M
Mohammad Dadashipour
Researcher at Toyama Prefectural University
Publications - 13
Citations - 356
Mohammad Dadashipour is an academic researcher from Toyama Prefectural University. The author has contributed to research in topics: Hydroxynitrile lyase & Protein engineering. The author has an hindex of 9, co-authored 13 publications receiving 322 citations. Previous affiliations of Mohammad Dadashipour include Pasteur Institute of Iran & Kyushu University.
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Journal ArticleDOI
Hydroxynitrile Lyases: Insights into Biochemistry, Discovery, and Engineering
TL;DR: Characteristics of many S- and R-selective HNLs with comparative tables for several enzymatic properties under biochem... will be presented.
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Effect of Salinity on the Tolerance to Toxic Metals and Oxyanions in Native Moderately Halophilic Spore-forming Bacilli
TL;DR: In this paper, 10 moderately halophilic spore-forming bacilli were isolated from saline soils in Iran and their intrinsic high-level resistance to chromate, arsenate, tellurite, selenite and biselenite was identified by an agar dilution method.
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Discovery and molecular and biocatalytic properties of hydroxynitrile lyase from an invasive millipede, Chamberlinius hualienensis
TL;DR: The isolation of HNL from the cyanide-emitting invasive millipede Chamberlinius hualienensis is reported, along with its molecular properties and application in biocatalysis.
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S-selective hydroxynitrile lyase from a plant Baliospermum montanum: molecular characterization of recombinant enzyme.
Mohammad Dadashipour,Mizue Yamazaki,Kazumi Momonoi,Ken’ichirou Tamura,Ken-ichi Fuhshuku,Yurina Kanase,Etsuzoh Uchimura,Guan Kaiyun,Yasuhisa Asano +8 more
TL;DR: A novel S-hydroxynitrile lyase (HNL) was purified from leaves of a plant by ammonium sulfate fractionation and column chromatographies and showed variations in residues involved in substrate pocket and substrate entrance channel compared to other S-selective HNLs, based on a model was built.
Journal ArticleDOI
Functional expression of a plant hydroxynitrile lyase in Escherichia coli by directed evolution: creation and characterization of highly in vivo soluble mutants
TL;DR: The findings challenge the rationale of producing recombinant proteins in this host at 37°C and generate highly in vivo soluble mutants of a hydroxynitrile lyase in E.coli using protein engineering.