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Y0875
Keyword:'Y0875'
Showing 1-12 of 12 results for "Y0875" within Papers
Biology, 10(10) (2021-10-24)
Carrageenases appear in various species of marine bacteria and are widely used for the degradation of carrageenans, the commercially significant sulphated polysaccharides. The carrageenase production ability of six different Cellulophaga species was identified, with ι-carrageenase being the most abundant carrageenolytic
Characterization and antimicrobial potential of extremely halophilic archaea isolated from hypersaline environments of the Algerian Sahara
Microbiological research, 186, 119-131 (2016)
Fermentation optimization, purification and biochemical characterization of a porphyran degrading enzyme with funoran side-activity from Zobellia uliginosa
Biocatalysis and agricultural biotechnology, 43.0, 102394-102394 (2022)
The Journal of biological chemistry, 279(19), 20118-20126 (2004-02-21)
The effect of Ca2+ in calpain activation is mediated via several binding sites in the enzyme molecule. To test the contribution of structural elements suspected to be part of this Ca2+ relay system, we made a site-directed mutagenesis study on
Chlamydomonas in the Laboratory
The Chlamydomonas Sourcebook (2009)
The Biochemical journal, 362(Pt 2), 383-388 (2002-02-21)
Typical calpains are heterodimeric cysteine proteases which have distinct large catalytic subunits (80 kDa) but share a common small regulatory subunit (30 kDa; css1). Here we report the identification, cloning and characterization of a novel human small subunit (css2) encoded
Journal of applied microbiology, 97(1), 93-103 (2004-06-10)
Isolation, identification and characterization of a highly efficient isomaltulose producer. After an enrichment procedure for bacteria likely to metabolize isomaltulose in sucrose-rich environments, 578 isolates were screened for efficient isomaltulose biosynthesis using an aniline/diphenylamine assay and capillary electrophoresis. An isolate
FEBS letters, 582(15), 2149-2154 (2008-06-04)
The activity of calpain is controlled by the free intracellular calcium level and by the protein's intrinsically disordered endogenous inhibitor, calpastatin, mediated by short conserved segments: subdomains A-C. The exact binding mode of calpastatin to the enzyme has until now
International journal of biological macromolecules, 166, 789-797 (2020-11-07)
The ι-carrageenan degrading marine bacterium, Cellulophaga baltica, was isolated from the surface of a filamentous red alga Vertebrata fucoides. Maximum ι-carrageenase production was optimized by single-factor experiments. Optimal fermentation conditions were 1.6 g/L furcellaran, 4 g/L yeast extract as carbon sources, 5 g/L
Comparison of different signal peptides for secretion of heterologous proteins in fission yeast
Biochemical and Biophysical Research Communications, 336(3), 974-982 (2005)
Biochemical and biophysical research communications, 336(3), 974-982 (2005-09-15)
In the fission yeast Schizosaccharomyces pombe, there are relatively few signal peptides available and most reports of their activity have not been comparative. Using sequence information from the S. pombe genome database we have identified three putative signal peptides, designated
International journal of systematic and evolutionary microbiology, 59(Pt 4), 886-892 (2009-03-31)
A Gram-negative, arsenate-respiring and arsenite-oxidizing marine bacterium, NKSG1(T), was isolated from hydrothermal sediment at Santorini, Greece. Strain NKSG1(T) was a facultatively anaerobic, motile, non-spore-forming, rod-shaped bacterium. Growth occurred optimally at 35-40 degrees C, between pH 5.5 and 9.0 and with
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