| a novel protein-deamidating enzyme from chryseobacterium proteolyticum sp. nov., a newly isolated bacterium from soil. | a novel protein-deamidating enzyme, which has potential for industrial applications, was purified from the culture supernatant of chryseobacterium proteolyticum strain 9670(t) isolated from rice field soil in tsukuba, japan. the deamidating activities on carboxybenzoxy (cbz)-gln-gly and caseins and protease activity were produced synchronously by the isolate. both deamidating activities were eluted as identical peaks separated from several proteases by phenyl-sepharose chromatography of the cult ... | 2000 | 10919788 |
| protein-glutaminase from chryseobacterium proteolyticum, an enzyme that deamidates glutaminyl residues in proteins. purification, characterization and gene cloning. | a novel protein-deamidating enzyme was purified to homogeneity from chryseobacterium proteolyticum and the gene encoding it was cloned. the enzyme is a monomer with a pi of 10.0, a measured m(r) of approximately 20,000 and a calculated m(r) of 19,860. extensive comparison with streptoverticillium transglutaminase showed that the protein-deamidating enzyme lacked transglutaminase activity in terms of hydroxamate-formation between benzyloxycarbonyl-gln-gly and hydroxylamine, or monodansylcadaverin ... | 2001 | 11231294 |
| effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten. | protein-glutaminase (pg) purified from chryseobacterium proteolyticum was used to investigate its deamidation effects on wheat gluten. water-insoluble gluten was able to be deamidated to the extent of deamidation degree (dd) 72% in 200 mm sodium phosphate buffer (ph 7) at 40 degrees c for 30 h. sodium dodecyl sulfate-polyacrylamide gel electrophoresis exhibited an upper shift of gluten bands with only deamidation for 1.5-2.0 h (dd 35-45%) compared to the bands of nondeamidated gluten. results of ... | 2006 | 16881713 |
| studies on the non-pathogenicity of chryseobacterium proteolyticum and on the safety of the enzyme: protein-glutaminase. | protein-glutaminase (pg) is a protein-deamidating enzyme produced from the microorganism chryseobacterium proteolyticum strain 9670. food safety studies were conducted on both the enzyme and the production organism. the strain was evaluated for pathogenicity and toxigenicity by intravenous and oral inoculation studies in slc:icr male spf mice. the results demonstrate that the tested c. proteolyticum strain is of very low pathogenicity comparable to known food source bacterial strains and is very ... | 2007 | 17630060 |
| production of chryseobacterium proteolyticum protein-glutaminase using the twin-arginine translocation pathway in corynebacterium glutamicum. | the protein glutaminase (pg) secreted by the gram-negative bacterium chryseobacterium proteolyticum can deamidate glutaminyl residues in several substrate proteins, including insoluble wheat glutens. this enzyme therefore has potential application in the food industry. we assessed the possibility to produce pg containing a pro-domain in corynebacterium glutamicum which we have successfully used for production of several kinds of proteins at industrial-scale. when it was targeted to the general p ... | 2008 | 18064454 |
| tatabc overexpression improves corynebacterium glutamicum tat-dependent protein secretion. | the twin-arginine translocation (tat) pathway in corynebacterium glutamicum has been described previously. the minimal functional tat system in c. glutamicum required tata and tatc but did not require tatb, although this component was required for maximal efficiency of tat-dependent secretion. we previously demonstrated that chryseobacterium proteolyticum pro-protein glutaminase (pro-pg) and streptomyces mobaraensis pro-transglutaminase (pro-tg) could be secreted via the tat pathway in c. glutam ... | 2009 | 19074606 |
| the nmr structure of protein-glutaminase from chryseobacterium proteolyticum. | | 2010 | 20195702 |