A Superior, High-Performance Enzyme for Breaking Borate Crosslinked Fracturing Fluids Under Extreme Well Conditions
- Bin Zhang (Verenium Corporation) | Adrienne H. Davenport (Verenium Corporation) | Lawrence Whipple (Verenium Corporation) | Hugo Urbina (Verenium Corporation) | Kenneth Barrett (Verenium Corporation) | Mark Wall (Verenium Corporation) | Richard Hutchins (Schlumberger Technology Corporation) | Andrey Mirakyan (Schlumberger Technology Corporation)
- Document ID
- Society of Petroleum Engineers
- SPE Production & Operations
- Publication Date
- April 2013
- Document Type
- Journal Paper
- 210 - 216
- 2013. Society of Petroleum Engineers
- 5.4.10 Microbial Methods, 5.8.2 Shale Gas, 2.5.2 Fracturing Materials (Fluids, Proppant), 1.8 Formation Damage
- 2 in the last 30 days
- 459 since 2007
- Show more detail
- View rights & permissions
|SPE Member Price:||USD 12.00|
|SPE Non-Member Price:||USD 35.00|
Enzyme breakers have been previously used for hydrolyzing guar gels at temperatures below 150°F. There is an industry-wide demand for enzyme breakers that can function under higher-temperature (200-250°F) and extreme pH (=10.5) conditions. To meet this demand, efforts have been made to develop an exceptionally thermostable cellulase enzyme, referred to hereafter as mannanase, that was originally discovered in a hydrothermal vent sample. This mannanase exhibits well-differentiated performance under extreme downhole conditions encountered in gas shales and deeper oil/gas wells.
This superior mannanase can effectively break linear and borate crosslinked guar under broad ranges of temperature (80°F up to at least 225°F as seen by rheology, and up to 275°F using residual activity analysis) and pH (3.0 up to 10.5). The results of rheological tests show that only a small dose is required (100 ppm or less) to achieve the complete break. The enzymatic reaction can be triggered by the changes of temperature and pH during fracturing operations. This mannanase also exhibits a dose response that allows the operator to generate a desirable viscosity/time profile by adjusting enzyme dosage. Even in the presence of fluid additives, such as buffers, salts, stabilizers, and crosslinkers, this mannanase is active for effective viscosity reduction.
This mannanase breaker belongs to the glucanase family. It reduces gel viscosity by specifically targeting ß-1,4 glycosidic bonds between the mannose units in guar. The carbohydrate-profiling tests demonstrate that this enzyme effectively and efficiently breaks the long-guar polymers into small, soluble fragments that will eliminate gel rehealing. The conductivity tests demonstrate extensive cleaving of guar and removal of polymer residues that cause formation damage and reduce fracture conductivity.
|File Size||1 MB||Number of Pages||7|
Brannon, H.D., Tjon-Joe-Pin, R.M., Carman, P.S. et al. 2003. Enzyme BreakerTechnologies: A Decade of Improved Well Stimulation. Presented at the SPEAnnual Technical Conference and Exhibition, Denver, 5-8 October. SPE-84213-MS.http://dx.doi.org/10.2118/84213-MS.
ISO 13503-1:2011, Petroleum and natural gas industries--Completion fluidsand materials--Part 1, Measurement of viscous properties of completionfluids, second edition. 2011. Geneva, Switzerland: ISO.
Kretz, K.A., Richardson, T.H., Gray, K.A. et al. 2004. Gene Site SaturationMutagenesis: A Comprehensive Mutagenesis Approach. In Methods inEnzymology, ed. E.R. Dan and P.N. Joseph, Vol. 388, 3-11. New York:Academic Press. http://dx.doi.org/10.1016/S0076-6879(04)88001-7.
Lafferty, M. and Dycaico, M.J. 2004a. GigaMatrix™: An Ultra High-ThroughputTool for Accessing Biodiversity. Journal of the Association for LaboratoryAutomation 9 (4): 200-208. http://dx.doi.org/10.1016/j.jala.2004.03.005.
Lafferty, M. and Dycaico, M.J. 2004b. GigaMatrix: A Novel UltrahighThroughput Protein Optimization and Discovery Platform. In Methods inEnzymology, ed. E.R. Dan and P.N. Joseph, Vol. 388, 119-134. New York:Academic Press. http://dx.doi.org/10.1016/S0076-6879(04)88011-X.
Mathur, E.J. and Lam, D.E. 2001. Carboxymethyl cellulase from Thermotogamaritima. US Patent No. 6,245,547, a divisional of US Patents No. 5,962,258and No. 6,008,032 (1999).
Pereira, J.H., Chen, Z., McAndrew, R.P. et al. 2010. Biochemicalcharacterization and crystal structure of endoglucanase Cel5A from thehyperthermophilic Thermotoga maritima. J. Struct. Biol. 172(3): 372-379. http://dx.doi.org/http://dx.doi.org/10.1016/j.jsb.2010.06.018.
Short, J.M. 2001. Saturation mutagenesis in directed evolution. US PatentNo. 6,171,820.
Short, J.M. 2003. Synthetic ligation reassembly in directed evolution. USPatent No. 6,537,776.
Weaver, J., Schmelzl, E., Jamieson, M. et al. 2002. New Fluid TechnologyAllows Fracturing Without Internal Breakers. Presented at the SPE GasTechnology Symposium, Calgary, 30 April-2 May. SPE-75690-MS. http://dx.doi.org/10.2118/75690-MS.
Wu, T.-H., Huang, C.-H., Ko, T.-P. et al. 2011. Diverse substraterecognition mechanism revealed by Thermotoga maritima Cel5A structures incomplex with cellotetraose, cellobiose and mannotriose. Biochimica etBiophysica Acta (BBA) - Proteins and Proteomics 1814 (12):1832-1840. http://dx.doi.org/http://dx.doi.org/10.1016/j.bbapap.2011.07.020.