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Fritz Loth

Researcher at Fraunhofer Society

Publications -  41
Citations -  797

Fritz Loth is an academic researcher from Fraunhofer Society. The author has contributed to research in topics: Cellulose & Starch. The author has an hindex of 15, co-authored 41 publications receiving 759 citations. Previous affiliations of Fritz Loth include Danube University Krems.

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Construction of a functional S-layer fusion protein comprising an immunoglobulin G-binding domain for development of specific adsorbents for extracorporeal blood purification.

TL;DR: Compared to commercial particles used as immunoadsorbents to remove autoantibodies from sera of patients suffering from an autoimmune disease, the IgG binding capacity of the S-layer fusion protein-coated microbeads was at least 20 times higher and should find application in the microsphere-based detoxification system.
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Structural Changes in Hemp Fibers as a Result of Enzymatic Hydrolysis with Mixed Enzyme Systems

TL;DR: While crystal linity changes upon hydrolysis are insignificant, the pore structure is strongly influenced by the choice of enzyme system, and Hemicellulase seems to promote the formation of smaller pores, while cellobiase forms larger pores.
Patent

Arrangement for removing substances from liquids, in particular blood

TL;DR: In this paper, an arrangement for removing substances has a membrane filter and is used in blood purification processes and in chemical and biotechnological separation processes and thus causes locally different positive and negative transmembrane pressure differentials.
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Extracorporeal endotoxin removal by immobilized polyethylenimine.

TL;DR: A new ET-adsorbent based on macroporous cellulosic beads with immobilized polyethylenimine (PEI) was tested for its ET-removal capacity in vitro and indicates that the PEI absorber is of high efficacy and possibly of interest for the treatment of endotoxemia.
Journal ArticleDOI

Development of specific adsorbents for human tumor necrosis factor-α : Influence of antibody immobilization on performance and biocompatibility

TL;DR: It is found that the conditions used during immobilization of the antibody profoundly influenced the biocompatibility of the resulting adsorbents, especially with respect to activation of the complement system.