Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Enzymatic production of a protein or polypeptide
Patent
1995-09-28
1998-04-07
Patterson, Jr., Charles L.
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Enzymatic production of a protein or polypeptide
435193, 4351723, 4352523, 43525233, 43525411, 4353201, 435325, 43525421, 536 232, 426573, C12N 1554, C12N 119, C12N 121, C12N 100, C12N 1563, C12N 912, C12N 510, C12P 2100
Patent
active
057363560
DESCRIPTION:
BRIEF SUMMARY
TECHNICAL FIELD
The present invention relates to a novel transglutaminase, i.e., transglutaminase originating from Japanese oyster (zoological name: Crassostrea gigas), a method for gelating a protein using the same, a gene coding for the transglutaminase originating from Crassostrea gigas, a recombinant plasmid carrying the gene incorporated therein, a transformant comprising the plasmid introduced therein, a method for preparing the transglutaminase originating from Crassostrea gigas comprising the step of cultivating the transformant or the like.
BACKGROUND OF THE INVENTION
The transglutaminase is an enzyme which catalyzes a reaction for converting, into a variety of primary amines, the acyl groups on the .gamma.-carboxyamide groups of glutamine residues present in a protein or a peptide chain.
When the .epsilon.-amino group of a lysine residue present in a protein acts as a receptor of acyl group, .epsilon.-(.gamma.-glutamyl)-lysine cross/ink are intramolecularly and intermolecularly formed. For this reason, if such intermolecular crosslinking takes place in a protein, the protein is converted into a crosslinked high molecular weight polymer through the polymerization. Moreover, if a primary amine such as lysine or a derivative thereof acts as an acyl group-receptor, the primary amine is incorporated into a protein serving as an acyl group-donor. In addition, a water molecule also serves as an acyl group-receptor and glutamine residues of a protein are converted into glutamine acid residues through deamidation in this case.
Until now, there have been identified various transglutaminases originating from mammals, microorganisms and fishes. Those originating from mammals have been discovered and identified in various animals and internal organs, including the transglutaminase originating from the liver of Cavia porcellus (Connellan, et al., Journal of Biological Chemistry, 1971, Vol. 246, No. 4, pp. 1093-1098) as a representative example.
As an example thereof derived from a microorganism, there has been identified a calcium ion (Ca.sup.2+)-independent transglutaminase derived from the genus Streptoverticillium (hereinafter referred to as "BTG"; Enzyme No. EC 2.3.2.13) (see Kanaji, et al., Journal of Biological Chemistry, 1993, Vol. 268, pp. 11565-11572 and U.S. Pat. No. 5,156,956).
In regard to those originating from fishes, cDNA's coding for the transglutaminases originating from Pagrus major, a Theragra chalcogramma, a flatfish(Paralichthys olivaceus) are isolated and the amino acid sequences thereof are elucidated (see YASUEDA, et al., Japanese Un-Examined Patent Publication (hereinafter referred to as "J.P. KOKAI") No. Hei.6-225775 and European Patent Publication No. EP-0555649A).
Moreover, there has recently been reported that the transglutaminase activity is also detected in a crude extract from the adductor muscle of a scallop (Patinopecten yessoensis) (MAMEKOSHI, et al., Collected Resume of Nippon Fisheries Association, Spring Meeting for the 5th fiscal year of Heisei, Lecture No. 715, p. 210). In this respect, however, the transglutaminase per se has not been isolated and therefore, various properties thereof have not yet been investigated.
The transglutaminase may be used for the production of, for instance, gel-like foods and gel-like cosmetics as well as yoghurt, jelly, boiled fish paste and cheese while making use of the ability of the enzyme to convert a protein into a high molecular weight product through crosslinking (ability thereof to gelate a protein) (Japanese Examined Patent Publication (hereinafter referred to as "J.P. KOKOKU") No. Hei 1-50382) and it may further be used in the preparation of thin films of proteins.
Moreover, the products prepared by a reaction which is catalyzed by the transglutaminase are stable to heat and therefore, the enzyme can be used in the production of, for instance, materials for microcapsules and carriers for immobilizing enzymes.
As the transglutaminase presently commercialized, there has been known BTG originating from a microorganism, but this e
REFERENCES:
The Journal of Biological Chemistry, vol. 246, No. 4, pp. 1093-1098, Feb. 25, 1971, John M. Connellan, et al., "Structural Properties of Guinea Pig Liver Transglutaminase".
The Journal of Biological Chemistry, vol. 268, No. 16, pp. 11565-11572, Jun. 5, 1993, Toshiya Kanaji, et al., "Primary Structure of Microbial Transglutaminase From Streptoverticillium sp. Strain s-8112*".
Bulletin of the Japanese Society of Scientific Fisheries, vol. 36, No. 2, 1970, pp. 169-172, Reiji Takashi, et al. "Studies on Muscular Proteins of Fish-II. Preparation of Actomyosin From Carp Muscle" (with partial English translation).
Nippon Suisan Gakkaishi, vol. 57, No. 6, pp. 1203-1210, 1991, Hajime Kishi, et al., "Reactivity of Muscle Transglutaminase on Carp Myofibrils and Myosin B".
Molecular Cloning, Second Edition, pp. 718-721, Sambrook, et al., "Extraction, Purification, and Analysis of Messenger RNA From Eukaryotic Cells".
Biochemistry, vol. 27, No. 8, pp. 2898-2905, 1988, Koji Ikura, et al., "Amino Acid Sequence of Guinea Pig Liver Transglutaminase From Its cDNA Sequence".
Journal of Biochemistry, vol. 104, No. 1, pp. 30-34, 1988 Naoto Tonouchi, et al., "High-Level Expression of Human BSF-2/IL-6 cDNA in Escherichia coli Using a New Type of Expression-Preparation System".
Kumazawa Yoshiyuki
Motoki Masao
Sano Koh-ichiro
Seguro Katsuya
Yasueda Hisashi
Ajinomoto Co. Inc.
Bugaisky Gabriele E.
Patterson Jr. Charles L.
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