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Performance Evaluation of Enzyme Breaker for Fracturing Applications under Simulated Reservoir Conditions

Fracturing fluids are being increasingly used for viscosity development and proppant transport during hydraulic fracturing operations. Furthermore, the breaker is an important additive in fracturing fluid to extensively degrade the polymer mass after fracturing operations, thereby maximizing fractur...

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Autores principales: Meng, Yuling, Zhao, Fei, Jin, Xianwei, Feng, Yun, Sun, Gangzheng, Lin, Junzhang, Jia, Baolei, Li, Piwu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8197314/
https://www.ncbi.nlm.nih.gov/pubmed/34073941
http://dx.doi.org/10.3390/molecules26113133
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author Meng, Yuling
Zhao, Fei
Jin, Xianwei
Feng, Yun
Sun, Gangzheng
Lin, Junzhang
Jia, Baolei
Li, Piwu
author_facet Meng, Yuling
Zhao, Fei
Jin, Xianwei
Feng, Yun
Sun, Gangzheng
Lin, Junzhang
Jia, Baolei
Li, Piwu
author_sort Meng, Yuling
collection PubMed
description Fracturing fluids are being increasingly used for viscosity development and proppant transport during hydraulic fracturing operations. Furthermore, the breaker is an important additive in fracturing fluid to extensively degrade the polymer mass after fracturing operations, thereby maximizing fracture conductivity and minimizing residual damaging materials. In this study, the efficacy of different enzyme breakers was examined in alkaline and medium-temperature reservoirs. The parameters considered were the effect of the breaker on shear resistance performance and sand-suspending performance of the fracturing fluid, its damage to the reservoir after gel breaking, and its gel-breaking efficiency. The experimental results verified that mannanase II is an enzyme breaker with excellent gel-breaking performance at medium temperatures and alkaline conditions. In addition, mannanase II did not adversely affect the shear resistance performance and sand-suspending performance of the fracturing fluid during hydraulic fracturing. For the same gel-breaking result, the concentration of mannanase II used was only one fifth of other enzyme breakers (e.g., mannanase I, galactosidase, and amylase). Moreover, the amount of residue and the particle size of the residues generated were also significantly lower than those of the ammonium persulfate breaker. Finally, we also examined the viscosity-reducing capability of mannanase II under a wide range of temperatures (104–158 °F) and pH values (7–8.5) to recommend its best-use concentrations under different fracturing conditions. The mannanase has potential for applications in low-permeability oilfield development and to maximize long-term productivity from unconventional oilwells.
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spelling pubmed-81973142021-06-13 Performance Evaluation of Enzyme Breaker for Fracturing Applications under Simulated Reservoir Conditions Meng, Yuling Zhao, Fei Jin, Xianwei Feng, Yun Sun, Gangzheng Lin, Junzhang Jia, Baolei Li, Piwu Molecules Article Fracturing fluids are being increasingly used for viscosity development and proppant transport during hydraulic fracturing operations. Furthermore, the breaker is an important additive in fracturing fluid to extensively degrade the polymer mass after fracturing operations, thereby maximizing fracture conductivity and minimizing residual damaging materials. In this study, the efficacy of different enzyme breakers was examined in alkaline and medium-temperature reservoirs. The parameters considered were the effect of the breaker on shear resistance performance and sand-suspending performance of the fracturing fluid, its damage to the reservoir after gel breaking, and its gel-breaking efficiency. The experimental results verified that mannanase II is an enzyme breaker with excellent gel-breaking performance at medium temperatures and alkaline conditions. In addition, mannanase II did not adversely affect the shear resistance performance and sand-suspending performance of the fracturing fluid during hydraulic fracturing. For the same gel-breaking result, the concentration of mannanase II used was only one fifth of other enzyme breakers (e.g., mannanase I, galactosidase, and amylase). Moreover, the amount of residue and the particle size of the residues generated were also significantly lower than those of the ammonium persulfate breaker. Finally, we also examined the viscosity-reducing capability of mannanase II under a wide range of temperatures (104–158 °F) and pH values (7–8.5) to recommend its best-use concentrations under different fracturing conditions. The mannanase has potential for applications in low-permeability oilfield development and to maximize long-term productivity from unconventional oilwells. MDPI 2021-05-24 /pmc/articles/PMC8197314/ /pubmed/34073941 http://dx.doi.org/10.3390/molecules26113133 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Meng, Yuling
Zhao, Fei
Jin, Xianwei
Feng, Yun
Sun, Gangzheng
Lin, Junzhang
Jia, Baolei
Li, Piwu
Performance Evaluation of Enzyme Breaker for Fracturing Applications under Simulated Reservoir Conditions
title Performance Evaluation of Enzyme Breaker for Fracturing Applications under Simulated Reservoir Conditions
title_full Performance Evaluation of Enzyme Breaker for Fracturing Applications under Simulated Reservoir Conditions
title_fullStr Performance Evaluation of Enzyme Breaker for Fracturing Applications under Simulated Reservoir Conditions
title_full_unstemmed Performance Evaluation of Enzyme Breaker for Fracturing Applications under Simulated Reservoir Conditions
title_short Performance Evaluation of Enzyme Breaker for Fracturing Applications under Simulated Reservoir Conditions
title_sort performance evaluation of enzyme breaker for fracturing applications under simulated reservoir conditions
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8197314/
https://www.ncbi.nlm.nih.gov/pubmed/34073941
http://dx.doi.org/10.3390/molecules26113133
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