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Werner A. Hampel

Researcher at Vienna University of Technology

Publications -  13
Citations -  152

Werner A. Hampel is an academic researcher from Vienna University of Technology. The author has contributed to research in topics: Brevibacterium & S-layer. The author has an hindex of 7, co-authored 13 publications receiving 146 citations.

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Pretreatment and Hydrolysis of Brewer's Spent Grains

TL;DR: In this article, different physical, thermal and enzymatic treatments were used to solubilize the polysaccharides in Brewer's spent grains (BSG), the voluminous residue after mashing.
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Development of a microbial bioassay for chlorinated and brominated hydrocarbons

TL;DR: In this paper, a microbial assay for the determination of halogenated organic hydrocarbons in water samples was developed using cells of a Rhodococcus strain, containing the enzyme alkyl-halidohydrolase (E.C. 3.1.1.) were immobilized in alginate gel by forming small beads which were added to the sample solution.
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A synthetic medium for continuous culture of the S‐layer carrying Bacillus stearothermophilus PV 72 and studies on the influence of growth conditions on cell wall properties

TL;DR: A synthetic medium for Bacillus stearothermophilus PV 72 was developed by applying the pulse and shift technique with the aim to produce cell wall fragments with properties required for ultrafiltration membrane production by varying the growth conditions in condtinuous culture.
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Characteristics of a microbial assay for the detection of halogenated hydrocarbons using cells of an Actinomycete-like organism as a biological component

TL;DR: Cells of an Actinomycete-like bacterium, strain GJ70, with the ability to degrade several haloalkanes were used as a biological component in a discontinuous microbial bioassay for the detection of 1,3-dichloropropene and 1,2-dibromoethane in water.
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Formation of lipolytic enzymes by Brevibacterium linens

TL;DR: The kinetics of lipase formation was closely related to the amount of biomass formed during growth, and the cell-associated lipase had maximum activity at pH 8.0 and 37 °C and was strongly inhibited by 3,4-dichloroisocoumarin, an inhibitor specific for serine esterases.