Genetically modified bacillus subtilis strain and use as a live delivery and production system
US-2024390433-A1 · Nov 28, 2024 · US
US2016108388A1 · US · A1
| Field | Value |
|---|---|
| Publication number | US-2016108388-A1 |
| Application number | US-201414893837-A |
| Country | US |
| Kind code | A1 |
| Filing date | May 29, 2014 |
| Priority date | May 29, 2013 |
| Publication date | Apr 21, 2016 |
| Grant date | — |
A practical reading order for non-experts. Skip the full description unless you need deep technical detail.
What the patent document calls the invention.
A short plain-language summary of the technical disclosure.
Who owns or filed the patent and who is credited as inventor.
Filing, priority, publication, and grant dates set the timeline.
The legal scope of protection — read this for what is actually claimed.
Technology tags used to group this patent with similar filings.
Prior art links and similar publications in this corpus.
Official abstract text for this publication.
Aspects of the present compositions and methods relate to novel metalloproteases polynucleotides encoding the novel metalloprotease, compositions and methods for use thereof.
Opening claim text (preview).
1 . A polypeptide comprising an amino acid sequence having at least 60% sequence identity to the amino acid sequence selected from the group consisting of SEQ ID NOs: 3, 6, 9 and 14. 2 . The polypeptide of claim 1 , wherein said polypeptide has at least 80%, 95% or 98% sequence identity to the amino acid sequence selected from the group consisting of SEQ ID NOs: 3, 6, 9 and 14. 3 - 4 . (canceled) 5 . The polypeptide of claim 1 , wherein said amino acid sequence is the amino acid sequence of SEQ ID NO: 3, 6, 9 and/or 14. 6 - 11 . (canceled) 12 . The polypeptide of claim 1 , wherein said polypeptide has protease activity. 13 . The polypeptide of claim 12 , wherein said protease activity comprises casein hydrolysis, collagen hydrolysis, elastin hydrolysis, keratin hydrolysis, soy protein hydrolysis or corn meal protein hydrolysis. 14 . The polypeptide of claim 1 , wherein said polypeptide retains at least 50% of its maximal activity between pH 5 and 9.5 and/or between 30° C. and 80° C. 15 . (canceled) 16 . The polypeptide of claim 1 , wherein said polypeptide has cleaning activity in a detergent composition. 17 . The polypeptide of claim 16 , wherein said detergent composition is an ADW detergent composition, a laundry detergent composition, a liquid laundry detergent composition, or a powder laundry detergent composition. 18 - 21 . (canceled) 22 . The polypeptide of claim 1 , wherein said polypeptide is a recombinant polypeptide. 23 . A composition comprising the polypeptide of claim 1 . 24 . The composition of claim 23 , wherein said composition is a cleaning composition or a detergent composition. 25 . (canceled) 26 . The composition of claim 24 , wherein said detergent composition is selected from the group consisting of a laundry detergent, a fabric softening detergent, a dishwashing detergent, and a hard-surface cleaning detergent. 27 . The composition of claim 23 , wherein said composition further comprises a surfactant; at least one calcium ion and/or zinc ion; at least one stabilizer; from about 0.001 to about 0.1 weight % of said polypeptide; at least one bleaching agent; at least one adjunct ingredient; and/or one or more additional enzymes or enzyme derivatives selected from the group consisting of acyl transferases, alpha-amylases, beta-amylases, alpha-galactosidases, arabinosidases, aryl esterases, beta-galactosidases, carrageenases, catalases, cellobiohydrolases, celluloses, chondroitinases, cutinases, endo-beta-1, 4-glucanases, endo-beta-mannanases, esterases, exo-mannanases, galactanases, glucoamylases, hemicellulases, hyaluronidases, keratinases, laccases, lactases, ligninases, lipases, lipoxygenases, mannanases, oxidases, pectate lyases, pectin acetyl esterases, pectinases, pentosanases, peroxidases, phenoloxidases, phosphatases, phospholipases, phytases, polygalacturonases, proteases, pullulanases, reductases, rhamnogalacturonases, beta-glucanases, tannases, transglutaminases, xylan acetyl-esterases, xylanases, xyloglucanases, and xylosidases, additional metallopotease enzymes and combinations thereof. 28 - 37 . (canceled) 38 . The composition of claim 23 , wherein said composition is a granular, powder, solid, bar, liquid, tablet, gel, or paste composition. 39 - 41 . (canceled) 42 . A method of cleaning, comprising contacting a surface or an item with a cleaning composition comprising the polypeptide of claim 1 . 43 - 44 . (canceled) 45 . The method of claims 42 - 44 , wherein said item is dishware or fabric. 46 - 51 . (canceled) 52 . A method for producing the polypeptide of claim 1 comprising: a. stably transforming a host cell with an expression vector comprising a polynucleotide encoding the polypeptide of claim 1 ; b. cultivating said transformed host cell under conditions suitable for said host cell to produce said protease; and c. recovering said protease. 53 - 59 . (canceled) 60 . A nucleic acid sequence comprising a nucleic acid sequence: (i) having at least 70% identity to SEQ ID NO: 4, 10 or 15, or (ii) being capable of hybridizing to a probe derived from the polynucleotide sequence set forth in SEQ ID NO: 4, 10 or 15, under conditions of intermediate to high stringency, or (iii) being complementary to the polynucleotide sequence set forth in SEQ ID NO: 4, 10 or 15. 61 . A vector comprising the nucleic acid sequence of claim 60 . 62 . A host cell transformed with the vector of claim 61 . 63 - 64 . (canceled) 65 . A textile processing, animal feed, leather processing, feather processing, or corn soy protein processing composition comprising the polypeptide of claim 1 . 66 - 69 . (canceled)
Preparations containing enzymes {, e.g. protease or amylase} · CPC title
bacteria being Bacillus · CPC title
Metalloendopeptidases (3.4.24) · CPC title
Organic per-compounds (C11D3/3902 takes precedence) · CPC title
derived from bacteria {or Archaea} · CPC title
Related publications grouped by family.
Answers are generated from the same data shown on this page.