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Dorte Møller Larsen

Researcher at Technical University of Denmark

Publications -  11
Citations -  277

Dorte Møller Larsen is an academic researcher from Technical University of Denmark. The author has contributed to research in topics: Lyase & Thermostability. The author has an hindex of 9, co-authored 10 publications receiving 241 citations.

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Identification, expression, and characterization of a novel bacterial RGI Lyase enzyme for the production of bio-functional fibers

TL;DR: The work thus demonstrated the workability of in silico based screening coupled with a synthetic biology approach for gene synthesis for identification and production of a thermostable enzyme.
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Enzyme catalysed production of sialylated human milk oligosaccharides and galactooligosaccharides by Trypanosoma cruzi trans-sialidase.

TL;DR: Proof of the concept of producing 3'-sialyllactose and potentially other sIALylated HMOs as well as sialylated GOS enzymatically by trans-sialidase activity is provided, while at the same time providing valorisation of CGMP, a co-processing product from cheese manufacture.
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Biocatalytic production of 3′-sialyllactose by use of a modified sialidase with superior trans-sialidase activity

TL;DR: Casein glycomacropeptide and lactose were used as substrates for enzyme catalyzed production of 3′-sialyllactose, a model case compound for human milk oligosaccharides (HMOs) demonstrating the versatility of the Tr6 trans -sialidase for catalyzing sialyl-transfer for generating different HMOs.
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Definition and characterization of enzymes for maximal biocatalytic solubilization of prebiotic polysaccharides from potato pulp

TL;DR: The objective of the present study was to characterize and compare four homogalacturonan degrading enzymes capable of catalyzing the required solubilization of these pectinaceous polysaccharides from potato pulp in a 1 min reaction.
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Rational design of a new Trypanosoma rangeli trans-sialidase for efficient sialylation of glycans.

TL;DR: Rational engineering of Trypanosoma rangeli sialidase is reported to develop an effective enzyme for a potentially important type of reactivity: production of sialylated prebiotic glycans and it is suggested that this motif can serve as a framework for future optimization of trans-sialylation towards prebiotics.