WO2004029082A1 - 乳酸菌が産生する抗菌性物質 - Google Patents
乳酸菌が産生する抗菌性物質 Download PDFInfo
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- WO2004029082A1 WO2004029082A1 PCT/JP2003/012123 JP0312123W WO2004029082A1 WO 2004029082 A1 WO2004029082 A1 WO 2004029082A1 JP 0312123 W JP0312123 W JP 0312123W WO 2004029082 A1 WO2004029082 A1 WO 2004029082A1
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- Prior art keywords
- jas
- aca
- tgt
- antibacterial
- aaa
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Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L3/00—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs
- A23L3/34—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs by treatment with chemicals
- A23L3/3454—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs by treatment with chemicals in the form of liquids or solids
- A23L3/3463—Organic compounds; Microorganisms; Enzymes
- A23L3/34635—Antibiotics
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/315—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L3/00—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs
- A23L3/34—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs by treatment with chemicals
- A23L3/3454—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs by treatment with chemicals in the form of liquids or solids
- A23L3/3463—Organic compounds; Microorganisms; Enzymes
- A23L3/3526—Organic compounds containing nitrogen
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
- C12N1/20—Bacteria; Culture media therefor
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
- C12N1/20—Bacteria; Culture media therefor
- C12N1/205—Bacterial isolates
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/74—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
- C12N15/746—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora for lactic acid bacteria (Streptococcus; Lactococcus; Lactobacillus; Pediococcus; Enterococcus; Leuconostoc; Propionibacterium; Bifidobacterium; Sporolactobacillus)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12R—INDEXING SCHEME ASSOCIATED WITH SUBCLASSES C12C - C12Q, RELATING TO MICROORGANISMS
- C12R2001/00—Microorganisms ; Processes using microorganisms
- C12R2001/01—Bacteria or Actinomycetales ; using bacteria or Actinomycetales
- C12R2001/46—Streptococcus ; Enterococcus; Lactococcus
Definitions
- the present invention belongs to the technical field of antibacterial substances that can be used for purposes such as preservation of foods, and particularly relates to a novel lactic acid bacterium strain and a novel antibacterial peptide produced by the strain.
- nisin A J. Am. Chem. Soc. 1971 Sep 8; 93 (18)
- Nisin Z Eur. J. Biochem. 1991 Nov 1; 201 (3): 581-4
- nisins A and Z have been reported to exist in nature.
- antibacterial substances produced by lactic acid bacteria to prevent food spoilage and spoilage is an important technology from the viewpoint of preserving food without deterioration in quality and providing safe food.
- Such antibacterial substances can be said to be a fight against resistant bacteria.
- An object of the present invention is to provide a new antibacterial agent useful for preserving foods, etc., which has a different antibacterial spectrum (difference in antibacterial activity against multiple bacterial strains to be inhibited) from conventionally known antibacterial agents. To provide a substance. Ming disclosure
- the present inventor focused on antibacterial substances produced by lactic acid bacteria, and as a result of repeated research, found that the genus Bacillus Bacillus, Micrococcus, Mici-ococcus, genus, Listeria. Enterococcus, Entei-ococcus, genus, genus Ratococcus (Lactococcus), genus Lactobacillus (Lactobacillus), and genus Leuconostoc (euconostoc), which have antimicrobial activity against microorganisms that cause food deterioration (that is, susceptible gram-positive bacteria) Lactococcus lactis, a novel lactic acid bacterium strain that produces a substance (having inhibitory activity against lactococcus), purification and identification of the antibacterial substance (peptide), elucidation of its primary structure, and higher-order structure was estimated to derive the present invention.
- the present invention provides an antimicrobial peptide having a primary structure consisting of the following amino acid sequence (SEQ ID NO: 1):
- a precursor peptide of the above antibacterial peptide which peptide has the following amino acid sequence (SEQ ID NO: 2): -20 -1 5-10
- DNA encoding each of the above peptides there is provided DNA encoding each of the above peptides.
- a preferred example of a DNA encoding the above-mentioned precursor peptide consists of the following nucleotide sequence (SEQ ID NO: 4):
- the present invention further provides a food preservative containing the above antibacterial peptide as an active ingredient.
- FIG. 1 shows the primary amino acid sequence of the antimicrobial peptide (Nisin Q) of the present invention. This is shown in comparison with the known primary amino acid sequence of nisin Z.
- FIG. 2 shows an example of the results of an experiment conducted to investigate that the antimicrobial peptide (Nisin Q) of the present invention can be used as a food preservative.
- the antibacterial substance obtained by the present invention is a novel peptide (bacteriocin) produced by a ratatococcus ratatis strain newly isolated from river water. Is considered to be a new type of nisin composed of different amino acid sequences.
- 61-14 strain It was identified as ⁇ Lactococcus lac tis) and named 61-14 strain.
- the 61-14 strain has been deposited with the Patent Organism Depositary, and has the accession number FERM BP-08492 (FERM P-18994: original date of deposit: September 4, 2002).
- the cells were cultured in MRS liquid medium for 16 hours, centrifuged, the supernatant was collected, and the pH was adjusted to 6. After that, it was sterilized by filtration. Two-fold serial dilutions were performed and used for testing. A serial dilution of 10 ⁇ ⁇ ⁇ was placed on the agar medium inoculated with the indicator bacteria.
- the antimicrobial activity was defined as XX 1000/10 (AU / ml), where X is the magnification at which a clear inhibition circle was observed.
- the test results are shown in Table 1 in comparison with the case using Nisin Z.
- nisin Q the antibacterial substance (antibacterial peptide) produced by the 61-14 strain (FERM BP-08492) according to the present invention is referred to herein as nisin Q.
- Preculture the isolates 61-14 inoculate 8 ml of the preculture into 1 L of MRS (oxoid) liquid medium, culture at 30 ° C for 18 hours, centrifuge, Qing was recovered. 1 L of the culture supernatant was recovered, and the activity was 1.28 ⁇ 10 4 (AU / ml). 20 g of Amberlite XAD-16 (Sigma) sufficiently immersed in 2-propanol was added to the supernatant, and the mixture was shaken for 3 hours to adsorb the supernatant.
- SP—Sepharose cation exchange chromatography resin (Pharmacia) The column (ltol volume) was packed, 50 ml of the concentrated sample was added, and equilibrated with 20 mM sodium phosphate buffer. Elution was performed at a flow rate of 100 ml I hour using a sodium phosphate buffer containing 0.25, 0.5, 0.75, and 0.1 M NaCl.
- the antibacterial activity of each eluted fraction was measured, and the activity of the 0.25 M NaCl eluted fraction, which was the strongest, was 2.62 ⁇ 10 5 (AU / ml).
- 10 ml of the eluted total volume of 50 ml was subjected to reverse phase HPLC (column: Pharmacia P-marked RPC HR 5/5).
- Acetonitrile was used as the mobile phase, and fractionation was performed at a concentration gradient (linear gradient of 0 to 100%) at a flow rate of 1 ml / min at a flow rate of 1 ml / min.
- UV UV (UV 220, 280 nm) was used for the detector.
- the antibacterial activities of the 30 fraction samples were measured, and the fractions with elution times of 12 to 13 minutes having strong antibacterial activities were concentrated and subjected to reverse-phase HPLC again under the same conditions. A single peak and a fraction with an elution time of 9-11 minutes with strong antibacterial activity were obtained. It should be noted that the indicator bacteria of antibacterial activity, using the Bacillus cos "/? S JCM2257 T .
- the antibacterial substance obtained as described above was subjected to N-terminal analysis using an amino acid sequencer (SHMADZU PSQ-1U protein sequener) utilizing the Edman degradation method.
- an amino acid sequencer SHMADZU PSQ-1U protein sequener
- Edman degradation method As a result, the N-terminus of the peptide sequence was identified as lie, but the next amino acid could not be identified.
- the amino acid second from the N-terminus was Thr in the primary structure, but was shown to be modified to a special amino acid.
- the whole genome DNA was extracted using MagExtractor-Genome- (T0Y0B0) from the isolate FERM BP-08 ⁇ 92 (Lactococcus 1 act is). The concentration was 60.5 ng / ⁇ 1.
- PCR polymerase chain reaction
- the PCR primers used at this time were designed based on the nucleotide sequences around the nisin A and nisin Z precursor structural genes. It consists of an oligonucleotide sequence.
- PCR was performed using Premix TaqONA polymerase (Ex-Taq TAKARA). The extension reaction was performed at 94 ° C for 30 seconds, 51 ° C for 30 seconds, and 72 ° C for 60 seconds for 30 cycles.
- TA cloning was performed using a pUC18-derived T vector.
- DNA Ligation Kit Ver. 2 (TAKARA) was used for ligation of the PCR amplified fragment and the T vector.
- E. coli JM109 was transformed by electroporation. After transformants were cultured in LB medium for 8 hours, plasmids were extracted using MagExtractor-Plasmid- (T0Y0B0). This plasmid was designated as type II of the sequence reaction.
- a Thrmo Sequense fluorescent label led primer cycle sequencing kit was used for the sequencing reaction.
- sequence reaction was incubated at 95 ° C for 5 minutes, followed by 15 cycles of 95 ° C for 30 seconds, 55 ° C for 30 seconds, and 72 ° C for 1 minute, followed by 15 cycles of 95 ° C for 30 seconds and 72 ° C for 1 minute I went.
- T at base 18 is C
- G at base 24 is A
- G at base 42 is A
- G at base 45 is A
- a of base 47 is C
- a of base 54 is T
- T of base 57 is C
- a of base 60 is T
- C of base 64 is A
- C of base 69 is A
- base 75 A is base C
- base 78 base T is base C
- base 87 base A is base T
- base 96 base C is base A
- base 111 base A is base T
- base 113 The base C was different from T
- the base 123 was different from A
- the base 130 was different from A
- the base 156 was different from T
- the base 157 was different from G.
- the difference in the nucleotide sequence that affects the peptide sequence compared to Nisin Z is that the amino acid residue _8th Lys is Thr due to the difference in base 47 and the amino acid residue-Thr 2 , 113 base difference, amino acid residue 15 Ala is Val, 130 base difference is amino acid residue 21 Met is Leu, 157 base difference is amino acid residue The 30th lie is Val (see Figure 1). In FIG. 1
- nisin Q which is the amino acid sequence (SEQ ID NO: 2) of the precursor peptide of the antibacterial peptide produced from FERM P-18994 according to the present invention, and I (isoleucine: lie) ) Is the amino acid sequence of the primary structure of the peptide (SEQ ID NO: 1), which finally functions as an antibacterial peptide. The attached portion becomes the amino acid sequence of the leader peptide.
- the antimicrobial peptide (Nisin Q) of the present invention is a substance completely different from known Nisin Z.
- nisin Q (nisin Q precursor peptide) is not limited to the DNA sequence of SEQ ID NO: 4, and DNA that can encode nisin Q consisting of the amino acid sequence of SEQ ID NO: 2 in consideration of codon degeneracy. All sequences are included.
- nisin Q may be similar to the higher-order structure of nisin Z Is done. Therefore, the higher-order structure of nisin Q was estimated as follows. That is, the following amino acid sequence:
- Met Gly Cys Asn Leu Lys Thr Ala Thr Cys Asn Cys Ser ValHis Has a primary structure consisting of Val Ser Lys. Serine is modified to 2,3-didehydroalanine, respectively, and serine at position 3 is modified to alanine, and threonine at positions 8, 13, 23, 25 is modified. Are modified to 2-aminobutyric acid (Abu), respectively.
- the thioether bond of Abu-S-Cys forms 3-methyllantonin, and positions 25 and 28 form the thioether bond of Abu-S-Cys to form 3-methyllantonin (SEQ ID NO: 3).
- the theoretical molecular weight was calculated from the amino acid sequence of SEQ ID NO: 3 estimated as described above, and the result was 33327.43. Therefore, the molecular weight was measured using MALDI-TOF MS (PE Biosystems Voyager System 4025), which can accurately measure the molecular weight. Since the measured sample is measured by adding a proton, the measured value is 1 Da. Higher than the actual molecular weight.
- Ratatococcus lactis 61-14 strain (FERM BP-08492) was cultured in 10 ml of MRS (D co) medium at 30 ° C. for 24 hours.
- the culture solution was inoculated into 100 ml of MRS medium (containing 2% calcium carbonate) and cultured at 30 ° C for 24 hours.
- This culture solution is added to MRS medium (2% 1 L was inoculated, cultured for 16 hours, centrifuged, and the supernatant was collected.
- To the supernatant was added 20 g of Amberley 1, XAD-16 (Sigma) (a substance sufficiently swollen with 2-propanol and washed with distilled water), immersed for 16 hours, and adsorbed.
- Figure 2 shows the test results. At each pH, we examined the conditions under the same conditions as the retort sterilization conditions.Since dilution had an inhibitory effect on growth, food materials that are expected to undergo heat treatment at about the retort level, and unheated food materials are also considered. Has also been confirmed to be available.
- MRS medium manufactured by DIFCO
- strain 61-14 strain 61-14
- FERM BP-08492 strain 61-14
- a novel antibacterial substance useful as a food preservative or the like is provided,
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Abstract
Description
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Priority Applications (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
KR1020057005304A KR100662719B1 (ko) | 2002-09-25 | 2003-09-24 | 유산균으로부터 생산되는 항균성 물질 |
AU2003275532A AU2003275532A1 (en) | 2002-09-25 | 2003-09-24 | Antibacterial substance produced by lactic acid bacterium |
JP2004539487A JP3740499B2 (ja) | 2002-09-25 | 2003-09-24 | 乳酸菌が産生する抗菌性物質 |
CNA038227940A CN1684976A (zh) | 2002-09-25 | 2003-09-24 | 乳酸菌产生的抗菌性物质 |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
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JP2002278901 | 2002-09-25 | ||
JP2002-278901 | 2002-09-25 |
Publications (1)
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WO2004029082A1 true WO2004029082A1 (ja) | 2004-04-08 |
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PCT/JP2003/012123 WO2004029082A1 (ja) | 2002-09-25 | 2003-09-24 | 乳酸菌が産生する抗菌性物質 |
Country Status (5)
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JP (1) | JP3740499B2 (ja) |
KR (1) | KR100662719B1 (ja) |
CN (1) | CN1684976A (ja) |
AU (1) | AU2003275532A1 (ja) |
WO (1) | WO2004029082A1 (ja) |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN102181383A (zh) * | 2011-02-23 | 2011-09-14 | 中国科学院微生物研究所 | 一株来源于妇女生殖道产细菌素的益生乳酸菌 |
JP2015526095A (ja) * | 2012-08-22 | 2015-09-10 | クラフト・フーズ・グループ・ブランズ・エルエルシー | 発酵乳成分を有するプロセスチーズ及びその製造方法 |
WO2023080136A1 (ja) | 2021-11-02 | 2023-05-11 | 住友化学株式会社 | 抗菌ペプチド |
Families Citing this family (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
KR20070051589A (ko) * | 2005-11-15 | 2007-05-18 | 엘지전자 주식회사 | 증기분사식 드럼세탁기의 항균 및 살균장치 |
US8316673B2 (en) | 2005-11-15 | 2012-11-27 | Lg Electronics Inc. | Apparatus of supplying and discharging fluid and method of operating the same |
ES2557578T3 (es) * | 2010-12-17 | 2016-01-27 | Compagnie Gervais Danone | Cepas de Lactococcus lactis para uso en la mejora del estado digestivo |
CN104945467B (zh) * | 2015-06-23 | 2018-12-18 | 中山大学 | 一种抗菌肽的人工合成方法 |
CN109485701B (zh) * | 2018-11-27 | 2020-06-16 | 仲恺农业工程学院 | 抗菌肽、抗菌药物以及制备方法 |
Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1992018633A1 (en) * | 1991-04-11 | 1992-10-29 | Stichting Nederlands Instituut Voor Zuivelonderzoek (Nizo) | Lantibiotics similar to nisin a, lactic acid bacteria which produce such lantibiotics, method for constructing such lactic acid bacteria and method for preserving foodstuffs with the aid of these lantibiotics and these lactic acid bacteria producing lantibiotics |
US5232849A (en) * | 1991-07-01 | 1993-08-03 | Quest International Flavors & Food Ingredients Company Division Of Indopco, Inc. | Bacteriocin from lactococcus lactis subspecies lactis |
EP0573768A2 (en) * | 1992-05-08 | 1993-12-15 | Quest International B.V. | Multiple bacteriocin producing lactococcus and compositions |
-
2003
- 2003-09-24 KR KR1020057005304A patent/KR100662719B1/ko not_active IP Right Cessation
- 2003-09-24 CN CNA038227940A patent/CN1684976A/zh active Pending
- 2003-09-24 WO PCT/JP2003/012123 patent/WO2004029082A1/ja active Application Filing
- 2003-09-24 AU AU2003275532A patent/AU2003275532A1/en not_active Abandoned
- 2003-09-24 JP JP2004539487A patent/JP3740499B2/ja not_active Expired - Fee Related
Patent Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1992018633A1 (en) * | 1991-04-11 | 1992-10-29 | Stichting Nederlands Instituut Voor Zuivelonderzoek (Nizo) | Lantibiotics similar to nisin a, lactic acid bacteria which produce such lantibiotics, method for constructing such lactic acid bacteria and method for preserving foodstuffs with the aid of these lantibiotics and these lactic acid bacteria producing lantibiotics |
US5232849A (en) * | 1991-07-01 | 1993-08-03 | Quest International Flavors & Food Ingredients Company Division Of Indopco, Inc. | Bacteriocin from lactococcus lactis subspecies lactis |
EP0573768A2 (en) * | 1992-05-08 | 1993-12-15 | Quest International B.V. | Multiple bacteriocin producing lactococcus and compositions |
Non-Patent Citations (3)
Title |
---|
TADANORI FUKAO ET AL.: "Nisin Q, Dai 3 no Shinki Nisin ten' nen Ruientai,", JAPAN SOCIETY FOR BIOSCIENCE, BIOTECHNOLOGY, AND AGROCHEMISTRY 2003 NENDO (HEISEI 15 NENDO) TAIKAI KOEN YOSHISHU, 5 March 2003 (2003-03-05), pages 155, XP002977434 * |
TAKEFUMI YOSHIFUJI ET AL.: "Atarashii Nyusankin Bacteriocin no Tansaku to Riyo", BIOSCIENCE TO BIOINDUSTRY, vol. 61, no. 9, 1 September 2003 (2003-09-01), pages 597 - 602, XP002977433 * |
ZENDO T. ET AL.: "Identification of the lantibiotic nisin Q, a new natural nisin variant produced by lactococcus lactis 61-14 isolated from a river in Japan,", BIOSCI. BIOTECHNOL. BIOCHEM, vol. 67, no. 7, July 2003 (2003-07-01), pages 1616 - 1619, XP002977432 * |
Cited By (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN102181383A (zh) * | 2011-02-23 | 2011-09-14 | 中国科学院微生物研究所 | 一株来源于妇女生殖道产细菌素的益生乳酸菌 |
CN102181383B (zh) * | 2011-02-23 | 2012-10-10 | 中国科学院微生物研究所 | 一株来源于妇女生殖道产细菌素的益生乳酸菌 |
JP2015526095A (ja) * | 2012-08-22 | 2015-09-10 | クラフト・フーズ・グループ・ブランズ・エルエルシー | 発酵乳成分を有するプロセスチーズ及びその製造方法 |
US10375972B2 (en) | 2012-08-22 | 2019-08-13 | Kraft Foods Group Brands Llc | Processed cheese with cultured dairy components and method of manufacturing |
US11464238B2 (en) | 2012-08-22 | 2022-10-11 | Kraft Foods Group Brands Llc | Processed cheese with cultured dairy components and method of manufacturing |
WO2023080136A1 (ja) | 2021-11-02 | 2023-05-11 | 住友化学株式会社 | 抗菌ペプチド |
KR20240095281A (ko) | 2021-11-02 | 2024-06-25 | 스미또모 가가꾸 가부시키가이샤 | 항균 펩티드 |
Also Published As
Publication number | Publication date |
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JPWO2004029082A1 (ja) | 2006-01-26 |
KR20050057594A (ko) | 2005-06-16 |
KR100662719B1 (ko) | 2006-12-28 |
AU2003275532A1 (en) | 2004-04-19 |
JP3740499B2 (ja) | 2006-02-01 |
CN1684976A (zh) | 2005-10-19 |
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