Výsledky vyhledávání - "Marta Erra-Pujada"

Autor: Michael J. O’Donohue, Florent Chang-Pi-Hin, Marta Erra-Pujada, Philippe Debeire, Francis Duchiron

Publikováno v: Biotechnology Letters. 23:1273-1277

A pullulanase type II was produced in Escherichia coli using the relevant gene from Thermococcus hydrothermalis. This protein was purified and its pullulanolytic and amylolytic activities were characterised. The optimum temperature and Ca2+ concentra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::01e7d4c1233164ab560af7196608dbfc
https://doi.org/10.1023/a:1010597619811

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Water buffalo (Bubalus bubalis): complete nucleotide mitochondrial genome sequence

Autor: Marta Erra-Pujada, Gianfranco Greppi, Maria Feligini, Pietro Parma, Giuseppe Enne

Publikováno v: DNA sequence : the journal of DNA sequencing and mapping. 15(5-6)

In this work, we report the whole sequence of the water buffalo (Bubalus bubalis) mitochondrial genome. The water buffalo mt molecule is 16.355 base pair length and shows a genome organization similar to those reported for other mitochondrial genome.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe4af4da80de8b33d21019fdbd875a67
https://pubmed.ncbi.nlm.nih.gov/15621663

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The type II pullulanase of Thermococcus hydrothermalis : Molecular characterization of the gene and expression of the catalytic domain

Autor: Michael J. O’Donohue, Francis Duchiron, Marta Erra-Pujada, Philippe Debeire

Publikováno v: Journal of Bacteriology
Journal of Bacteriology, American Society for Microbiology, 1999, 181 (10), pp.3284-3287
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The gene encoding a hyperthermostable type II pullulanase produced by Thermococcus hydrothermalis (Th-Apu) has been isolated. Analysis of a total of 5.2 kb of genomic DNA has revealed the presence of three open reading frames, one of which ( apuA ) e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fae4ca5ebbec65077721d61f12164fd9
https://hal.inrae.fr/hal-02697820

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Experimental evidence for the essential role of the C-terminal residue in the strict aminopeptidase activity of the thiol aminopeptidase PepC, a bacterial bleomycin hydrolase

Autor: Michel-Yves Mistou, Marta Erra-Pujada, Luis Mata, Jean-Claude Gripon

Publikováno v: Biochemical Journal
Biochemical Journal, Portland Press, 1997, 328, pp.343-347

PepCs isolated from lactic acid bacteria and bleomycin hydrolases of eukaryotic organisms are strict aminopeptidases which belong to the papain family of thiol peptidases. The structural basis of the enzymic specificity of the lactococcal PepC has be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a98a7deb55c661824a8aa58a09fab1b
https://hal.inrae.fr/hal-02687845

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