TY  - JOUR
A1  - Rühl, Martin
A1  - Pietzner, Verena
A1  - Vilcinskas, Andreas
A1  - Zorn, Holger
T1  - Insects and molds as bio-resources: food biotechnology
JF  - Chemie in unserer Zeit
N2  - Microorganisms are used for the production of foodstuffs since thousands of years. By now, these biotechnological processes are not restricted to some of the known microorganisms. The possibility to produce enzymes independently from their host organisms extended their range of application. Since then, exploration of new bioresources leads to novel enzymes and peptides applicable for a diverse set of food production processes: peptidases of grain pest beetles are able to hydrolyse gluten and antimicrobial active peptides of insects maybe of use for preservation of food. Examples of our own work depict strategies to identify novel biocatalysts for food biotechnology.
N2  - Mikroorganismen werden seit Jahrtausenden zur Herstellung von Lebensmitteln genutzt. Mittlerweile sind diese biotechnologischen Verfahren nicht mehr auf die Verwendung einiger Organismen beschränkt. Die Möglichkeit, Enzyme unabhängig von ihrem Wirtsorganismus zu produzieren, erweiterte den Einsatzbereich dieser technischen Hilfsmittel ungemein. Seither werden vermehrt neue Bioressourcen erschlossen, um neuartige Enzyme und Peptide für die Lebensmittelproduktion verfügbar zu machen: Peptidasen aus Getreideschädlingen vermögen Gluten zu hydrolysieren und antimikrobiell wirksame Peptide aus Insekten könnten zur Haltbarmachung von Lebensmitteln eingesetzt werden. Aber wie findet man solche Katalysatoren? Beispiele aus eigenen Arbeiten zeigen es.
T2  - Insekten und Schimmelpilze als Bioressource
KW  - Gelbe Biotechnologie
KW  - Insekten
KW  - Ascomyceten
KW  - antimikrobielle Peptide
Y1  - 2019
U6  - https://doi.org/10.1002/ciuz.201900833
SN  - 0009-2851
SN  - 1521-3781
VL  - 53
IS  - 5
SP  - 342
EP  - 348
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - BOOK
A1  - Vilcinskas, Andreas
T1  - Einheimische Süßwasserfische : alle Arten ; Merkmale, Verbreitung, Lebensweise
Y1  - 1999
SN  - 3-8289-1510-8
PB  - Bechtermünz
CY  - Augsburg
ER  - 
TY  - BOOK
A1  - Vilcinskas, Andreas
T1  - Heimische Aquarienfische
T3  - Ihr Hobby
Y1  - 2000
SN  - 3-933646-50-2
VL  - 42
PB  - bede-Verl.
CY  - Ruhmannsfelden
ER  - 
TY  - BOOK
A1  - Vilcinskas, Andreas
T1  - Fische : mitteleuropäische Süßwasserarten und Meeresfische der Nord- und Ostsee
T3  - BVL-Bestimmungsbuch
Y1  - 2000
SN  - 3-405-15848-6
PB  - BLV-Verl.-Ges
CY  - München
ER  - 
TY  - BOOK
A1  - Vilcinskas, Andreas
T1  - Meerestiere der Tropen : ein Bestimmungsbuch für Taucher, Schnorchler und Aquarianer ; über 700 niedere Tiere, Fische, Reptilien und Säuger
T3  - Kosmos Naturführer
Y1  - 2000
SN  - 3-440-07943-0
PB  - Kosmos
CY  - Stuttgart
ER  - 
TY  - JOUR
A1  - Kress, H.
A1  - Jarrin, A.
A1  - Thuroff, E.
A1  - Saunders, R.
A1  - Weise, C.
A1  - Schmidt am Busch, Marcel
A1  - Knapp, E. W.
A1  - Wedde, M.
A1  - Vilcinskas, Andreas
T1  - A Kunitz type protease inhibitor related protein is synthesized in Drosophila prepupal salivary glands and released into the moulting fluid during pupation
N2  - From the Drosophila virilis late puff region 31C, we microcloned two neighbouring genes, Kil-1 and Kil-2, that encode putative Kunitz serine protease inhibitor like proteins. The Kil-1 gene is expressed exclusively in prepupal salivary glands. Using a size mutant of the KIL-1 protein and MALDI-TOF analysis, we demonstrate that during pupation this protein is released from the prepupal salivary glands into the pupation fluid covering the surface of the pupa. 3-D- structure predictions are consistent with the known crystal structure of the human Kunitz type protease inhibitor 2KNT. This is the first experimental proof for the extra-corporal presence of a distinct Drosophila prepupal salivary gland protein. Possible functions of KIL-1 in the context of the control of proteolytic activities in the pupation fluid are discussed. (C) 2004 Elsevier Ltd. All rights reserved
Y1  - 2004
SN  - 0965-1748
ER  - 
TY  - JOUR
A1  - Clermont, A.
A1  - Wedde, M.
A1  - Seitz, V.
A1  - Podsiadlowski, L.
A1  - Lenze, D.
A1  - Hummel, M.
A1  - Vilcinskas, Andreas
T1  - Cloning and expression of an inhibitor of microbial metalloproteinases from insects contributing to innate immunity
N2  - The first IMPI (inhibitor of metalloproteinases from insects) was identified in the greater wax moth, Galleria mellonella [Wedde, Weise, Kopacek, Franke and Vilcinskas (1998) Eur. J. Biochem. 255, 535-543]. Here we report cloning and expression of a cDNA coding for this IMPI. The IMPI mRNA was identified among the induced transcripts from a subtractive and suppressive PCR analysis after bacterial challenge of G. mellonella larvae. Induced expression of the IMPI during a Immoral immune response was confirmed by real-time PCR, which documented up to 500 times higher amounts of IMPI mRNA in immunized larvae in comparison with untreated ones. The IMPI sequence shares no similarity with those of tissue inhibitors of metalloproteinases or other natural inhibitors of metalloproteinases, and the recombinant IMPI specifically inhibits thermolysin-like metalloproteinases, but not matrix metalloproteinases. These results support the hypothesis that the IMPI represents a novel type of immune-related protein which is induced and processed during the G. mellonella humoral immune response to inactivate pathogen-associated thermolysin-like metalloproteinases
Y1  - 2004
SN  - 0264-6021
ER  -