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Søren Flensted Lassen

Researcher at Novozymes

Publications -  27
Citations -  847

Søren Flensted Lassen is an academic researcher from Novozymes. The author has contributed to research in topics: Cellulase & Proteases. The author has an hindex of 12, co-authored 27 publications receiving 804 citations.

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Journal ArticleDOI

The consensus concept for thermostability engineering of proteins: further proof of concept

TL;DR: The present findings support the general validity of the consensus concept for thermostability engineering of proteins.
Journal ArticleDOI

Expression, gene cloning, and characterization of five novel phytases from four basidiomycete fungi: Peniophora lycii, Agrocybe pediades, a Ceriporia sp., and Trametes pubescens.

TL;DR: In this paper, the first five PhyA phytases from four orders within the phylum Basidiomycota were cloned from Aspergillus niger (16, 20, 28), Sordariales (19), Myceliophthora thermophila (14), Emericella nidulans, Talaromyces thermophilus (18), and Thermomyces lanuginosus (2).
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Engineering of phytase for improved activity at low pH.

TL;DR: Approaches to rationally engineer the pH activity profiles of Aspergillus fumigatus and consensus phytases are described and active-site amino acids that were considered to correlate with the activity maxima at low pH are identified.
Patent

Novel proteases and variants thereof

TL;DR: In this paper, isolated proteases of the RP-II type and variants of RP -II proteases exhibiting improved properties in comparison to the parent protease, DNA constructs and vectors coding for the expression of said proteases and variants, host cells capable of expressing the proteases from the DNA constructs, as well as a method of producing them by cultivating said host cells.
Journal ArticleDOI

Origin of initial burst in activity for Trichoderma reesei endo-glucanases hydrolyzing insoluble cellulose.

TL;DR: It is proposed that the frequency of structures on the substrate surface that cause transient in activation determine the extent of the burst phase of endo-glucanases, and it is suggested that the slowdown is linked to transient inactivation of enzyme on the cellulose surface.