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US4737460A Expired / Lapsed US ⏱️ 0.0 years remaining

Peroxidase and a process of its preparation

Assignee: Suntory Ltd
•
Filing: 1985-08-06
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Granted: 1988-04-12
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Expires: 2005-08-06
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Abstract

Abstract A novel peroxidase that is non specific and that does not contain isozymes and hence, is suitable as a diagnostic reagent or as a marker enzyme in enzyme immunoassay is provided as well as a process of its preparation. The novel peroxidase is produced by a microorganism of a new genus Arthromyces.

Inventors

  • 👤 Yoshifumi Shinmen
  • 👤 Sumio Asami
  • 👤 Norihide Amano
  • 👤 Teruo Amachi
  • 👤 Hajime Yoshizumi
  • 👤 Eiichi Kosugi

Bibliographic Details

Application Number —
Jurisdiction US
Data Source google_patents
Last Synchronized 2026-10-27 21:25
CPC Classifications
C; C12; C12N; C12N9/00; C12N9/0004; C12N9/0065; Y; Y10; Y10S; Y10S435/00; Y10S435/8215; Y10S435/911

Claims Analysis

Total Claims: 5
Claim 1
Independent Claim 146 words
A process for producing a peroxidase comprising the following steps: cultivating a peroxidase producing microorganisum of the strain FERM BP-838 of the genus Arthromyces characterized by the following definitions: belonging to subdivision Deuteromycotina, class Hyphomycetes; the hypha is hyaline, septate and branched; the conidiophore is difficult to discern from a vegetative hyphae; the process of conidium formation is of thallic type; the formation of a conidium starts with the cutting off of the tip of the hypha from the base portion, ad the residual hypha is then fragmented to form a conidium; at the same time, a new hypha arises from the side of the residual hypha immediately beneath the cut plane, and another conidium forms by the same process; the conidium is a short cylinder, and hyaline; type species: Arthromyces ramosus (FERM BP-838) N. Amano, sp. nov.; and recovering the peroxidase accumulated in the culture.
Claim 2
Dependent Claim 146 words
A process for producing a peroxidase comprising the following steps: cultivating a peroxidase producing microorganisum of the strain FERM BP-838 of the genus Arthromyces characterized by the following definitions: belonging to subdivision Deuteromycotina, class Hyphomycetes; the hypha is hyaline, septate and branched; the conidiophore is difficult to discern from a vegetative hyphae; the process of conidium formation is of thallic type; the formation of a conidium starts with the cutting off of the tip of the hypha from the base portion, ad the residual hypha is then fragmented to form a conidium; at the same time, a new hypha arises from the side of the residual hypha immediately beneath the cut plane, and another conidium forms by the same process; the conidium is a short cylinder, and hyaline; type species: Arthromyces ramosus (FERM BP-838) N. Amano, sp. nov.; and recovering the peroxidase accumulated in the culture.
Claim 3
Dependent Claim 188 words
A peroxidase produced by a peroxidase producing microorganism of the strain FERM BP-838 of the genus Arthromyces characterized by the following definitions: belonging to subdivision Deuteromycotina, class Hyphomycetes; the hypha is hyaline, septate and branched; the conidiophore is difficult to discern from a vegetative hyphae; the process of conidium formation is of thallic type; the formation of a conidium starts with the cutting off of the tip of the mycelium from the base portion, and the residual hypha is then fragmented to form a conidium; at the same time, a new hypha arises from the side of the residual hypha immediately beneath the cut plane, and another conidium forms by the same process; the condium is short and cylindrical, and hyaline; type species: Arthromyces ramosus (FERM BP-838) N. Amano, sp. nov., wherein said peroxidase has the following characteristics: optimum pH: 5-7; optimum temperature: 30°-45° C.; stable at pH between 5 and 10; stable at 50° C. or below; molecular weight as determined by SDS-polyacrylamide gel electrophoresis (PAGE): ca. 36,000; isoelectric point (PI) as measured by isoelectric focusing (with Amphorite): pH of ca. 3.4; and absence of any isozyme.
Claim 4
Dependent Claim 188 words
A peroxidase produced by a peroxidase producing microorganism of the strain FERM BP-838 of the genus Arthromyces characterized by the following definitions: belonging to subdivision Deuteromycotina, class Hyphomycetes; the hypha is hyaline, septate and branched; the conidiophore is difficult to discern from a vegetative hyphae; the process of conidium formation is of thallic type; the formation of a conidium starts with the cutting off of the tip of the mycelium from the base portion, and the residual hypha is then fragmented to form a conidium; at the same time, a new hypha arises from the side of the residual hypha immediately beneath the cut plane, and another conidium forms by the same process; the condium is short and cylindrical, and hyaline; type species: Arthromyces ramosus (FERM BP-838) N. Amano, sp. nov., wherein said peroxidase has the following characteristics: optimum pH: 5-7; optimum temperature: 30°-45° C.; stable at pH between 5 and 10; stable at 50° C. or below; molecular weight as determined by SDS-polyacrylamide gel electrophoresis (PAGE): ca. 36,000; isoelectric point (PI) as measured by isoelectric focusing (with Amphorite): pH of ca. 3.4; and absence of any isozyme.
Claim 5
Dependent Claim 118 words
A peroxidase according to claim 2 having the following characteristics: ______________________________________ sedimentation velocity (S.sub.2o,w) Ca. 3.12 S molecular weight as determined by Ca. 36,000 SDS-PAGE sedimentation equilibrium Ca. 41,200 HPLC Ca. 41,000 subunit molecular weight Ca. 36,000 as determined by SDS-PAGE numbers of subunit 1 prosthetic group Protoheme IX E (10 mg/ml, 1 cm, 280 nm) Ca. 7.9 pI Ca. 3.4 sugar content Ca. 5% Km (H.sub.2 O.sub.2) Ca. 0.12 mM (2,4-DCP-4-AA) inhibited by CN.sup.-, N.sub.3.sup.-, S.sub.2 O.sub.4.sup.2-, NH.sub.2 OH, Fe.sup.2+, Hg.sup.2+ optimum pH Ca. 6.0 optimum temperature Ca. 40° C. pH stability stable at pH 5.0-9.0 (30° C., 16 hr) temperature stability stable at 50° C. or below (pH 7.0, 30 min) absence of any isozyme. ______________________________________

References Cited (Backward Citations)

US4328312A Cited
JPS5799192A Cited
JPS59179075A Cited

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