.BETA.-Glucosidase and .BETA.-galactosidase from the periplasmic space of Rhizobium trifolii cells.
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منابع مشابه
Overexpression of Recombinant Human Beta Interferon (rhINF-β) in Periplasmic Space of Escherichia coli
Human Interferon β (INF-β) is a member of cytokines family which different studies have shown its immunomodulatory and antiviral activities. In this study an expression vector was designed and constructed for expression of human INF-β-1b either in shake flasks and bench top bioreactor. The designed vector was constructed based upon pET-25b(+) with T7 promoter. Recombinant human beta interferon ...
متن کاملOverexpression of Recombinant Human Beta Interferon (rhINF-β) in Periplasmic Space of Escherichia coli
Human Interferon β (INF-β) is a member of cytokines family which different studies have shown its immunomodulatory and antiviral activities. In this study an expression vector was designed and constructed for expression of human INF-β-1b either in shake flasks and bench top bioreactor. The designed vector was constructed based upon pET-25b(+) with T7 promoter. Recombinant human beta interferon ...
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A /3-galactosidase was purified 600-fold from bovine testes by ammonium sulfate precipitation, acetone fractionation, and at5nity chromatography on agarose substituted with terminal thio-fl-galactopyranosyl residues. The preparation was devoid of protease, a-fucosidase, ar-mannosidase, pglucosidase, P-glucuronidase, and hyaluronidase activities. A wide variety of compounds containing terminal n...
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The beta-galactosidase from the Antarctic gram-negative bacterium Pseudoalteromonas haloplanktis TAE 79 was purified to homogeneity. The nucleotide sequence and the NH(2)-terminal amino acid sequence of the purified enzyme indicate that the beta-galactosidase subunit is composed of 1,038 amino acids with a calculated M(r) of 118,068. This beta-galactosidase shares structural properties with Esc...
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beta-D-Galactosidase (EC 3.2.1.23) was extracted from Streptococcus thermophilus grown in deproteinized cheese whey. Cultural conditions optimum for maximum enzyme production were pH 7.0, 40 degrees C, and 24 h. Proteose peptone (2.0%, wt/vol) and corn steep liquor (2.8%, wt/vol) were highly stimulatory, increasing the enzyme units available in their absence from 660 U/liter of medium to 18,200...
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ژورنال
عنوان ژورنال: The Journal of General and Applied Microbiology
سال: 1982
ISSN: 1349-8037,0022-1260
DOI: 10.2323/jgam.28.551