Proteins from PHB granules
نویسندگان
چکیده
منابع مشابه
The complex structure of polyhydroxybutyrate (PHB) granules: four orthologous and paralogous phasins occur in Ralstonia eutropha.
Analysis of the genome sequence of the polyhydroxyalkanoate- (PHA) accumulating bacterium Ralstonia eutropha strain H16 revealed three homologues (PhaP2, PhaP3 and PhaP4) of the phasin protein PhaP1. PhaP1 is known to constitute the major component of the layer at the surface of poly(3-hydroxybutyrate), poly(3HB), granules. PhaP2, PhaP3 and PhaP4 exhibited 42, 49 and 45 % identity or 61, 62 and...
متن کاملSimulation of Bioreactors for PHB Production from Natural Gas
Recently, many economic studies of poly(3-hydroxybutyrate) PHB production on an industrial scale, and the impact of replacing petrochemical polymers by PHB were carried out, clearly indicating that the most crucial factors to reduce the cost of producing biopolymers are allotted to the application of microbial production strains capable of high productivi...
متن کاملNovel Extracellular PHB Depolymerase from Streptomyces ascomycinicus: PHB Copolymers Degradation in Acidic Conditions
The ascomycin-producer strain Streptomyces ascomycinicus has been proven to be an extracellular poly(R)-3-hydroxybutyrate (PHB) degrader. The fkbU gene, encoding a PHB depolymerase (PhaZ Sa ), has been cloned in E. coli and Rhodococcus sp. T104 strains for gene expression. Gram-positive host Rhodococcus sp. T104 was able to produce and secrete to the extracellular medium an active protein form....
متن کاملMultiple Poliovirus Proteins Repress Cytoplasmic RNA Granules
We have previously shown that poliovirus (PV) infection induces stress granule (SG) formation early in infection and then inhibits the formation of SG and disperses processing bodies (PBs) by the mid-phase of infection. Loss of SG was linked to cleavage of G3BP1 by viral 3C proteinase (3C(pro)), however dispersal of PBs was not strongly linked to cleavage of specific factors by viral proteinase...
متن کاملStudy of Co(II) adsorption from aqueous solution using protein granules produced from chicken feather
Background: Co(II) constitutes a part of vitamin B12, hence, it is necessary for human health. However, at concentrations higher than the permissible limits, humans and animals suffer adverse chronic effects. It is necessary to reduce the concentration to a permissible level. In the present study, pre-purification and thermal modification of chicken’s feather increased their porosity and ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Protein Science
سال: 2009
ISSN: 0961-8368
DOI: 10.1110/ps.051418305