Lysozyme solubility in H2O and D2O solutions: a simple relationship

Autor: O. Vidal, François Boué, C. Gripon, L. Legrand, I. Rosenman, M.C. Robert

Publikováno v: ResearcherID

We have determined the temperature dependence of the solubility of lysozyme in light water, heavy water and in a mixture 50% H 2 O 50% D 2 O for various NaCl contents at a given pH. For the solubility measurements, we have used a static light device

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2ccaa5e1325c3067a00ba06f06c88d3
https://doi.org/10.1016/s0022-0248(96)01077-9

Study of Undersaturated C60Solutions in Cs2by Small Angle Neutron Scattering

Autor: L. Legrand, C. Gripon, François Boué, I. Rosenman

Publikováno v: Fullerene Science and Technology. 4:1195-1211

We measured precisely, using the Small Angle Neutron Scattering (SANS) technique, the radius of the carbon nuclei shell of the C60 molecule, in spite of its small value. For this purpose, controlled undersaturated solutions of C60 in CS2, where theC6

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::186606551c45f12164b3c1b3b10fb0e0
https://doi.org/10.1080/10641229608001174

Surface mould-ripened cheeses

Autor: H.-E. Spinnler, J.-C. Gripon

Publisher Summary This chapter discusses the different methods of production and technologies of these cheeses, the microflora, the various biochemical changes that occur during their ripening, their aroma and textural properties, and the control of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2e8c263b1f3cc6088580801ebf6c4507
https://doi.org/10.1016/s1874-558x(04)80043-5

Catalytic properties of the cysteine aminopeptidase PepC, a bacterial bleomycin hydrolase

Autor: J.-C Gripon, M.-Y Mistou

Publikováno v: Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, Elsevier, 1998, 1383, pp.63-70

PepC is a cytoplasmic thiol aminopeptidase widely conserved among lactic acid bacteria. PepC from Lactococcus lactis shares 35-38% identity with aminopeptidases of eukaryotic origins: the yeast and mammalian bleomycin hydrolases (BLMase). In this wor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::257cdd73dd41f3b2c8ecc2eed7144cdd
https://hal.inrae.fr/hal-02693349

Xaa-Pro-dipeptidyl-aminopeptidase from Lactococcus lactis catalyses kinetically controlled synthesis of peptide bonds involving proline

Autor: I, Yoshpe-Besançon, J C, Gripon, B, Ribadeau-Dumas

Publikováno v: Biotechnology and applied biochemistry. 20(1)

Xaa-Pro-dipeptidyl-aminopeptidase (EC 3.4.14.5) from Lactococcus lactis (PepX) was used, for the first time, as a catalyst in kinetically controlled synthesis of peptide bonds involving proline. PepX had amidase and esterase activities in addition to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f7de0f139b4f1d4f4ecf73392f34d616
https://pubmed.ncbi.nlm.nih.gov/7917062