Process for producing hydroxynitrile lyases

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Lyase

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C435S069100, C435S252330, C435S320100, C536S023200

Reexamination Certificate

active

10169430

ABSTRACT:
The present invention relates to an improved process for producing hydroxynitrile lyases. A process is provided whereby hydroxynitrile lyases may be produced by cultivation in bacteria or suitable host cells. Cells containing a gene encoding for a hydroxynitrile lyase may be precultivated, induced with a low concentration of IPTG, cultured, and lysed. The process allows for the production of relatively large quantities of hydroxynitrile lyases in a dissolved, native, and active form, and without the presence of substantial amounts of inclusion bodies, and thus allowing for the production of the lyases without requiring expensive and time consuming renaturation steps.

REFERENCES:
patent: 6046042 (2000-04-01), Hasslacher et al.
patent: 6387659 (2002-05-01), Semba
patent: 0927766 (1998-12-01), None
Hasslacher et al. High-level intracellular expression of hydroxynitrile lyase from the tropical rubber treeHevea brasiliensisin microbial hosts. Protein Expr Purif. Oct. 1997;11: p. 61-71.
Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase fromHevea brasiliensis.Hasslacher et al. Molecular cloning of full-length cDNA of (S)-Hydroxynitrile Lyase fromHevea brasiliensis.J Biol Chem. Mar. 8, 1996;271(10):p. 5884-91. □□.
Nakamura et al. Hyperproduction of recombinant ferredoxins inEscherichia coliby coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hs cA-fdx-ORF3 gene cluster.J Biochem (Tokyo). Jul. 1999;126(1):p. 10-8. □□.
Kopetzki et al. “Control of formation of active soluble or inactive insoluble baker's yeast alpha-glucosidase PI inEscherichia coliby induction and growth conditions”, Mol Gen Genet. Mar. 1989; 216(1):149-55.
Ouzzine et al. “Expression of active, human lysyl oxidase inEscherichia coli”, FEBS Lett. Dec. 16, 1996;399(3):215-9).
Weickert et al. “Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin inEscherichia coli”, Appl Environ Microbiol. Nov. 1997; 63(11): 4313-20.
Breithaupt et al., Cloning and expression of (R)-hydroxynitrile lyase fromLinum usitatissimum(flax), (1999) pp. 315-332, Elsevier Science.
Hasslacher et al., High-Level Intracellular Expression of Hydroxynitrile Lyase from the Tropical Rubber TreeHevea brasiliensisin Microbial Hosts, Protein Expression and Purification 11, (1997), pp. 61-71, Article No. PT970765, Academic Press.
Enzyme-Catalyzed Preparation and Synthetic Applications of Optically Active Cyanohydrins; Franz Effenberger, CHIMIA 1999.
Identification of Potential Active-site Residues in the Hydroxynitrile Lyase fromManihot esculentaby Site-directed Mutagenesis*; Harald Wajant and Klaus Pfizenmaier; vol. 271, No. 42, Issue Oct. 18, pp. 25830-25834, 1996.
High-Level Intracellular Expresson of Hydroxynitrile Lyase from the Tropical Rubber TreeHevea brasiliensisin Microbial Hosts; Meinhard Hasslacher, et al; Protein Expression and Purification 11, 61-71 (1997) Article No. PT970765.
Molecular Cloning of the Full-length cDNA of (S)-Hydroxynitrile Lyase fromHevea brasiliensis; Meinhard Hasslacher, et al; vol. 271, No. 10, Issue of Mar. 8, pp. 5884-5891, 1996—The Journal of Biological Chemistry.

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Process for producing hydroxynitrile lyases does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Process for producing hydroxynitrile lyases, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Process for producing hydroxynitrile lyases will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3783263

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.