This study aimed to screen in-silico a novel acidic-thermostable α-amylase (PersiAmy2) from the sheep rumen metagenome to increase the quality of gluten-free bread. The PersiAmy2 was cloned, expressed, purified and characterized. The enzyme was highly stable at a wide range of pH, temperature and storage conditions. The PersiAmy2 had excellent activity in the presence of ions, inhibitors, and surfactants. Utilization of the acidic thermostable PersiAmy2 in gluten-free bread resulted in a softer crumb, higher specific volume, porosity, moisture content and caused a darker crust color. The rheological measurement showed a solid-elastic behavior in batters. Also the addition of this enzyme reduced the firmness. From the results of this study it can be concluded that the PersiAmy2 can be used to improve the quality of gluten-free bread.

Research paper thumbnail of Identification and characterization of a novel thermostable xylanase from camel rumen metagenome

International Journal of Biological Macromolecules, Apr 1, 2019

Metagenomics has emerged to isolate novel enzymes from the uncultured microbiota in the environme... more Metagenomics has emerged to isolate novel enzymes from the uncultured microbiota in the environment. In this study, the metagenomic data obtained from camel rumen was considered as the potential source of microbial xylanase enzymes with proper activity in extreme conditions. The metagenomic data were assembled and contigs were used for in-silico identification of candidate thermostable enzyme. A novel thermostable xylanase enzyme, named PersiXyn1, with 1146 bp full-length gene which encodes a 381 amino acid protein was identified. Using the DNA template extracted from camel rumen metagenomic samples, the candidate enzyme genes were cloned and expressed in proper E. coli strains. The phylogenetic analysis showed the evolutionary position of PersiXyn1 among the known thermostable xylanases. The results of the CD analysis and determining the secondary structure of the enzyme, confirmed the presence of a high percentage of β-sheets as an important characteristic of thermophilic xylanases. The PersiXyn1 was active at a broad range of pH (6-11) and temperature (25-90 °C). The optimum pH and temperature were 8 and 40 °C respectively, and the enzyme maintained 80% of its maximum activity in the pH 8 and temperature 40 °C for 1 h. The Scanning electron microscope (SEM) micrograph of enzyme treated pulp clearly showed that the effective use of enzymes in fiber separation may reduce the cost of carton paper production. The novelty of this enzyme lies in the fact that it is highly active and stable in a broad range of pH and temperature. This study highlights the potential importance of camel microbiome for discovering novel thermostable enzymes with applications in agriculture and industries.

Research paper thumbnail of Improved saccharification of rice straw by removing phenolic compounds using a stable immobilized metagenome-derived laccase on sodium alginate-based hydrogel

Biochemical Engineering Journal

Research paper thumbnail of Effects of agro-waste resources on characteristics of Fe/nanocellulose hybrids and their applications as novel Fenton-like catalysts in dye removal from wastewater

Process Safety and Environmental Protection

Research paper thumbnail of Lignocellulose degradation by rumen bacterial communities: New insights from metagenome analyses

Research paper thumbnail of The impact of immobilizing two metagenome-derived α-amylases by cellulose nanocrystals, on enhancing the functional properties by experimental and computational approaches

Zenodo (CERN European Organization for Nuclear Research), Mar 17, 2023

Research paper thumbnail of Enhancing the ethanol production by exploiting a novel metagenomic-derived bifunctional xylanase/β-glucosidase enzyme with improved β-glucosidase activity by a nanocellulose carrier

Frontiers in Microbiology

Some enzymes can catalyze more than one chemical conversion for which they are physiologically sp... more Some enzymes can catalyze more than one chemical conversion for which they are physiologically specialized. This secondary function, which is called underground, promiscuous, metabolism, or cross activity, is recognized as a valuable feature and has received much attention for developing new catalytic functions in industrial applications. In this study, a novel bifunctional xylanase/β-glucosidase metagenomic-derived enzyme, PersiBGLXyn1, with underground β-glucosidase activity was mined by in-silico screening. Then, the corresponding gene was cloned, expressed and purified. The PersiBGLXyn1 improved the degradation efficiency of organic solvent pretreated coffee residue waste (CRW), and subsequently the production of bioethanol during a separate enzymatic hydrolysis and fermentation (SHF) process. After characterization, the enzyme was immobilized on a nanocellulose (NC) carrier generated from sugar beet pulp (SBP), which remarkably improved the underground activity of the enzyme up...

Research paper thumbnail of Efficiency of an alkaline, thermostable, detergent compatible, and organic solvent tolerant lipase with hydrolytic potential in biotreatment of wastewater

Science of The Total Environment

Research paper thumbnail of Enzymatically triggered delignification through a novel stable laccase: A mixed in-silico /in-vitro exploration of a complex environmental microbiota

International Journal of Biological Macromolecules

Research paper thumbnail of Author Correction: In vitro bioprocessing of corn as poultry feed additive by the influence of carbohydrate hydrolyzing metagenome derived enzyme cocktail

Research paper thumbnail of A computational learning paradigm to targeted discovery of biocatalysts from metagenomic data: A case study of lipase identification

Biotechnology and Bioengineering, 2022

The growing adoption of enzymes as biocatalysts in various industries has accentuated the demand ... more The growing adoption of enzymes as biocatalysts in various industries has accentuated the demand for acquiring access to the great natural diversity and, in the meantime, the advent and advancements of metagenomics and high‐throughput sequencing technologies have offered an unprecedented opportunity to explore this extensive resource. Lipases, enzymes responsible for the biological turnover of lipids, are among the most commercialized biocatalysts with numerous applications in different domains and therefore are of high industrial value. The relatively costly and time‐consuming wet‐lab experimental pipelines commonly used for novel enzyme discovery, highlight the necessity of agile in silico approaches to keep pace with the exponential growth of available sequencing data. In the present study, an in‐depth analysis of a tannery wastewater metagenome, including taxonomic and enzymatic profiling, was performed. Using sequence homology‐based screening methods and supervised machine learning‐based regression models aimed at prediction of lipases' pH and temperature optima, the metagenomic data set was screened for lipolytic enzymes, which led to the isolation of alkaline and highly thermophilic novel lipase. Moreover, MeTarEnz (metagenomic targeted enzyme miner) software was developed and made freely accessible (at https://cbb.ut.ac.ir/MeTarEnz) as a part of this study. MeTarEnz offers several functions to automate the process of targeted enzyme mining from high‐throughput sequencing data. This study highlights the competence of computational approaches in exploring vast biodiversity within environmental niches, while providing a set of practical in silico tools as well as a generalized methodology to facilitate the sequence‐based mining of biocatalysts.

Research paper thumbnail of Additional file 1 of A novel high performance in-silico screened metagenome-derived alkali-thermostable endo-β-1,4-glucanase for lignocellulosic biomass hydrolysis in the harsh conditions

Research paper thumbnail of Highly efficient removal of dyes from wastewater using nanocellulose from quinoa husk as a carrier for immobilization of laccase

Bioresource Technology, 2022

In this study, the synthesis of nanocellulose (NC) from an agro-waste of quinoa husks (QS) was re... more In this study, the synthesis of nanocellulose (NC) from an agro-waste of quinoa husks (QS) was reported for the first time. The NC nano-carrier was utilized for immobilization of a model laccase enzyme (PersiLac1) providing an innovative, green, and practical nano-biocatalyst for efficient two different model dyes removal (malachite green (MG) and congo red (CR)) from water.This nano-biocatalyst developed a synergistic adsorption-degradation approach leading the dye molecules easily gathered near the nano-carrier by adsorption and then degraded effectively by the enzyme. Upon enzyme immobilization, the dye removals (%) were remarkably improved for both 150 mg/L of dyes (from 54% and 12%, for MG and CR respectively, in case of the pristine NCs, to 98% and 60% for the immobilized enzyme). The immobilized PersiLac1 could decolorize the concentrated dye solutions and showed superior reusability (up to 83% dye removal after 18th runs for MG) and remarkable performance from complex real textile effluents.

Research paper thumbnail of Synthesis of two novel bio-based hydrogels using sodium alginate and chitosan and their proficiency in physical immobilization of enzymes

Scientific Reports, 2022

Herein, four novel and bio-based hydrogel samples using sodium alginate (SA) and chitosan (CH) gr... more Herein, four novel and bio-based hydrogel samples using sodium alginate (SA) and chitosan (CH) grafted with acrylamide (AAm) and glycidyl methacrylate (GMA) and their reinforced nanocomposites with graphene oxide (GO) were synthesized and coded as SA-g-(AAm-co-GMA), CH-g-(AAm-co-GMA), GO/SA-g-(AAm-co-GMA), and GO/CH-g-(AAm-co-GMA), respectively. The morphology, net charge, and water absorption capacity of samples were entirely changed by switching the biopolymer from SA to CH and adding a nano-filler. The proficiencies of hydrogels were compared in the immobilization of a model metagenomic-derived xylanase (PersiXyn9). The best performance was observed for GO/SA-g-poly(AAm-co-GMA) sample indicating better stabilizing electrostatic attractions between PersiXyn9 and reinforced SA-based hydrogel. Compared to the free enzyme, the immobilized PersiXyn9 on reinforced SA-based hydrogel showed a 110.1% increase in the released reducing sugar and almost double relative activity after 180 min...

Research paper thumbnail of The novel homologue of the human α‐glucosidase inhibited by the non‐germinated and germinated quinoa protein hydrolysates after in vitro gastrointestinal digestion

Journal of Food Biochemistry, 2021

Quinoa (Chenopodium quinoa Willd) is a potential source of protein with ideal amino acid profiles... more 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 (IC50 ) of 0.07 mg/ml. Based on the kinetic analysis, both the germinated and non-germinated samples before and after digestion were competitive-type inhibitors of α-glucosidase. Results of this study showed the improved α-glucosidase inhibitory activity of the quinoa bioactive peptides after germination and gastrointestinal digestion and highlighted the potential of metagenome-derived PersiAlpha-GL1 as a novel homologue of the human α-glucosidase for developing the future anti-diabetic drugs. PRACTICAL APPLICATIONS: This study aimed to evaluate the effect of germination and gastrointestinal digestion of the quinoa protein and bioactive peptides on α-glucosidase inhibitory activity against the novel PersiAlpha-GL1. Metagenomic data were used to identify the novel α-glucosidase structurally and functionally homologue of human intestinal. The results showed the highest inhibition on PersiAlpha-GL1 by a germinated quinoa after gastroduodenal digestion and confirmed the potential of PersiAlpha-GL1 to enhance the effectiveness of the anti-diabetic drugs for industrial application.

Research paper thumbnail of Lack of Antioxidant Effect of Selenium on Interaction of Methyl Tert-butyl Ether (MTBE) with Cytochrome c

Antioxidants are of great importance because they can protect the body from oxidation agents. Rea... more Antioxidants are of great importance because they can protect the body from oxidation agents. Reactive oxygen species (ROS) are constantly producing as a result of metabolic processes. However, environmental factors such as methyl tert-butyl ether (MTBE) can enhance oxidation stress. MTBE is a widely used fuel oxygenation liquid that has been shown to cause potential cancer. The use of antioxidants may help to reduce the oxidation condition caused by MTBE. Selenium is an essential element with antioxidant property. In this study, the interaction between Cyt C and MTBE has been investigated in the absence and presence of Se. Molecular level examinations are extremely important to investigate the structural change of proteins by MTBE. In this research, molecular behaviour of Cyt c as an important model of protein, in the presence and absence of MTBE and Se is detected by biophysical methods such as UV-vis, fluorescence and FTIR spectroscopy, chemiluminescence and molecular docking. Th...

Research paper thumbnail of Synergistic Effect of Metagenome‐Derived Starch‐Degrading Enzymes on Quality of Functional Bread with Antioxidant Activity

Starch - Stärke, 2021

Starch‐degrading enzymes have gained particular importance in recent decades due to their crucial... more 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 ...

Research paper thumbnail of Efficient removal of various textile dyes from wastewater by novel thermo-halotolerant laccase

Bioresource Technology, 2021

A novel thermostable/halotolerant metagenome-derived laccase (PersiLac2) from tannery wastewater ... more A novel thermostable/halotolerant metagenome-derived laccase (PersiLac2) from tannery wastewater was purified to remove textile dyes in this study. The enzyme was highly active over a wide temperature and pH range and maintained 73.35% of its initial activity after 30 days, at 50 °C. The effect of various metal and organic-solvent tolerance on PersiLac2 showed, retaining greater than 53% activity at 800 mM of metal ions, 52.12% activity at 6 M NaCl, and greater than 44.09% activity at 20% organic solvents. PersiLac2 manifested effective removal of eight different textile dyes from azo, anthraquinone, and triphenylmethane families. It decolorized 500 mg/L of Alizarin yellow, Carmine, Congo red and Bromothymol blue with 99.74-55.85% efficiency after 15 min, at 50 °C, without mediator. This enzyme could practically remove dyes from a real textile effluent and it displayed significant detoxification in rice seed germination tests. In conclusion, PersiLac2 could be useful in future for decolorization/detoxification of wastewater.

Research paper thumbnail of Immobilization of enzyme cocktails on dopamine functionalized magnetic cellulose nanocrystals to enhance sugar bioconversion: A biomass reusing loop

Carbohydrate Polymers, 2021

Research paper thumbnail of A Novel High Glucose-Tolerant β-Glucosidase: Targeted Computational Approach for Metagenomic Screening

Frontiers in Bioengineering and Biotechnology, 2020

Research paper thumbnail of Improving the quality of gluten-free bread by a novel acidic thermostable α-amylase from metagenomics data

Food Chemistry, 2021

Development of gluten-free products is important due to their role in gluten related disorders an... more Development of gluten-free products is important due to their role in gluten related disorders and health improvement. α-Amylase enzymes have shown to have a positive effect on wheat bread quality. This study aimed to screen in-silico a novel acidic-thermostable α-amylase (PersiAmy2) from the sheep rumen metagenome to increase the quality of gluten-free bread. The PersiAmy2 was cloned, expressed, purified and characterized. The enzyme was highly stable at a wide range of pH, temperature and storage conditions. The PersiAmy2 had excellent activity in the presence of ions, inhibitors, and surfactants. Utilization of the acidic thermostable PersiAmy2 in gluten-free bread resulted in a softer crumb, higher specific volume, porosity, moisture content and caused a darker crust color. The rheological measurement showed a solid-elastic behavior in batters. Also the addition of this enzyme reduced the firmness. From the results of this study it can be concluded that the PersiAmy2 can be used to improve the quality of gluten-free bread.