H
Hadi Nedaei
Researcher at University of Tehran
Publications - 7
Citations - 79
Hadi Nedaei is an academic researcher from University of Tehran. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 3, co-authored 4 publications receiving 25 citations.
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Journal ArticleDOI
A novel metagenome-derived thermostable and poultry feed compatible α-amylase with enhanced biodegradation properties.
Seyedeh Fatemeh Sadeghian Motahar,Ali Khatibi,Maryam Salami,Shohreh Ariaeenejad,Zahra Emam-Djomeh,Hadi Nedaei,Kaveh Kavousi,Atefeh Sheykhabdolahzadeh Mamaghani,Ghasem Hosseini Salekdeh +8 more
TL;DR: The power of computational selected candidates to discover novel acidic thermostable α-amylases is indicated and effective biodegradation of the poultry feed for industry was achieved using the selected candidate PersiAmy3.
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Designing a new alginate-fibrinogen biomaterial composite hydrogel for wound healing
Marjan Soleimanpour,Samaneh Sadat Mirhaji,Samira Jafari,Hossein Derakhshankhah,Fatemeh Mamashli,Hadi Nedaei,Mohammad M. Karimi,Hamid R. Motasadizadeh,Yousef Fatahi,Atiyeh Ghasemi,Maryam sadat Nezamtaheri,Mohadese Khajezade,Masoumeh Teimouri,Bahram Goliaei,Cédric Delattre,Ali Akbar Saboury +15 more
TL;DR: In this paper , a wound dressing was designed using a combination of appropriate coagulating and anti-bacterial materials like fibrinogen (coagulating agent), nisin (as antibacterial agent), ethylenediaminetetraacetic acid (as antibacterial agent) and alginate (as wound healing agent).
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In-silico discovery of bifunctional enzymes with enhanced lignocellulose hydrolysis from microbiota big data
Shohreh Ariaeenejad,Kaveh Kavousi,Atefeh Sheykh Abdollahzadeh Mamaghani,Seyedeh Fatemeh Sadeghian Motahar,Hadi Nedaei,Ghasem Hosseini Salekdeh +5 more
TL;DR: In this paper, a stable bifunctional cellulase/xylanase, PersiCelXyn1, was identified from the rumen microbiota by the multi-stage in-silico screening pipeline and computationally assisted methodology.
Journal ArticleDOI
Polyphenolic self-association accounts for redirecting a high-yielding amyloid aggregation
Hadi Nedaei,Ali Akbar Saboury,Ali A. Meratan,Leila Karami,Lindsay Sawyer,Babak Kaboudin,Najmeh Jooyan,Atiyeh Ghasemi +7 more
TL;DR: It is suggested that polyphenolic self-association is the main cause of protein amyloid aggregation in vitro, and rosmarinic acid with a much lower tendency toSelf-associate was examined and was unable to redirect the process even at concentrations two and three times those of the other two.
Journal ArticleDOI
Nile red compensates for thioflavin T assay biased in the presence of curcumin
TL;DR: Nile red (NR) anisotropy is recommended as an alternative fluorescence-based method which considers molecular sizes, not emissions and can further minimize the interference effect of curcumin.