Relevant bibliographies by topics / Aspergillopepsin ii

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Aspergillopepsin ii'

Author: Grafiati
Published: 4 June 2021
Last updated: 4 February 2022

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Journal articles on the topic "Aspergillopepsin ii"

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Sriranganadane, Dev, Utz Reichard, Karine Salamin, et al. "Secreted glutamic protease rescues aspartic protease Pep deficiency in Aspergillus fumigatus during growth in acidic protein medium." Microbiology 157, no. 5 (2011): 1541–50. http://dx.doi.org/10.1099/mic.0.048603-0.

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In an acidic protein medium Aspergillus fumigatus secretes an aspartic endoprotease (Pep) as well as tripeptidyl-peptidases, a prolyl-peptidase and carboxypeptidases. In addition, LC-MS/MS revealed a novel glutamic protease, AfuGprA, homologous to Aspergillus niger aspergillopepsin II. The importance of AfuGprA in protein digestion was evaluated by deletion of its encoding gene in A. fumigatus wild-type D141 and in a pepΔ mutant. Either A. fumigatus Pep or AfuGprA was shown to be necessary for fungal growth in protein medium at low pH. Exoproteolytic activity is therefore not sufficient for complete protein hydrolysis and fungal growth in a medium containing proteins as the sole nitrogen source. Pep and AfuGprA constitute a pair of endoproteases active at low pH, in analogy to A. fumigatus alkaline protease (Alp) and metalloprotease I (Mep), where at least one of these enzymes is necessary for fungal growth in protein medium at neutral pH. Heterologous expression of AfuGprA in Pichia pastoris showed that the enzyme is synthesized as a preproprotein and that the propeptide is removed through an autoproteolytic reaction at low pH to generate the mature protease. In contrast to A. niger aspergillopepsin II, AfuGprA is a single-chain protein and is structurally more similar to G1 proteases characterized in other non-Aspergillus fungi.
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Maeda, Masahiro, Kayoko Takeuchi, Masaki Kojima, et al. "Kinetic studies of unfolding process of aspergillopepsin II by pH-jump methods." Biochemical and Biophysical Research Communications 301, no. 3 (2003): 745–50. http://dx.doi.org/10.1016/s0006-291x(03)00031-7.

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Kojima, Masaki, Masaru Tanokura, Masahiro Maeda, et al. "pH-Dependent Unfolding of Aspergillopepsin II Studied by Small-Angle X-ray Scattering†." Biochemistry 39, no. 6 (2000): 1364–72. http://dx.doi.org/10.1021/bi991584o.

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Marangon, Matteo, Steven C. Van Sluyter, Ella M. C. Robinson, et al. "Degradation of white wine haze proteins by Aspergillopepsin I and II during juice flash pasteurization." Food Chemistry 135, no. 3 (2012): 1157–65. http://dx.doi.org/10.1016/j.foodchem.2012.05.042.

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Huang, Xiang-Ping, Naofumi Kagami, Hideshi Inoue, et al. "Identification of a Glutamic Acid and an Aspartic Acid Residue Essential for Catalytic Activity of Aspergillopepsin II, a Non-pepsin Type Acid Proteinase." Journal of Biological Chemistry 275, no. 34 (2000): 26607–14. http://dx.doi.org/10.1074/jbc.m910243199.

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Dissertations / Theses on the topic "Aspergillopepsin ii"

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Chomarat, Nadine. "Attaque enzymatique d'un tissu conjonctif, la peauTexte imprimé." Toulouse, INSA, 1993. http://www.theses.fr/1993ISAT0022.

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La peau, tissu conjonctif tres hydrate, se compose d'un reseau collagenique impliquant des interactions avec des proteoglycannes et des glycoproteines de structure, selon un modele d'organisation supramoleculaire (scott). Dans le but de liberer le collagene de la peau, notre attention s'est focalisee sur l'approche enzymatique, soit par les proteases acides, soit par les osidases. Nous avons demontre la quasi-insolubilite du collagene dans les bases et l'uree et confirme son caractere nettement acido soluble. Dans les conditions experimentales, les exoglycosidases testees n'ont qu'un role negligeable. Par contre, nous avons montre l'importance de l'action d'enzymes proteolytiques (pepsine et proctase) dans l'extraction du collagene de peaux de bovides. La maniere avec laquelle ces deux enzymes attaquent la peau differe: la pepsine hydrolyse selectivement les telopeptides du collagene et libere des brins relativement intacts, alors que la proctase attaque aleatoirement le reseau collagenique et solubilise des agregats contenant des molecules de collagene plus ou moins degradees. Ces caracteristiques sont confirmees par les proprietes rheologiques des gelatines issues de solutions de collagene extrait par la pepsine et la proctase. Seule la pepsine permet d'obtenir une gelatine aux proprietes viscosifiantes superieures aux gelatines industrielles
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Book chapters on the topic "Aspergillopepsin ii"

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Schomburg, Dietmar, and Dörte Stephan. "Aspergillopepsin II." In Enzyme Handbook 16. Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58903-4_18.

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2

Takahashi, Kenji. "Aspergillopepsin II." In Handbook of Proteolytic Enzymes. Elsevier, 2004. http://dx.doi.org/10.1016/b978-0-12-079611-3.50072-0.

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