Granted Patent
B2
US 12,351,532 · App. 17/459,031 · Granted Jul 8, 2025
Methods for promoting plant health using free enzymes and microorganisms that overexpress enzymes
Assignee:
Spogen Biotech Inc.
C05F17/20A01N63/50C05B15/00C05C9/00C05F11/08C05G3/60C07K14/415C12N1/20C12N9/78C12N15/8237C12N15/8249C12N15/8279C12Y302/01C12Y305/99007C12Y402/0202Y02A40/22Y02P60/21
View Patent ↗
Loading inventors, assignments & file history…
Abstract
Methods for stimulating plant growth and/or promoting plant health using free enzymes or recombinant microorganisms that overexpress enzymes are provided. Plant seeds coated with free enzymes or recombinant microorganisms that overexpress enzymes are also provided. Compositions comprising a fertilizer and an enzyme or a recombinant microorganism that overexpresses an enzyme are provided. Modified enzymes having ACC deaminase activity, recombinant microorganisms expressing the modified enzymes, plant seeds treated with the modified enzymes or recombinant microorganisms, and methods for stimulating plant growth and/or promoting plant health using the modified enzymes or recombinant microorganisms are also provided.
Claims (41)
1. A method for stimulating plant growth and/or promoting plant health comprising applying a free enzyme to a plant growth medium, a plant seed, or an area surrounding a plant or a plant seed, wherein the enzyme comprises a Triticum aestivum acid phosphatase; and
wherein the plant or a plant produced from the plant seed exhibits an increase in plant height.
2. The method of claim 1 , wherein the method further comprises applying at least a second free enzyme selected from a phospholipase, a lipase, a xylanase, a xylosidase, a lactonase, a chitosanase, a protease, a phytase, a mannanase, a pectinase, a glucanase, and an ACC deaminase.
3. The method of claim 1 , wherein the method comprises applying the enzyme to the plant growth medium.
4. The method of claim 3 , wherein the plant growth medium comprises a fertilizer.
5. The method of claim 3 , wherein the plant growth medium consists essentially of a fertilizer.
6. The method of claim 1 , wherein the method comprises applying the enzyme to the plant.
7. The method of claim 6 , wherein the method comprises applying the enzyme to roots of the plant.
8. The method of claim 1 , wherein the enzyme comprises:
a crude cell extract containing the enzyme;
a partially purified enzyme;
a substantially purified enzyme; or
an enzyme that is immobilized on a matrix or support.
9. The method of claim 1 , wherein applying the enzyme comprises an in-furrow treatment.
10. The method of claim 1 , wherein the acid phosphatase comprises an amino acid sequence having at least 80% identity to SEQ ID NO: 130 or 131.
11. The method of claim 1 , wherein the method further comprises applying a agrochemical.
12. The method of claim 1 , wherein the applying the enzyme comprises applying a liquid solution comprising the enzyme.
13. The method of claim 1 , wherein the applying the enzyme comprises applying a powder agent comprising the enzyme.
14. The method of claim 1 , wherein the applying the enzyme comprises applying a granular formulation comprising the enzyme.
15. The method of claim 1 , wherein the acid phosphatase comprises an amino acid sequence having SEQ ID NO: 130 or 131.
16. The method of claim 2 , wherein:
the phospholipase comprises an amino acid sequence having at least 80% identity to any one of SEQ ID NOs. 13-19 and 115-117;
the lipase comprises an amino acid sequence having at least 80% identity to any one of SEQ ID NOs: 20-21 and 118-120;
the mannanase comprises an amino acid sequence having at least 80% identity to SEQ ID NO: 128;
the pectinase comprises an amino acid sequence having at least 80% identity to SEQ ID NO: 129; or
the xylanase comprises an amino acid sequence having at least 80% identity to any one of SEQ ID NOs: 22-25 and 121-122.
17. The method of claim 2 , wherein the second free enzyme comprises the mannanase, and wherein the mannanase comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 128.
18. The method of claim 1 , wherein the acid phosphatase comprises a Triticum aestivum acid phosphatase.
19. The method of claim 2 , wherein the acid phosphatase and the at least second enzyme are present in synergistically effective amounts.
20. The method of claim 3 , wherein the method comprises applying the enzyme and applying a fertilizer to the plant growth medium.
21. The method of claim 20 , wherein the fertilizer comprises urea, superphosphate, a chelated micronutrient, a chelating agent, monoammonium phosphate, or diammonium phosphate.
22. The method of claim 20 , wherein the fertilizer comprises a nitrogen stabilizer, a polymer, a microbe, or a microbial extract.
23. The method of 2 , wherein the method comprises applying the enzymes to the plant growth medium.
24. The method of claim 23 , wherein the plant growth medium comprises a fertilizer.
25. The method of claim 23 , wherein the plant growth medium consists essentially of a fertilizer.
26. The method of claim 23 , wherein the method comprises applying the enzymes and applying a fertilizer to the plant growth medium.
27. The method of claim 26 , wherein the fertilizer comprises urea, superphosphate, a chelated micronutrient, a chelating agent, monoammonium phosphate, or diammonium phosphate.
28. The method of claim 26 , wherein the fertilizer comprises a nitrogen stabilizer, a polymer, a microbe, or a microbial extract.
29. The method of claim 2 , wherein the method comprises applying the enzyme to roots of the plant.
30. The method of claim 2 , wherein the acid phosphatase comprises an amino acid sequence having at least 80% identity to SEQ ID NO: 130 or 131.
31. The method of claim 2 , wherein applying the enzymes comprises applying a granular formulation comprising the enzymes.
Assignments (2)
SECURITY INTEREST
Recorded Jan 23, 2023
From: SPOGEN BIOTECH INC; ELEMENTAL ENZYMES AG AND TURF, LLC; THOMPSON, BRIAN M; THOMPSON, KATIE C
To: GENISYS CREDIT UNION
Reel/Frame 062458/0476 →
SECURITY INTEREST
Recorded Jan 23, 2023
From: SPOGEN BIOTECH INC; ELEMENTAL ENZYMES AG AND TURF, LLC; THOMPSON, BRIAN M; THOMPSON, KATIE C
To: GENISYS CREDIT UNION
Reel/Frame 062458/0544 →
Continuity (3)
Provisional Application
62309426
· Mar 16, 2016
References Cited (320)
US 5348743A
· Ryals et al.
· 1994
[cited by applicant]
US 5631007A
· Ryals et al.
· 1997
[cited by applicant]
US 5776448A
· Suslow et al.
· 1998
[cited by applicant]
US 5958104A
· Nonomura et al.
· 1999
[cited by applicant]
US 6184440B1
· Shoseyov et al.
· 2001
[cited by applicant]
US 6323023B1
· Shoseyov et al.
· 2001
[cited by applicant]
US 6333302B1
· Beer et al.
· 2001
[cited by applicant]
US 6346131B1
· Bergevin et al.
· 2002
[cited by applicant]
US 6548743B1
· Sheen et al.
· 2003
[cited by applicant]
US 6566114B1
· Kauppinen et al.
· 2003
[cited by applicant]
US 6630340B2
· Wilting et al.
· 2003
[cited by applicant]
US 7417181B2
· Wang et al.
· 2008
[cited by applicant]
US 7432097B2
· Short et al.
· 2008
[cited by applicant]
US 7504120B2
· Steer et al.
· 2009
[cited by applicant]
US 7615681B2
· Georges et al.
· 2009
[cited by applicant]
US 7919678B2
· Mironov
· 2011
[cited by applicant]
US 7960148B2
· Steer et al.
· 2011
[cited by applicant]
US 8097769B2
· Sarria-Millan et al.
· 2012
[cited by applicant]
US 9068189B2
· Mishra et al.
· 2015
[cited by applicant]
US 9068194B2
· Unkefer et al.
· 2015
[cited by applicant]
US 9125419B2
· Asolkar et al.
· 2015
[cited by applicant]
US 9132175B2
· Stewart et al.
· 2015
[cited by applicant]
US 9476058B2
· Lim
· 2016
[cited by applicant]
US 9540633B2
· Brinch-Pedersen et al.
· 2017
[cited by applicant]
US 9573980B2
· Thompson et al.
· 2017
[cited by applicant]
US 9826743B2
· Curtis et al.
· 2017
[cited by applicant]
US 9845342B2
· Thompson et al.
· 2017
[cited by applicant]
US 9850289B2
· Thompson et al.
· 2017
[cited by applicant]
US 9932275B2
· Puah et al.
· 2018
[cited by applicant]
US 20030026797A1
· Beudeker
· 2003
[cited by applicant]
US 20030167506A1
· Multani et al.
· 2003
[cited by applicant]
US 20030228679A1
· Smith et al.
· 2003
[cited by applicant]
US 20110321197A1
· Schon et al.
· 2011
[cited by applicant]
US 20120227134A1
· Schon et al.
· 2012
[cited by applicant]
US 20120259101A1
· Tan et al.
· 2012
[cited by applicant]
US 20130216653A1
· Perkins et al.
· 2013
[cited by applicant]
US 20130324493A1
· Ma et al.
· 2013
[cited by applicant]
US 20140259225A1
· Frank et al.
· 2014
[cited by applicant]
US 20150274605A1
· Waldron et al.
· 2015
[cited by applicant]
US 20160236996A1
· Chaudhry
· 2016
[cited by applicant]
US 20160340658A1
· Lessl
· 2016
[cited by examiner]
US 20170295798A1
· Curtis et al.
· 2017
[cited by applicant]
US 20170347664A1
· Thompson et al.
· 2017
[cited by applicant]
US 20230069595A1
· Curtis et al.
· 2023
[cited by applicant]
US 20230322642A1
· Thompson et al.
· 2023
[cited by applicant]
US 20240109819A1
· Thompson et al.
· 2024
[cited by applicant]
US 20240132417A1
· Thompson et al.
· 2024
[cited by applicant]
US 20240132418A1
· Thompson et al.
· 2024
[cited by applicant]
US 20240132419A1
· Thompson et al.
· 2024
[cited by applicant]
US 20240206466A1
· Thompson et al.
· 2024
[cited by applicant]
US 20240324599A1
· Thompson et al.
· 2024
[cited by applicant]
CN 101056536
· 2007
[cited by applicant]
CN 101481666
· 2011
[cited by applicant]
CN 102674960
· 2012
[cited by applicant]
CN 103086784A
· 2013
[cited by applicant]
CN 103467148
· 2013
[cited by applicant]
CN 103708907
· 2014
[cited by applicant]
CN 104388448
· 2015
[cited by applicant]
CN 104498403
· 2015
[cited by applicant]
CN 104892199
· 2015
[cited by applicant]
CN 104909884
· 2015
[cited by applicant]
CN 104909920
· 2015
[cited by applicant]
CN 104945037
· 2015
[cited by applicant]
CN 104945164A
· 2015
[cited by applicant]
CN 105085053
· 2015
[cited by applicant]
CN 105152771
· 2015
[cited by applicant]
CN 105237137
· 2016
[cited by applicant]
EP 0792363A1
· 1997
[cited by applicant]
EP 1359134A1
· 2003
[cited by applicant]
EP 0901527B1
· 2005
[cited by applicant]
EP 1590466B1
· 2010
[cited by applicant]
EP 2276835B1
· 2011
[cited by applicant]
EP 2357242
· 2011
[cited by applicant]
EP 2561760A2
· 2013
[cited by applicant]
EP 2069504B1
· 2015
[cited by applicant]
EP 2658961B1
· 2015
[cited by applicant]
JP 253870A
· 2000
[cited by applicant]
KR 20030015943
· 2003
[cited by applicant]
RU 2160778C1
· 2000
[cited by applicant]
RU 2503721C2
· 2009
[cited by applicant]
RU 2529949C2
· 2009
[cited by applicant]
RU 2012129907A
· 2011
[cited by applicant]
RU 2439148C1
· 2012
[cited by applicant]
WO 0200232A2
· 2002
[cited by applicant]
WO 03066846A1
· 2003
[cited by applicant]
WO 2005028654A1
· 2005
[cited by applicant]
WO 2006012366A2
· 2006
[cited by applicant]
WO 2007078127A1
· 2007
[cited by applicant]
WO WO2007086898A2
· 2007
[cited by applicant]
WO 2008017483A2
· 2008
[cited by applicant]
WO 2008100112
· 2008
[cited by applicant]
WO 2009037329A2
· 2009
[cited by applicant]
WO 2010046221A1
· 2010
[cited by applicant]
WO 2011106794A1
· 2011
[cited by applicant]
WO 2011158203
· 2011
[cited by applicant]
WO 2013102934A1
· 2013
[cited by applicant]
WO 2013116700
· 2013
[cited by applicant]
WO 2014004487A1
· 2014
[cited by applicant]
WO 2014145964A1
· 2014
[cited by applicant]
WO 2015118516A1
· 2015
[cited by applicant]
WO 2016044661A1
· 2016
[cited by applicant]
WO 2016029646
· 2016
[cited by applicant]
WO 2016044529
· 2016
[cited by applicant]
WO 2016044533A1
· 2016
[cited by applicant]
WO 2016044542A1
· 2016
[cited by applicant]
WO 2016044548
· 2016
[cited by applicant]
WO 2016044563A1
· 2016
[cited by applicant]
WO 2016044575
· 2016
[cited by applicant]
WO 2019060574A1
· 2019
[cited by applicant]
U.S. Appl. No. 17/932,994, filed Sep. 16, 2022, Thompson et al.
[cited by applicant]
U.S. Appl. No. 18/302,458, filed Apr. 18, 2023, Thompson, et al.
[cited by applicant]
GenBank Accession No. P33378, dated Feb. 22, 2023.
[cited by applicant]
Singh et al., Protein Engineering Approaches in the Post-Genomic Era, Current Protein and Peptide Science 18:1-11, 2017.
[cited by applicant]
Zhang et al., Propagated Perturbations from a Peripheral Mutation Show Interaction Supporting WW Domain Thermostability, Structure 26:1474-1485, 2018.
[cited by applicant]
S. Shah, et al., “Isolation and Characterization of ACC Deaminase Genes From Two Different Plant Growth-Promoting Rhizobacteria” Canadian Journal of Microbiology (1998) vol. 44, pp. 833-843.
[cited by applicant]
Vasil et al. Herbicide Resistant Fertile Transgenic Wheat Plants Obtained by Microprojectile Bombardment of Regenerable Embryogenic Callus Bio/Technology vol. 10, pp. 667-674 (1992).
[cited by applicant]
UniProt\KB Accession No. C4PKL1, Purple acid phosphatase, Jul. 7, 2009.
[cited by applicant]
Murashige, T. and Skoog, F. (1962) A Revised Medium for Rapid Growth and Bioassays with Tobacco Tissue Cultures, Physiologia Plantarum 15, 473-497.
[cited by applicant]
Siddikee, Md. A., et al. , “Regulation of Ethylene Biosynthesis Under Salt Stress in Red Pepper (
[cited by applicant]
Brandt Steric P DS Water Soluble Fertilizer Product Description, Brandt Consolidated, Inc., Springfield, IL, May 2013.
[cited by applicant]
UniProtKB Accession No. P23903, Glucan endo-1,3-beta-glucosidase A1, Nov. 1, 1991.
[cited by applicant]
UniProtKB Accession No. O52864, Phosphatidyl-degrading phospholipase C, Jun. 1, 1998.
[cited by applicant]
Takekawa, et al. “Proteases involved in generation of beta- and alpha-amylases from a large amylase precursor in Bacillus polymyxa”, Journal of Bacteriology 173 (21), 6820-6825, (1991).
[cited by applicant]
Shahid, M., et la., “Root Colonization and Growth Promotion of Sunflower (
[cited by applicant]
Shani, Z., et al., “Expression of Endo-1,4-B-Gllucanase (cel1) in
[cited by applicant]
Shankar, M., et al., “Root Colonization of a Rice Growt Promoting Strain of Enterobacter cloacae,” Journal of Basic Microbiology, 2011, pp. 523-530, vol. 51, No. 5.
[cited by applicant]
Shao, J., et al., “Contribution of Indole-3-acetic Acid in the Plant Growth Promotion b the Rhizospheric Strain Bacillus amyloliquefaciens SQR9,” Biology and Fertility of Soils, Apr. 2015, pp. 321-330, vol. 51, Issue 3.
[cited by applicant]
Shen, M., et al., “Effect of Plant Growth-Promoting Rhizobacteria (PGPRs) on Plant Growth, Yield, and Quality of Tomato (
[cited by applicant]
Siddikee, Md., A., et al., “Halotolerant Bacteria with ACC Deaminase Activity Alleviate Salt Stress Effect in Canola Seed Germination,” Journal of the Korean Society for Applied Biological Chemistry, Apr. 2015, pp. 237-…
[cited by applicant]
Singh, B., et al., “Microbial Phytases in Phosphorus Acquisition and Plant Growth Promotion,” Physiology and Molecular Biology of Plants, Apr.-Jun. 2011, pp. 93-103, vol. 17, Issue 2.
[cited by applicant]
Singh, B., et la., “Plant Growth Promotion by an Extracellular HAP-Phytase of A Thermophilic Mold Sporotrichum thermophile,” Applied Biochemistry and Biotechnology, Mar. 2010, pp. 1267-1276, vol. 160, Issue 5.
[cited by applicant]
Smirnova, I., et al., “The Effect of Inoculaton by Cellulolytic Bacteria Bacillus cytaseus on Wheat Productivity,” Plant Growth-Promoting Rhizobacteria (PGPR) for Substainable Agriculture, Proceedings of the 2nd Asian P…
[cited by applicant]
Stearns, J. C., et la., “Effects of Bacterial ACC Deamnase on
[cited by applicant]
Trivedi, P., et al., “Plant Growth Promotion Abilities and Formulation of Bacillus megaterium Strain B 388 (MTCC6521) Isolated from a Temperate Himalayan Location,” Indian Journal of Microbiology, 2008, pp. 342-347, vol…
[cited by applicant]
Vendan, R. T., et al., “Diversity of Endophytic Bacteria in Ginseng and Their Potential for Plant Growth Promotion,” The Journal of Microbiology, 2010, pp. 559-565, vol. 48, Issue 5.
[cited by applicant]
Wang, X., et al., “PLD: Phospholipase Ds in Plant Signaling,” Phospholipases in Plant Signaling, 2013, pp. 3-26.
[cited by applicant]
Written Opinion issued for PCT/US2017/022662 dated Jun. 5, 2017, 6 pages.
[cited by applicant]
Yadav, S., et al., “Diversityand Phylogeny of Plant Growth-Promoting Bacilli from Moderately Acidic Soil,” Journal of Basic Microbiology, Feb. 2011, pp. 98-106, vol. 51, Issue 1.
[cited by applicant]
Zeigler, D. R., “Bacillus Thuringiensis Bacillus Cereus,” Bacillus Genetic Stock Center Catalog of Strains, 1999, Seventh Edition, vol. 2, 58 pages.
[cited by applicant]
Fan, L., et al., “Antisense Suppression of Phospholipase D(alpha) Retards Abscisic Acid- and Ethylene-Promoted Senescence of Postharvest
[cited by applicant]
Glass, M., et la., “Endo-(beta)-1,4-Glucanases Impact Plant Cell Wall Development by Influencing Cellulose Crystallizaiton,” Journal of Integrative Plant Biology, Apr. 2015, pp. 396-410, vol. 57, Issue 4.
[cited by applicant]
Hong, Y., et al., “Phospholipase D(alpha)3 is Involved in the Hyperormotic Response in
[cited by applicant]
Li, M., et al., Overexpression of Patatin-Related Phospholipase AIII(delta) Altered Plant Growth and Increased Seed Oil Content in Camelina, Plant Biotechnology Journal, 2015, pp. 766-778, vol. 13.
[cited by applicant]
Shani, Z, et al., “Growth Enhancement of Transgenic Poplar Plants by Overexpression of
[cited by applicant]
Sadowski, M. I., et al., “The Sequence-Structure Relationship and Protein Function Prediction,” Current Opinion in Structural Biology, 2009, pp. 357-362, vol. 19, No. 3.
[cited by applicant]
Seffernick, J. L., et al., “Melamine Deaminase and Afrazine Chlorohydrolase: 98 Percent Identical but Functionally Different,” Journal of Bacteriology, Apr. 2001, pp. 2405-2410, vol. 183, No. 8.
[cited by applicant]
Sloma, A., et al., “Cloning and Characterization of the Gene for an Additional Extracellular Serine Protease of Bacillus subtilis,” Journal of Bacteriology, Nov. 1991, pp. 6889-6895, vol. 173, No. 21.
[cited by applicant]
Tang, S., et al., “Identification of Dehalobacter Reductive Dehalogenases that Catalyse Dechlorination of Chloroform, 1,1,1-Trichlorethane and 1,1-Dichlorethane,” Phil.
[cited by applicant]
Thallinger, B., et al., “Antimicrobial Enzymes: An Emerging Strategy to Fight Microbes and Microbial Biofilms,” Biotechnology Journal, 2013, pp. 97-109, vol. 8, No. 1.
[cited by applicant]
Valbuzzi, A., et al., “A Novel Member of the Subtilsin-like Protease Family from Bacillus subtilis,” Microbiology, 1999, pp. 3121-3127, vol. 145, Par 11.
[cited by applicant]
Bewley, J. D., “Breaking Down the Walls—A Role for Endo-beta-mannanase in Release from Seed Dormancy?,” Trends in Plant Science, Dec. 1997, pp. S1360-S1365, vol. 2, No. 12.
[cited by applicant]
Leviatov, S., et al., “Involvement of Endomannanase in the Control of Tomato Seed Germination Under Low Temperature Conditions,” Annals of Botany, 1995, pp. 1-6, vol. 76.
[cited by applicant]
Partial Supplementary European Search Report issued for EP17767505.5 dated Feb. 26, 2020, 5 pages.
[cited by applicant]
Rodriguez-Gacio, M. C., et al., “Softening-up Mannan-rich Cell Walls,” Journal of Experimental Botany, 2012, pp. 3975-3988, vol. 63, No. 11.
[cited by applicant]
Yang, P., et al., “A Novel Beta-Mannanase with High Specific Activity from Bacillus circulans CGMCC1554: Gene Cloning, Expression and Enzymatic Characterization,” Applied Biochemistry and Biotechnology, 2009, pp. 85-94,…
[cited by applicant]
Akinrinlola, et al., “Evaluation of Bacillus Strains for Plant Growth Promotion and Predictability of Efficacy b In Vitro Physiological Traits,” Intl. Journal of Microbiology, vol. 2008, Article ID 5686874, 11 pages.
[cited by applicant]
Benfield, et al., “Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Proteiins Variants” (2007), vol. 460, No. 1, pp. 41-47.
[cited by applicant]
Cheng, “Purification and Characterization of a Thermostable Beta-Mannanase from Bacilllus Subtilis BE-91: Potential Application in Inflammatory Diseases” BioMed Research International (2016) vol. 2016, Article ID 638014…
[cited by applicant]
UniProtKB Accession No. W7KRH1, Intracellular Serine-Protease, Apr. 16, 2014, 2 pages.
[cited by applicant]
UniProtKB Accession No. A0A380XNG8, Intracellular Serine Protease, Nov. 7, 2018, 1 page.
[cited by applicant]
Di Benedetto, et al., “Isolation, Screening, and Characterization of Plant-Growth-Promoting Bacteria from Durum Wheat Rhizosphere to Improve N and P Nutrient Use Efficiency,” Microorganisms (2019) vol. 7, No. 541, pp. 1…
[cited by applicant]
Dowd and Gilrow, “The Emerging Roles of Phospholipase C in Plant Growth and Development,” Plant Cell Monographs (2009) vol. 16, pp. 23-27.
[cited by applicant]
Dunne, C., et al., “Overproduction of an Inducible Extracellular Serine Protease Improves Biological Control of Pythium ultimum by Stenotrophomonas maltophilia Strain W81,” Microbiology, (2000) vol. 146, Part 8 pp. 2069…
[cited by applicant]
Emi, et al., “Crystllization and Some Properties of Mannanase” Agricultural and Biological Chemistry (1972) vol. 36, No. 6, pp. 991-1001.
[cited by applicant]
Geng et al., “A Novel Serine Protease, Sep1 from Bacillus Firmus DS-1 Has Nematicidal Activityand Degrades Multiple Intestinal-Associated Nematode Proteins,” Scientific Reports, (2016) vol. 6, pp. 1-12.
[cited by applicant]
Khan, N., et al., “Antifungal Activity of
[cited by applicant]
Li, et al., “Structure Prediction and Enzymatic Properties of Phytase PhyS,” Advances in Enzyme Research (2019) vol. 7, pp. 57-65.
[cited by applicant]
Quan, et al., “Purification and Properties of a Phytase from Candida Krusei WZ-001,” Journal of Bioscience (2002) vol. 94, No. 5, pp. 419-425.
[cited by applicant]
Quecine, et al., “Sugarcane Growth Promotion by the Endoophytic Bacterium Pantoea Agglomerans 33.1,” Applied and Environmental Microbiology (2012) vol. 78, No. 21, pp. 7511-7518.
[cited by applicant]
Raddadi, et al., “Screening of Plant Growth Promoting Traits of Bacillus Thuringiensis” Annals of Microbiology (2008) vol. 58, No. 1, pp. 47-52.
[cited by applicant]
Van Pouderoyen, et al., “Structural Insights Into the Processivity of Endopolygalacturonase I form Aspergillus niger,” FEBS Letters (2003) vol. 554, No. 3, pp. 462-466.
[cited by applicant]
Yen, Y. H., et al., “An Antifungal Protease Produced byPseudomonas aeruginosa M-1001 with Shrimp and Crab Shell Powder as a Carbon Source,” Enzyme and Microbial Technology (2006) vol. 39, pp. 311-317.
[cited by applicant]
K. Jetiyanon, et al., “Film Coating of Seeds with Bacillus Cereus RS87 Spores for Early Plant Growth Enhancement,” Canadian Journal of Microbiology (2008) vol. 54, pp. 861-867.
[cited by applicant]
Bailey-Smith et al., The ExsA protein of Bacillus cereus is required for assembly of coat and exosporium onto the spore surface, J Bacteriol. 187(11): 3800-3806, 2005.
[cited by applicant]
Boydston et al., The ExsY protein is required for complete formation of the exosporium of Bacillus anthracis, J Bacteriol. 188(21): 7440-7448, 2006.
[cited by applicant]
Crane et al., Bacterial Nitric Oxide Synthases, Annual Review in Biochemistry 79:445-470, 2010.
[cited by applicant]
Thompson, Amino-Terminal Sequences of the Bacillus anthracis Exosporium Proteins BclA and BclB Important for Localization and Attachment to the Spore Surface, A Thesis presented to the Faculty of the Graduate School at …
[cited by applicant]
Thompson et al, Assembly of the BclB Glycoprotein into the Exosporium and Evidence for its role in the Formation of Exosporium “cap” Structure in Bacillus anthracis, Molecular Microbiology 86(5): 1073-1084, 2012.
[cited by applicant]
U.S. Appl. No. 17/459,019, filed Aug. 27, 2021, Thompson et al.
[cited by applicant]
U.S. Appl. No. 17/852,607, filed Jun. 29, 2022, Curtis, et al.
[cited by applicant]
Thompson and Stewart, Targeting of the BclA and BclB proteins to the
[cited by applicant]
Ahemad, M., et al., “Mechanisms and Applications of Plant Growth Promoting Rhizobacteria: Current Perspective,” Journal of King Saud University—Science, 2014, pp. 1-20, vol. 26.
[cited by applicant]
Bae, C., et al., “Multiple Classes of Immune-Related Proteases Associated with the Cell Death Response in Pepper Plants,” PLoS One, May 2013, pp. 1-11, vol. 8, Issue 5, e63533.
[cited by applicant]
Berlemont, R., et al., “Phylogenetic Distribution of Potential Cellulases in Bacteria,” Applied and Environmental Microbiology, Mar. 2013, pp. 1545-1554, vol. 79, No. 5.
[cited by applicant]
Chakraborty, U., et al., “Plant Growth Promotion and Induction of Resistance in Camellia sinesis by Bacillus megaterium,” Journal of Basic Microbiology, 2006, pp. 186-195, vol. 46, No. 3.
[cited by applicant]
Chapman, K. D., “Phospholipase Activity During Plant Growth and Development and in Response to Environmental stress,” Trends in Plant Science, Nov. 1998, pp. 419-426, vol. 3, No. 11.
[cited by applicant]
Choudhart, D. K., et al., “Interactions of
[cited by applicant]
Corbineau, F., et al., “Improvement of Germination of Terminalia Ivorensis Seeds,” Forest Genetic Resources Information No. 21, http://www.fao.org/docrep/006/v3030e/V3030E10.htm, 7 pages.
[cited by applicant]
De Freitas, J. R., et al., “Phosphate-Solubilizing Rhizobacteria Enhance the Growth and Yield but not Phosphorus Uptake of Canola (
[cited by applicant]
Dong, Y. H., et al., “Identification of Quorum-Quenching N-Acyll Homoserine Lactonases from
[cited by applicant]
Dourado, M. N., et al., “Biotechnological and Agronomic Potential of Endophytic Pink-Pigmented Methylotrophic
[cited by applicant]
Dowd, P. E., et al., “The Emerging Roles of Phospholipase C in Plant Growth and Development,” Lipid Signaling in Plants, Plant Cell Monographs 16, 2010, pp. 23-37.
[cited by applicant]
Faria, D. C., et al., “Endophytic Bacteria Isolated From Orchid and Their Potential to Promote Plant Growth,” World Journal of Microbiology and Biotechnology, Feb. 2013, pp. 217-221, vol. 29, Issue 2.
[cited by applicant]
Gamalero, E., et al., “Bacterial Modulation of Plant Ethylene Levels,” Plant Physiology, Sep. 2015, pp. 13-22, vol. 169.
[cited by applicant]
Glick, B. R., “Modulation of Plant Ethylene Levels by the Bacterial Enzyme ACC Deaminase,” FEMS Microbiology Letters, 2005, pp. 1-7, vol. 251.
[cited by applicant]
Gnanaraj, M., et al., “Isolation and Gene Expression Analysis of Phospholipase C in Response to Abiotic Stresses from
[cited by applicant]
Goldberg, L. J., et al., “A Bacterial Spore Demonstrating Rapid Larvicidal Activity Against Anopheles Sergentii, Uranotaenia Unguiculata, Culex Univitattus, Aedes Aegypti and Culex Pipiens,” Mosquito News, Sep. 1977, pp…
[cited by applicant]
Guerchicoff, A., et al., “Identification and Characterization of a Previously Undescribed cyt Gene in
[cited by applicant]
Gujar, P. D .. , et al., “Effect of Phytase from Aspergillus niger on Plant Growth and Mineral Assimilation in Wheat (
[cited by applicant]
Hafeez, F. Y., et al., “PGPR: Versatile Tool to Combat Soil Borne Pathogens and Improve Plant Health,” Aspects of Applied Biology, Crop Protection in Southern Britain, 2011, pp. 241-245, vol. 106.
[cited by applicant]
Han, W., et al., “The Application of Exogenous Cellulase to Improve Soil Fertility and Plant GrowthDue to Acceleration of Straw Decomposition,” Bioresource Technology, 2010, pp. 3724-3731, vol. 101.
[cited by applicant]
Hartati, S., et al., “Overexpression of Poplar Cellulase Accelerates Growth and Disturbs the Closing Movements of Leaves in Sengon,” Plant Physiology, Jun. 2008, pp. 552-561, vol. 147.
[cited by applicant]
Hong, Y., et al., “Phospholipases in Plant Response to Nitrogen and Phosphorus Availability,” Phospholipases in Plant Signaling, Signaling and Communication in Plants, 2014, pp. 159-180, vol. 20, Springer, Berlin, Heide…
[cited by applicant]
Hontzeas, N., et al., “Changes in Gene Expression in Canola Roots Induced by ACC-Deaminase-Containing Plant-Growth-Promotoing Bacteria,” Molecular Plant-Microbe Interactions, Aug. 2004, pp. 865-871, vol. 17, No. 8.
[cited by applicant]
Howard, G., et al., “Effects of Cellulolytic Ruminol Bacteria and of Cell Extracts on Germination of
[cited by applicant]
Idriss, E. E., et al., “Extracellular Phytase Activity of Bacillus amyloliquefaciens FZB45 Contributes to its Plant-Growth-Promoting Effect,” Microbiology, 2002, pp. 2097-2109, vol. 148.
[cited by applicant]
International Search Report issued for PCT/US2017/022662 dated Jun. 5, 2017, 5 pages.
[cited by applicant]
Islam, M. R, et al., “Characterization of Plant Growth-Promoting Traits of Free-Living Diazotrophic Bacteria and Their Inoculation Effects on Growth and Nitrogen Uptake of Crop Plants,” Journal of Microbiology and Biote…
[cited by applicant]
Jackson, W. T., “Effect of Pectinase and Cellulase Preparations on the Growth and Development of Root Hairs,” Physiologia Plantarum, 1959, pp. 502-510, vol. 12.
[cited by applicant]
Jeong, H., et al., “Draft Genome Sequence of the Paenibacillus polymyxa Type Strain (ATCC 842T), A Plant Growth-Promoting Bacterium,” Journal of Bacteriologoy, 2011, pp. 5026-5027, vol. 193, No. 18.
[cited by applicant]
Kim, J. F., et al., “Genome Sequence of the Polymyxim-Producing Plant-Probiotic Rhizobacterium Paenibacillus polymyxa E681,” Journal of Bacteriology, 2010, pp. 6103-6104, vol. 192, No. 22.
[cited by applicant]
Kong, Z., et al., “Effects of 1-aminocyclopropane-1-carboxylate (ACC) Deaminase-Overproducing Sinorhizobium meliloti on Plant Growth and Copper Tolerance of Medicago lupulina,” Plant and Soil, Jun. 2015, pp. 383-398, vo…
[cited by applicant]
Leite, H. A., et al., “Bacillus subtilis and Enterobacter cloacae endophytes from healthy
[cited by applicant]
Li, J., et al., “An ACC Deaminase Minus Mutant of Enterobacter cloacae UW4 No Longer Promotes Root Elongation,” Current Microbiology, Aug. 2000, pp. 101-105, vol. 41, No. 2.
[cited by applicant]
Li, W., et al., “Cloning of the Thermostable Cellulose Gene from the Newly Isolated Bacillus subtillus and its Expression in
[cited by applicant]
Li, Z, et al., “A Colorimetric Assay of 1-aminocyclopropane-1-carboxylate (ACC) Based on Ninhydrin Reaction for Rapid Screening of Bacteria Containing ACC Deaminase,” Letters in Applied Microbiology, 2011, pp. 178-185, …
[cited by applicant]
Lin, Z, et al., “Recent Advances in Ethylene Research,” Journal of Experimental Botany, 2009, pp. 3311-3336, vol. 60, Issue 12.
[cited by applicant]
Liu, J. L., et al., “Effects of Two Plant Growth-Promotoing Rhizobacteria Containing 1-aminocyclopropane-1-carboxylate Deaminase on Oat Growth in Petroleum-Contaminated Soil,” Internaitonal Journal of Environmental Scie…
[cited by applicant]
Liu, W. et al., “THIS1 is a Putative Lipase that Regulates Tillering, Plant Height, and Spikelet Fertility in Rice,” Journal of Experimental Botany, 2013, pp. 1-14, vol. 64, No. 14.
[cited by applicant]
Medie< F., et al., “Genome Analysis Highlight the Different Biological Roles of Cellulases,” Nature Reviews, Microbiology, Mar. 2012, pp. 227-234, vol. 10.
[cited by applicant]
Meldau, D. G., et al., “A Native Plant Growth Promoting Bacterium,
[cited by applicant]
Mercado, J. A., et al., “Expression of the B-1,3-Glucanase Gene bgn13.1 From Trichoderma harzianum in Strawberry Increases Tolerance to Crown Rot Diseases but Interferes with Plant Growth,” Transgenic Research, 2015, 11…
[cited by applicant]
Ngamau, C., “Endophytic bacterial associated with bananas (
[cited by applicant]
Oh, T. K., et al., “Expression of Aspergillus nidulans phy Gene in Nicotiana benthamiana Produces Active Phytase with Broad Specificities,” International Journal of Molecular Sciences, 2014, p. 15571-15591, vol. 15, No.…
[cited by applicant]
Penrose, D. M., et al., “Levels of ACC and Related Compounds in Exudate and Extracts of Canola Seeds Treated with ACC Deaminase-Containing Plant Growth-Promoting Bacteria,” Canadian Journal of Microbiology, Apr. 2001, p…
[cited by applicant]
Phitsuwan, P., et al., “Present and Potential Applications of Cellulases in Agriculture, Biotechnology, and Bioenergy,” Folia Microbiology, 2013, pp. 163-176, vol. 58.
[cited by applicant]
Pilar-Izquierdo, M. D., et al., “Barley Seed Coating with Free and Immobilized Alkaline Phosphatase to Improve P Uptake and Plant Growth,” Crops and Soils Research Paper, Journal of Agricultural Science, 2012, pp. 691-7…
[cited by applicant]
Ping, R., et al., “Effect of Cellulase on Germination of
[cited by applicant]
Reetha, S., et al., “Screening of Cellulase and Pectinase by Using Pseudomonas fluorescence and Bacillus subtilis,” International Letters of Natural Sciences, 2014, pp. 75-80, vol. 8, No. 2.
[cited by applicant]
Saleh, S., et al., “Involvement of gacS and rpoS in Enhancement of the Plant Growth-Promoting Capabilities of Enterobacter cloacae CAL2 and UW4,” Canadian Journal of Microbiology, Aug. 2001, pp. 698-705, vol. 47, No. 8.
[cited by applicant]
Sales, J., et al., “
[cited by applicant]
Aakre, et al. Inhibition of Bacillus cereus phospholipase C by univalent anions. The Biochemical Journal 203, 799-801, (1982).
[cited by applicant]
Goldfine, et al. “Nonspecific phospholipase C of Listeria monocytogenes: activity on phospholipids in Triton X-100- mixed micelles and in biological membranes”. J Bacteriol 175, 4298-4306, (1993).
[cited by applicant]
Huang, et al. “Recombinant broad-range phospholipase C from Listeria monocytogenes exhibits optimal activity at acidic pH”. Biochimica et Biophysica Acta (BBA)—Proteins and Proteomics 1864(6), 697-705, (2016).
[cited by applicant]
Monturiol-Gross, et al. “Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase”. FEBS Open Bio, vol. 11(12), pp. 3262-3275, (2021).
[cited by applicant]
Otnaess. “The hydrolysis of sphingomyelin by phospholipase C from Bacillus cereus”. FEBS Letters 114, 202-204, (1980).
[cited by applicant]
Pomerantsev, et al. “Phosphatidylcholine-specific phospholipase C and sphingomyelinase activities in bacteria of the Bacillus cereus group”. Infect Immun. (2003); 71(11): 6591-606.
[cited by applicant]
Tan, et al. “Cloning, overexpression, refolding, and purification of the nonspecific phospholipase C from Bacillus cereus”. Protein Expr Purif 10, 365-372, (1997).
[cited by applicant]
Zuckert, et al. “Modulation of enzymatic activity and biological function of Listeria monocytogenes broad-range phospholipase C by amino acid substitutions and by replacement with the Bacillus cereus ortholog”. Infect I…
[cited by applicant]
Saile et al., Bacillus anthracis multiplication, persistence, and genetic exchange in the rhizosphere of grass plants, Appl. Environ. Microbiol., 72(5):3168-3174, 2006.
[cited by applicant]
U.S. Appl. No. 18/461,008, filed Sep. 5, 2023, Curtis, et al.
[cited by applicant]
U.S. Appl. No. 18/476,256, filed Sep. 27, 2023, Thompson, et al.
[cited by applicant]
U.S. Appl. No. 18/476,259, filed Sep. 27, 2023, Thompson, et al.
[cited by applicant]
U.S. Appl. No. 18/476,264, filed Sep. 27, 2023, Thompson, et al.
[cited by applicant]
U.S. Appl. No. 18/476,270, filed Sep. 27, 2023, Thompson, et al.
[cited by applicant]
Giorno, et al. “Morphogenesis of the
[cited by applicant]
U.S. Appl. No. 18/392,771, filed Dec. 21, 2023, Thompson, et al.
[cited by applicant]
U.S. Appl. No. 18/398,650, filed Dec. 28, 2023, Thompson, et al.
[cited by applicant]
Vikram, et al., “Production of Plant Growth Promoting Substances by Phosphate Solubilizing Bacteria isolated from vertisols.” Journal of Plant Sciences, vol. 2, No. 3, pp. 326-333 ref. 30, (2007).
[cited by applicant]
Han, W. et al., “Short-term effects of exogenous protease application on soil fertility”, European Journal of Soil Biology, 46, pp. 144-150, Feb. 2, 2010 (Feb. 2, 2010).
[cited by applicant]
Molla, A. et al., “Trichoderma-Enriched Biofertilizer Enhances Production and Nutritional Quality of Tomato (
[cited by applicant]
Extended European Search Report issued in EP Application No. 24152365.3, dated Oct. 11, 2024.
[cited by applicant]
Simontacchi, M., et al., “Enzymatic Sources of Nitric Oxide during Seed Germination.” In: Lamattina, L., Polacco, J.C. (eds) Nitric Oxide in Plant Growth, Development and Stress Physiology. Plant Cell Monographs, vol. 5…
[cited by applicant]
Zheng, et al., “Exogenous nitric oxide improves seed germination in wheat against mitochondrial oxidative damage induced by high salinity”, Environmental and Experimental Botany, vol. 67, Issue 1. pp. 222-227; (2009).
[cited by applicant]
U.S. Appl. No. 18/680,688, filed May 31, 2024, Thompson, et al.
[cited by applicant]
Matos. Invitation to Pay Additional Search Fees. PCT/US24/21327, mailed May 31, 2024.
[cited by applicant]
U.S. Appl. No. 18/615,771, filed Mar. 25, 2024, Thompson et al.
[cited by applicant]
Wang, et al. “Two distinct manganese-containing superoxide dismutase genes in
[cited by applicant]
Inaoka, et al. “SodA and manganese are essential for resistance to oxidative stress in growing and sporulating cells of
[cited by applicant]
Rasko, et al., UniProt Accession No. Q738B1—“DUF4183 domain-containing protein”—
[cited by applicant]
U.S. Appl. No. 18/944,720, filed Nov. 12, 2024, Thompson, et al.
[cited by applicant]
Liu, L. et al., “How to achieve high-level expression of microbial enzymes”, Bioengineered, 4:4, pp. 212-223, Apr. 25, 2013.
[cited by applicant]
Shaharoona et al. Effect of plant growth promoting rhizobacteria containing ACC-deaminase on maize (
[cited by applicant]
Dennis, Kinetic dependence of phospholipase A2 activity on the detergent Triton-X100, Journal of Lipid Research 14(2):152-159, 1973.
[cited by applicant]
De La Cruz et al., Purification and characterization of an endo-beta-1,6-glucanase from Trichoderma harzianum that is related to its mycoparasitism, J. Bacteriol. 177(7):1864-71, 1995.
[cited by applicant]
Hontzeas et al., Expression and characterization of 1-aminocyclopropane-1-carboxylate deaminase from the rhizobacterium Pseudomonas putida UW4: a key enzyme in bacterial plant growth promotion, Biochimica et Biophysica …
[cited by applicant]
Gelb et al., Cloning and recombinant expression of a structurally novel human secreted phospholipase A2, Journal of Biological Chemistry 275(51):39823-39826, 2000.
[cited by applicant]
Gellatly et al., Purification and characterization of a potato tuber acid phosphatase having significant phosphotyrosine phosphatase activity, Plant Physiology 106(1):223-232, 1994.
[cited by applicant]
Kashyap et al., Production, purification, and characterization of pectinase from a
[cited by applicant]
Slein & Logan Jr, Partial purification and properties of two phospholipases of Bacillus cereus, J. Bacteriol. 85(2):369-81, 1963.
[cited by applicant]
Office Action regarding Australian App. No. 2023226721, dated Jan. 30, 2025.
[cited by applicant]
Office Action regarding Australian App. No. 2023226725, dated Feb. 4, 2025.
[cited by applicant]
Office Action regarding Australian App. No. 2023226733, dated Jan. 30, 2025.
[cited by applicant]
Office Action regarding Australian App. No. 2023226740, dated Feb. 4, 2025.
[cited by applicant]
Office Action regarding Australian App. No. 2023226742, dated Feb. 4, 2025.
[cited by applicant]
Office Action regarding Australian App. No. 2023226743, dated Feb. 4, 2025.
[cited by applicant]
Office Action regarding Australian App. No. 2023226745, dated Feb. 5, 2025.
[cited by applicant]
Office Action regarding Australian App. No. 2023226746, dated Feb. 4, 2025.
[cited by applicant]
Sabaratnam, et al. “Mechanism of antagonism by
[cited by applicant]
Office Action regarding Australian App. No. 2023226740, dated Apr. 3, 2025.
[cited by applicant]
Office Action regarding Australian App. No. 2023226742, dated Apr. 3, 2025.
[cited by applicant]
Office Action regarding Australian App. No. 2023226745, dated Apr. 3, 2025.
[cited by applicant]
Office Action regarding Australian App. No. 2023226746, dated Apr. 7, 2025.
[cited by applicant]
Office Action regarding Australian App. No. 2023226721, dated Apr. 8, 2025.
[cited by applicant]
Cited By (1)