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María Angeles Camacho-Ruiz
Laboratorio de Investigación en Biotecnología, Centro Universitario del Norte, Universidad de Guadalajara, Colotlán 46200, Jalisco, Mexico

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Journal article
Published: 12 August 2021 in Sustainability
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In the present study, a novel laccase from ascomycete Gliomastix murorum was produced in agro-industrial wastes and entrapped in galactomannan beads for Reactive Blue 2 (Rb-2) decolorization. The maximum laccase production in agave bagasse-based medium occurred at 72 h (1798.6 UL−1). Entrapped laccase decolorized ˃80% of 0.5 mM Rb-2 in 2 h without the addition of redox mediator. Km for Rb-2 substrate was 1.42 mM, with a Vmax of 1.19 µmol min−1 for entrapped laccase. Galactomannan matrices produce stability to acid pH (2–5) and temperatures from 20–70 °C. Reusability assays showed that entrapped laccase could retain efficient Rb-2 decolorization of ˃80% six times. In general, galactomannan used for entrapment of laccase provides economic advantages in large-scale wastewater treatment due to its natural origin and efficient results.

ACS Style

Itzel C. Romero-Soto; Raúl B. Martínez-Pérez; Jorge A. Rodríguez; Rosa M. Camacho-Ruiz; Alejandra Barbachano-Torres; Martha Martín del Campo; Juan Napoles-Armenta; Jorge E. Pliego-Sandoval; María O. Concha-Guzmán; María Angeles Camacho-Ruiz. Galactomannans for Entrapment of Gliomastix murorum Laccase and Their Use in Reactive Blue 2 Decolorization. Sustainability 2021, 13, 9019 .

AMA Style

Itzel C. Romero-Soto, Raúl B. Martínez-Pérez, Jorge A. Rodríguez, Rosa M. Camacho-Ruiz, Alejandra Barbachano-Torres, Martha Martín del Campo, Juan Napoles-Armenta, Jorge E. Pliego-Sandoval, María O. Concha-Guzmán, María Angeles Camacho-Ruiz. Galactomannans for Entrapment of Gliomastix murorum Laccase and Their Use in Reactive Blue 2 Decolorization. Sustainability. 2021; 13 (16):9019.

Chicago/Turabian Style

Itzel C. Romero-Soto; Raúl B. Martínez-Pérez; Jorge A. Rodríguez; Rosa M. Camacho-Ruiz; Alejandra Barbachano-Torres; Martha Martín del Campo; Juan Napoles-Armenta; Jorge E. Pliego-Sandoval; María O. Concha-Guzmán; María Angeles Camacho-Ruiz. 2021. "Galactomannans for Entrapment of Gliomastix murorum Laccase and Their Use in Reactive Blue 2 Decolorization." Sustainability 13, no. 16: 9019.

Paper
Published: 16 July 2020 in Analytical Methods
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A continuous spectrophotometric assay for the screening of PHB depolymerase activity in microtiter plates was developed.

ACS Style

Maria Angeles Camacho-Ruiz; Marcelo Müller-Santos; Xitlalli D. Hernández-Mancillas; Vicente Paul Armenta-Perez; Edgar Zamora-Gonzalez; Jorge A. Rodríguez. A sensitive pH indicator-based spectrophotometric assay for PHB depolymerase activity on microtiter plates. Analytical Methods 2020, 12, 4048 -4057.

AMA Style

Maria Angeles Camacho-Ruiz, Marcelo Müller-Santos, Xitlalli D. Hernández-Mancillas, Vicente Paul Armenta-Perez, Edgar Zamora-Gonzalez, Jorge A. Rodríguez. A sensitive pH indicator-based spectrophotometric assay for PHB depolymerase activity on microtiter plates. Analytical Methods. 2020; 12 (32):4048-4057.

Chicago/Turabian Style

Maria Angeles Camacho-Ruiz; Marcelo Müller-Santos; Xitlalli D. Hernández-Mancillas; Vicente Paul Armenta-Perez; Edgar Zamora-Gonzalez; Jorge A. Rodríguez. 2020. "A sensitive pH indicator-based spectrophotometric assay for PHB depolymerase activity on microtiter plates." Analytical Methods 12, no. 32: 4048-4057.

Original article
Published: 10 December 2019 in International Microbiology
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Gastrointestinal lipase inhibitors are molecules of pharmaceutical interest due to their use as anti-obesity drugs. In this study, forty strains isolated from soil and sediments were identified with the ability to produce inhibition of gastrointestinal lipase activity. The biomass extract of these strains showed at least 50% inhibition in the hydrolysis of tributyrin by recombinant human pancreatic lipase (rHPL) or rabbit gastric lipase (RGL) by in vitro assays. Based on gene sequencing, the isolates were identified mainly as Streptomycetes. Moreover, none of the identified strains has been reported to be lipase inhibitor producers, so they can be viewed as potential sources for obtaining new drugs. IC50 values of the three best inhibitor extracts showed that AC104-10 was the most promising strain for production of gastrointestinal lipase inhibitors. AC104-10 shows 99% homology (16S rRNA gene fragment) to Streptomyces cinereoruber strain NBRC 12756. An inhibitory study over trypsin activity revealed that AC104-10 extract, as well as THL, had no significant effect on the activity of this protease, showing its specificity for lipases. In addition, analyzes by MALDI-TOF mass spectrometry of the enzyme-inhibitor complex revealed that there is a covalent interaction of the AC104-10 inhibitor with the catalytic serine of the pancreatic lipase, and that the molecular weight of the inhibitor is approximately 686.19 Da.

ACS Style

Maria Angeles Camacho-Ruiz; Enrique Ordaz; Manuel R. Kirchmayr; Hugo Esquivel-Solís; Ali Asaff-Torres; Juan Carlos Mateos-Díaz; Frédéric Carriѐre; Jorge A. Rodríguez. Screening of Gastrointestinal Lipase Inhibitors Produced by Microorganisms Isolated from Soil and Lake Sediments. International Microbiology 2019, 23, 335 -343.

AMA Style

Maria Angeles Camacho-Ruiz, Enrique Ordaz, Manuel R. Kirchmayr, Hugo Esquivel-Solís, Ali Asaff-Torres, Juan Carlos Mateos-Díaz, Frédéric Carriѐre, Jorge A. Rodríguez. Screening of Gastrointestinal Lipase Inhibitors Produced by Microorganisms Isolated from Soil and Lake Sediments. International Microbiology. 2019; 23 (2):335-343.

Chicago/Turabian Style

Maria Angeles Camacho-Ruiz; Enrique Ordaz; Manuel R. Kirchmayr; Hugo Esquivel-Solís; Ali Asaff-Torres; Juan Carlos Mateos-Díaz; Frédéric Carriѐre; Jorge A. Rodríguez. 2019. "Screening of Gastrointestinal Lipase Inhibitors Produced by Microorganisms Isolated from Soil and Lake Sediments." International Microbiology 23, no. 2: 335-343.

Journal article
Published: 01 June 2019 in Revista Mexicana de Ingeniería Química
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ACS Style

Raúl Balam Martínez Pérez; Centro De Investigación Y Asistencia En Tecnología Y Diseño Del Estado De Jalisco; M.A. Camacho-Ruiz; I. Estrada-Alvarado; V. Armenta-Pérez; R.M. Camacho-Ruíz. TIME-EFFICIENT pH-BASED METHOD TO QUANTIFY THE ACTIVITY OF ALKALINE AND HALO-ALKALINE PROTEASES. Revista Mexicana de Ingeniería Química 2019, 18, 1063 -1071.

AMA Style

Raúl Balam Martínez Pérez, Centro De Investigación Y Asistencia En Tecnología Y Diseño Del Estado De Jalisco, M.A. Camacho-Ruiz, I. Estrada-Alvarado, V. Armenta-Pérez, R.M. Camacho-Ruíz. TIME-EFFICIENT pH-BASED METHOD TO QUANTIFY THE ACTIVITY OF ALKALINE AND HALO-ALKALINE PROTEASES. Revista Mexicana de Ingeniería Química. 2019; 18 (3):1063-1071.

Chicago/Turabian Style

Raúl Balam Martínez Pérez; Centro De Investigación Y Asistencia En Tecnología Y Diseño Del Estado De Jalisco; M.A. Camacho-Ruiz; I. Estrada-Alvarado; V. Armenta-Pérez; R.M. Camacho-Ruíz. 2019. "TIME-EFFICIENT pH-BASED METHOD TO QUANTIFY THE ACTIVITY OF ALKALINE AND HALO-ALKALINE PROTEASES." Revista Mexicana de Ingeniería Química 18, no. 3: 1063-1071.

Original research paper
Published: 05 December 2018 in Biotechnology Letters
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Ustilago maydis lipase A (UMLA) expressed in Pichia pastoris was compared with Candida antarctica lipase A (CALA) to study its biochemical properties such as thermostability and selectivity. UMLA had similar behavior to its homologue CALA regarding the effect of pH and temperature on enzymatic activity, substrate preference and selectivity. Both lipases were active on insoluble triglycerides as well as natural oils and hydrolyzed preferably esters with short and medium acyl and alkyl chains. Both enzymes were slightly selective for the (S)-glycidyl butyrate enantiomer and had a remarkable preference for the sn-2 position of triglycerides. The optimal activity was 40 and 50 °C for UMLA and CALA, respectively. However, temperature had a greater effect on the stability of UMLA compared to CALA, observing a half-life at 50 °C of 2.07 h and 12.83 h, respectively. UMLA shares some biochemical properties with CALA such as the sn-2 preference on triglyceride hydrolysis and transesterification. However, the high thermostability attributed to CALA was not observed in UMLA; this can be due to the lack of stabilization via AXXXA motifs in helices and fewer proline residues at the surface.

ACS Style

Maria Marcela Robles; M. Martin Del Campo; Maria De Los Angeles Camacho Ruiz; Enrique Ordaz; Jorge Alberto Rodríguez González; Marcelo Müller-Santos; Jorge A. Rodríguez. Comparative features between recombinant lipases CALA-like from U. maydis and CALA from C. antarctica in thermal stability and selectivity. Biotechnology Letters 2018, 41, 241 -252.

AMA Style

Maria Marcela Robles, M. Martin Del Campo, Maria De Los Angeles Camacho Ruiz, Enrique Ordaz, Jorge Alberto Rodríguez González, Marcelo Müller-Santos, Jorge A. Rodríguez. Comparative features between recombinant lipases CALA-like from U. maydis and CALA from C. antarctica in thermal stability and selectivity. Biotechnology Letters. 2018; 41 (2):241-252.

Chicago/Turabian Style

Maria Marcela Robles; M. Martin Del Campo; Maria De Los Angeles Camacho Ruiz; Enrique Ordaz; Jorge Alberto Rodríguez González; Marcelo Müller-Santos; Jorge A. Rodríguez. 2018. "Comparative features between recombinant lipases CALA-like from U. maydis and CALA from C. antarctica in thermal stability and selectivity." Biotechnology Letters 41, no. 2: 241-252.

Journal article
Published: 06 July 2017 in PeerJ
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Novel microbial phospholipases A (PLAs) can be found in actinomycetes which have been poorly explored as producers of this activity. To investigate microbial PLA production, efficient methods are necessary such as high-throughput screening (HTS) assays for direct search of PLAs in microbial cultures and cultivation conditions to promote this activity. About 200 strains isolated with selected media for actinomycetes and mostly belonging toStreptomyces(73%) andMicromonospora(10%) genus were first screened on agar-plates containing the fluorophore rhodamine 6G and egg yolk phosphatidylcholine (PC) to detect strains producing phospholipase activity. Then, a colorimetric HTS assay for general PLA activity detection (cHTS-PLA) using enriched PC (≈60%) as substrate and cresol red as indicator was developed and applied; this cHTS-PLA assay was validated with known PLAs. For the first time, actinomycete strains were cultivated by solid-state fermentation (SSF) using PC as inductor and sugar-cane bagasse as support to produce high PLA activity (from 207 to 2,591 mU/g of support). Phospholipase activity of the enzymatic extracts from SSF was determined using the implemented cHTS-PLA assay and the PC hydrolysis products obtained, were analyzed by TLC showing the presence of lyso-PC. Three actinomycete strains of theStreptomycesgenus that stood out for high accumulation of lyso-PC, were selected and analyzed with the specific substrate 1,2-α-eleostearoyl-sn-glycero-3-phosphocholine (EEPC) in order to confirm the presence of PLA activity in their enzymatic extracts. Overall, the results obtained pave the way toward the HTS of PLA activity in crude microbial enzymatic extracts at a larger scale. The cHTS-PLA assay developed here can be also proposed as a routine assay for PLA activity determination during enzyme purification,directed evolution or mutagenesis approaches. In addition, the production of PLA activity by actinomycetes using SSF allow find and produce novel PLAs with potential applications in biotechnology.

ACS Style

Priscila Sutto-Ortiz; Maria De Los Angeles Camacho Ruiz; Manuel R. Kirchmayr; Rosa María Camacho-Ruiz; Juan Carlos Mateos-Díaz; Alexandre Noiriel; Frederic Carriere; Abdelkarim Abousalham; Jorge A. Rodríguez. Screening of phospholipase A activity and its production by new actinomycete strains cultivated by solid-state fermentation. PeerJ 2017, 5, e3524 -e3524.

AMA Style

Priscila Sutto-Ortiz, Maria De Los Angeles Camacho Ruiz, Manuel R. Kirchmayr, Rosa María Camacho-Ruiz, Juan Carlos Mateos-Díaz, Alexandre Noiriel, Frederic Carriere, Abdelkarim Abousalham, Jorge A. Rodríguez. Screening of phospholipase A activity and its production by new actinomycete strains cultivated by solid-state fermentation. PeerJ. 2017; 5 ():e3524-e3524.

Chicago/Turabian Style

Priscila Sutto-Ortiz; Maria De Los Angeles Camacho Ruiz; Manuel R. Kirchmayr; Rosa María Camacho-Ruiz; Juan Carlos Mateos-Díaz; Alexandre Noiriel; Frederic Carriere; Abdelkarim Abousalham; Jorge A. Rodríguez. 2017. "Screening of phospholipase A activity and its production by new actinomycete strains cultivated by solid-state fermentation." PeerJ 5, no. : e3524-e3524.

Journal article
Published: 01 May 2015 in Journal of Lipid Research
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A continuous assay is proposed for the screening of acidic, neutral, or alkaline lipases using microtiterplates, emulsified short- and medium-chain triacylglycerols (TGs) and a pH indicator. The lipase activity measurement is based on the decrease of the pH indicator optical density due to protonation which is caused by the release of free fatty acids during the hydrolysis of TGs and thus acidification. Purified lipases with distinct pH optima and an esterase were used to validate the method. The rate of lipolysis was found to be linear with time and proportional to the amount of enzyme added in each case. Specific activities measured with this microplate assay method were lower than those obtained by the pH-stat technique. Nevertheless, the pH-dependent profiles of enzymatic activity were similar with both assays. In addition, the substrate preference of each enzyme tested was not modified and this allowed discriminating lipase and esterase activities using tributyrin (low water solubility) and tricaprylin (not water-soluble) as substrates. This continuous lipase assay is compatible with a high sample throughput and can be applied for the screening of lipases and lipase inhibitors from biological samples.

ACS Style

Maria De Los Angeles Camacho Ruiz; Juan Carlos Mateos-Díaz; Frederic Carriere; Jorge A. Rodriguez. A broad pH range indicator-based spectrophotometric assay for true lipases using tributyrin and tricaprylin. Journal of Lipid Research 2015, 56, 1057 -1067.

AMA Style

Maria De Los Angeles Camacho Ruiz, Juan Carlos Mateos-Díaz, Frederic Carriere, Jorge A. Rodriguez. A broad pH range indicator-based spectrophotometric assay for true lipases using tributyrin and tricaprylin. Journal of Lipid Research. 2015; 56 (5):1057-1067.

Chicago/Turabian Style

Maria De Los Angeles Camacho Ruiz; Juan Carlos Mateos-Díaz; Frederic Carriere; Jorge A. Rodriguez. 2015. "A broad pH range indicator-based spectrophotometric assay for true lipases using tributyrin and tricaprylin." Journal of Lipid Research 56, no. 5: 1057-1067.

Book chapter
Published: 18 February 2012 in Advanced Structural Safety Studies
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High-throughput screening (HTS) methods for lipases and esterases are generally performed by using synthetic chromogenic substrates (e.g., p-nitrophenyl, resorufin, and umbelliferyl esters) which may be misleading since they are not their natural substrates (e.g., partially or insoluble triglycerides). In previous works, we have shown that soluble nonchromogenic substrates and p-nitrophenol (as a pH indicator) can be used to quantify the hydrolysis and estimate the substrate selectivity of lipases and esterases from several sources. However, in order to implement a spectrophotometric HTS method using partially or insoluble triglycerides, it is necessary to find particular conditions which allow a quantitative detection of the enzymatic activity. In this work, we used Triton X-100, CHAPS, and N-lauroyl sarcosine as emulsifiers, β-cyclodextrin as a fatty acid captor, and two substrate concentrations, 1 mM of tributyrin (TC4) and 5 mM of trioctanoin (TC8), to improve the test conditions. To demonstrate the utility of this method, we screened 12 enzymes (commercial preparations and culture broth extracts) for the hydrolysis of TC4 and TC8, which are both classical substrates for lipases and esterases (for esterases, only TC4 may be hydrolyzed). Subsequent pH-stat experiments were performed to confirm the preference of substrate hydrolysis with the hydrolases tested. We have shown that this method is very useful for screening a high number of lipases (hydrolysis of TC4 and TC8) or esterases (only hydrolysis of TC4) from wild isolates or variants generated by directed evolution using nonchromogenic triglycerides directly in the test.

ACS Style

Eduardo Mateos-Diaz; Jorge Alberto Rodríguez; María De Los Ángeles Camacho-Ruiz; Juan Carlos Mateos-Díaz. High-Throughput Screening Method for Lipases/Esterases. Advanced Structural Safety Studies 2012, 861, 89 -100.

AMA Style

Eduardo Mateos-Diaz, Jorge Alberto Rodríguez, María De Los Ángeles Camacho-Ruiz, Juan Carlos Mateos-Díaz. High-Throughput Screening Method for Lipases/Esterases. Advanced Structural Safety Studies. 2012; 861 ():89-100.

Chicago/Turabian Style

Eduardo Mateos-Diaz; Jorge Alberto Rodríguez; María De Los Ángeles Camacho-Ruiz; Juan Carlos Mateos-Díaz. 2012. "High-Throughput Screening Method for Lipases/Esterases." Advanced Structural Safety Studies 861, no. : 89-100.