Removal of polymeric filter cake in petroleum wells: A study of commercial amylase stability
The drilling fluid contact with the productive zone of drilling wells, with horizontal or complex configurations, can reduce its productivity by fluid invasion in the borehole wall. Drilling fluids usually comprise natural polymers as starch and xanthan gum. These polymers are deposited as a filter...
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Published in: | Journal of petroleum science & engineering Vol. 59; no. 3; pp. 263 - 270 |
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01-11-2007
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Abstract | The drilling fluid contact with the productive zone of drilling wells, with horizontal or complex configurations, can reduce its productivity by fluid invasion in the borehole wall. Drilling fluids usually comprise natural polymers as starch and xanthan gum. These polymers are deposited as a filter cake on the wellbore wall. A common approach to remove this filter cake is the application of acids or strong oxidative solutions. However, these are non-specific species and a possible alternative lies in enzymatic preparations that are able to hydrolyze such polymers. The enzymes catalyze specific substrates, are environmentally friendly and the enzymatic degradation rate is slower than that achieved by the oxidative species, permitting to produce uniform degradation of the filter cake. Openhole operations require thermo and pressure stability of these enzymatic products. The results herein reported deals with the technical viability analysis of a commercial α-amylase as a new catalyst for filter cake removal. The effects of process parameters, like temperature (65, 80 and 95 °C), enzyme concentration (1, 5.5 and 10% v/v), calcium concentration (5, 70 and 135 ppm), and pressure (100, 500, 100 and 6000 psi), on amylase stability under openhole operations were investigated. Temperature demonstrated to be the most important parameter for the enzyme stability. The enzyme thermostability behavior in high salt (NaCl) concentration (completion fluid) was not significantly different from the control solution in distillated water. The pressure effect on enzyme stability did not affect the enzyme stability as temperature. Hydrostatic pressure (6000 psi) did not impact the amylolytic activity in brine solution. Combined pressure–temperature assays showed that temperature is the key factor in enzyme stability for application in polymeric filter cake removal in petroleum wells. |
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AbstractList | The drilling fluid contact with the productive zone of drilling wells, with horizontal or complex configurations, can reduce its productivity by fluid invasion in the borehole wall. Drilling fluids usually comprise natural polymers as starch and xanthan gum. These polymers are deposited as a filter cake on the wellbore wall. A common approach to remove this filter cake is the application of acids or strong oxidative solutions. However, these are non-specific species and a possible alternative lies in enzymatic preparations that are able to hydrolyze such polymers. The enzymes catalyze specific substrates, are environmentally friendly and the enzymatic degradation rate is slower than that achieved by the oxidative species, permitting to produce uniform degradation of the filter cake. Openhole operations require thermo and pressure stability of these enzymatic products. The results herein reported deals with the technical viability analysis of a commercial α-amylase as a new catalyst for filter cake removal. The effects of process parameters, like temperature (65, 80 and 95 °C), enzyme concentration (1, 5.5 and 10% v/v), calcium concentration (5, 70 and 135 ppm), and pressure (100, 500, 100 and 6000 psi), on amylase stability under openhole operations were investigated. Temperature demonstrated to be the most important parameter for the enzyme stability. The enzyme thermostability behavior in high salt (NaCl) concentration (completion fluid) was not significantly different from the control solution in distillated water. The pressure effect on enzyme stability did not affect the enzyme stability as temperature. Hydrostatic pressure (6000 psi) did not impact the amylolytic activity in brine solution. Combined pressure–temperature assays showed that temperature is the key factor in enzyme stability for application in polymeric filter cake removal in petroleum wells. |
Author | de Queiroz Neto, João C. Langone, Marta A.P. Coelho, Maria Alice Z. Kameda, Etel |
Author_xml | – sequence: 1 givenname: Etel surname: Kameda fullname: Kameda, Etel email: etelk@yahoo.com.br organization: Escola de Química, Universidade Federal do Rio de Janeiro, Centro de Tecnologia, Bloco E, Lab. 113, Cidade Universitária, 21949-900, Rio de Janeiro, RJ, Brazil – sequence: 2 givenname: João C. surname: de Queiroz Neto fullname: de Queiroz Neto, João C. email: joaoqueiroz@petrobras.com.br organization: Cenpes/Petrobras, Cidade Universitária, Rio de Janeiro, RJ, Brazil – sequence: 3 givenname: Marta A.P. surname: Langone fullname: Langone, Marta A.P. email: langone@uerj.br organization: Instituto de Química, Universidade do Estado do Rio de Janeiro, Rua São Francisco Xavier, 524, PHLC/IQ sala 310, Rio de Janeiro, RJ, Brazil – sequence: 4 givenname: Maria Alice Z. surname: Coelho fullname: Coelho, Maria Alice Z. email: alice@eq.ufrj.br organization: Escola de Química, Universidade Federal do Rio de Janeiro, Centro de Tecnologia, Bloco E, Lab. 113, Cidade Universitária, 21949-900, Rio de Janeiro, RJ, Brazil |
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CitedBy_id | crossref_primary_10_1016_j_petrol_2016_10_059 crossref_primary_10_1016_j_upstre_2022_100075 crossref_primary_10_2118_200845_PA crossref_primary_10_1007_s12010_009_8773_y crossref_primary_10_1016_j_ejpe_2017_01_002 crossref_primary_10_15407_fm31_01_76 crossref_primary_10_1021_acsomega_0c03436 crossref_primary_10_1016_j_geoen_2023_212287 crossref_primary_10_3390_en14165032 crossref_primary_10_3923_ajaps_2011_526_534 crossref_primary_10_1016_j_petrol_2020_107963 crossref_primary_10_1016_j_petrol_2009_10_002 |
Cites_doi | 10.1016/0920-4105(95)00051-8 10.1016/0167-4838(96)00049-0 10.1042/bj2630665 10.1128/AEM.60.3.932-939.1994 10.1016/j.petrol.2005.06.013 10.1021/ac60147a030 10.1016/S0300-9629(96)00355-6 10.1016/S0167-4838(01)00347-8 10.1016/j.bbapap.2006.01.017 10.1002/(SICI)1097-0134(199601)24:1<81::AID-PROT6>3.0.CO;2-R 10.1016/j.petrol.2005.01.003 10.1002/(SICI)1097-0290(19960405)50:1<49::AID-BIT6>3.0.CO;2-1 10.1016/S0032-9592(03)00053-0 10.1021/bp980024y |
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Keywords | Openhole conditions Starch filter-cake removal Petroleum wells Amylase Drilling fluid Drilling Enzyme Brine Xanthan gum Polymer Borehole Petroleum Salt Completion Pressure effect Acids Hydrostatic pressure Horizontal well Filter cake |
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SPE 31082 contributor: fullname: Hodge – year: 1996 ident: 10.1016/j.petrol.2007.04.005_bib9 article-title: Textiles contributor: fullname: Godfrey – volume: 31 start-page: 426 year: 1959 ident: 10.1016/j.petrol.2007.04.005_bib18 article-title: Use of dinitrosalicylic acid reagent for determination of reducing sugar publication-title: Anal. Chem. doi: 10.1021/ac60147a030 contributor: fullname: Miller – year: 2006 ident: 10.1016/j.petrol.2007.04.005_bib21 article-title: Filter-cake cleanup in MRC wells using enzyme/surfactant solutions SPE 98300 contributor: fullname: Nasr-El-Din – year: 2000 ident: 10.1016/j.petrol.2007.04.005_bib17 article-title: Factors affecting the performance of enzyme breakers for removal of xantan-based filter-cakes. SPE 58749 contributor: fullname: Luyster – year: 2001 ident: 10.1016/j.petrol.2007.04.005_bib19 contributor: fullname: Montgomery – volume: 116 start-page: 299 year: 1997 ident: 10.1016/j.petrol.2007.04.005_bib2 article-title: Hydrostatic pressure and protein: basic concepts and new data publication-title: Comp. Biochem. Physiol., Part A Physiol. doi: 10.1016/S0300-9629(96)00355-6 contributor: fullname: Balny – volume: 1595 start-page: 235 year: 2002 ident: 10.1016/j.petrol.2007.04.005_bib5 article-title: Pressure effects on intra- and intermolecular interactions within proteins publication-title: Biochim. Biophys. Acta doi: 10.1016/S0167-4838(01)00347-8 contributor: fullname: Boonyaratanakornkit – volume: 1764 start-page: 619 year: 2006 ident: 10.1016/j.petrol.2007.04.005_bib11 article-title: High pressure application for food biopolymers publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbapap.2006.01.017 contributor: fullname: Knorr – volume: 24 start-page: 81 year: 1996 ident: 10.1016/j.petrol.2007.04.005_bib20 article-title: High pressure effects on protein structure and function publication-title: Protein, Struct., Funct., Genet. doi: 10.1002/(SICI)1097-0134(199601)24:1<81::AID-PROT6>3.0.CO;2-R contributor: fullname: Mozhaev – volume: 46 start-page: 225 year: 2005 ident: 10.1016/j.petrol.2007.04.005_bib16 article-title: Tailor-modified starch/cyclodextrin-based polymers for use in tertiary oil recovery publication-title: J. Pet. Sci. Eng. doi: 10.1016/j.petrol.2005.01.003 contributor: fullname: Leislie – volume: 94 start-page: 137 year: 2002 ident: 10.1016/j.petrol.2007.04.005_bib25 article-title: Properties and applications of starch-converting enzymes of the α-amylase family publication-title: J. Biol. 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Prog. doi: 10.1021/bp980024y contributor: fullname: Lecker – year: 2002 ident: 10.1016/j.petrol.2007.04.005_bib22 article-title: Optimizing drill-in fluid composition on filter-cake lift-off pressure for openhole completation offshore applications SPE 73713 contributor: fullname: Queiroz |
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Snippet | The drilling fluid contact with the productive zone of drilling wells, with horizontal or complex configurations, can reduce its productivity by fluid invasion... |
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SubjectTerms | Amylase Applied sciences Completion equipments and methods. Casing. Cementing. Tests and measurements in wells Crude oil, natural gas and petroleum products Drilling fluid Drilling fluids Drilling methods and equipments. Rocks mechanics. Directional and horizontal drilling Drilling. Casing. Preparing wells for production Energy Exact sciences and technology Fuels Openhole conditions Petroleum wells Prospecting and production of crude oil, natural gas, oil shales and tar sands Starch filter-cake removal |
Title | Removal of polymeric filter cake in petroleum wells: A study of commercial amylase stability |
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