Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Alberto Ruiz-Arribas"'
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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The production of the cellulase Cell from Streptomyces halstedii JM8 was studied in cells grown in the presence of glucose, cellobiose or microcrystalline cellulose (Avicel). Among these, glucose repressed expression while cellobiose and Avicel exert
Autor:
Ramón I. Santamaría, Valery L. Shnyrov, Alberto Ruiz-Arribas, José M. Fernández-Abalos, Javier De Las Rivas, Sonia Rodríguez, Margarita Díaz
Publikováno v:
FEMS Microbiology Letters. 240:237-243
Mutagenesis of the xylanase Xys1 of Streptomyces halstedii JM8 has been done by error prone PCR. Mutants with modified hydrolytic activity were isolated, the recombinant variant proteins purified and the catalytic activities of each one determined an
Autor:
Juan J. Calvete, Galina G. Zhadan, Victor P. Kutyshenko, Alberto Ruiz-Arribas, Enrique Villar, Ramón I. Santamaría, Manuel Cortijo, José M. Fernández-Abalos, Valery L. Shnyrov
Publikováno v:
European Journal of Biochemistry. 253:462-468
In a continuation of our earlier study [Ruiz-Arribas, A., Santamaria, R.I., Zhadan, G. G., Villar, E. & Shnyrov, V. L. (1994) Differential scanning calorimetric study of the thermal stability of xylanase from Streptomyces halstedii JM8, Biochemistry
Autor:
Alberto Ruiz-Arribas, Ramón I. Santamaría, Pilar Sánchez, Ana Lila Garda, José M. Fernández-Abalos
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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Streptomyces halstedii JM8, isolated from straw, produces and secretes into the culture supernatant at least two proteins with hydrolytic activity towards xylan. The cloning of a DNA fragment of this microorganism in several Streptomyces strains perm
Autor:
Ramón I. Santamaría, Enrique Villar, Alberto Ruiz-Arribas, Galina G. Zhadan, Valery L. Shnyrov
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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The thermal stability of two xylanases with molecular masses of 45 (Xys1L) and 35 (Xys1S) kDa has been characterized thermodynamically by high-sensitivity scanning microcalorimetry in the pH range 3.0-9.0. Thermal denaturation of Xys1L reveals three
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc61a1cfeecc496662c5c4bd87e35328
http://hdl.handle.net/10261/66324
http://hdl.handle.net/10261/66324
Autor:
Pablo Sánchez, Ramón I. Santamaría, M Raida, Juan J. Calvete, Alberto Ruiz-Arribas, José M. Fernández-Abalos
Publikováno v:
Scopus-Elsevier
ResearcherID
CIÊNCIAVITAE
Europe PubMed Central
ResearcherID
CIÊNCIAVITAE
Europe PubMed Central
The gene xysA from Streptomyces halstedii JM8 encodes a protein of 461 amino acids (Xys1) which is secreted into the culture supernatant as a protein of 45 kDa (Xys1L). Later, this form is proteolytically processed after residue D-362 to produce the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::745cba18cce035fe6443c5e880107629
http://www.scopus.com/inward/record.url?eid=2-s2.0-0343307144&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0343307144&partnerID=MN8TOARS