Macrophomina phaseolina was cultivated in complex and simple media for the production of extracellular lipolytic enzymes. Culture supernatants were batch foam fractionated for the recovery of these enzymes, and column design and operation included the use of P 2 frit (porosity 40 to 100？μm), air as sparging gas at variable flow rates, and Triton X-100 added at the beginning or gradually in aliquots. Samples taken at intervals showed the progress of the kinetic and the efficiency parameters. Best results were obtained with the simple medium supernatant by combining the stepwise addition of small amounts of the surfactant with the variation of the air flow rates along the separation. Inert proteins were foamed out first, and the subsequent foamate was enriched in the enzymes, showing estimated activity recovery (R), enrichment ratio (E), and purification factor (P) of 45%, 34.7, and 2.9, respectively. Lipases were present in the enriched foamate. 1. Introduction Macrophomina phaseolina (Tassi) Goid. , the only species of its gender, is a phytopathogenic filamentous fungus, belonging to the anamorphic Ascomycota, Botryosphaeriaceae family . It was recently described as possessing “tools to kill”  due to its genome providing a diversified arsenal of enzymatic and toxin tools to destroy the host plants, a capacity that is confirmed by its ability to infect over 500 different plant species . Thus, to presume that Macrophomina phaseolina is able to produce several enzymes suitable for industrial applications is a reasonable hypothesis. To this purpose, many studies on its cell wall degrading hydrolases were performed [5–12]. However, M. phaseolina produces several other extracellular enzymes  of potential industrial use, among them lipolytic enzymes, which are excreted into the culture media in different amounts depending on the strain and incubation conditions. No studies were found attempting to purify these lipolytic enzymes. Several processes in the food industry, as well as environmental and industrial biotechnological applications, use enzymes as biocatalysts  due to their many advantages over chemical catalysts: the ability to function under relatively mild conditions of temperature, pH, and pressure; their specificity and, in some cases, their stereoselectivity. In addition, they do not produce unwanted byproducts . Lipases are of particular interest because of their many applications in oleochemistry, organic synthesis, the detergent industry, and nutrition , and there is constant search for new options . Eco-friendly
U. Roy and V. C. Vora, “Purification and properties of a carboxymethylcellulase from phytopathogenic fungus Macrophomina phaseolina,” Indian Journal of Biochemistry and Biophysics, vol. 26, no. 4, pp. 243–248, 1989.
P. K. Roy, U. Roy, and V. C. Vora, “Hydrolysis of wheat bran, rice bran and jute powder by immobilized enzymes from Macrophomina phaseolina,” World Journal of Microbiology and Biotechnology, vol. 9, no. 2, pp. 164–167, 1993.
H. Wang and R. W. Jones, “A unique endoglucanase-encoding gene cloned from the phytopathogenic fungus Macrophomina phaseolina,” Applied and Environmental Microbiology, vol. 61, no. 5, pp. 2004–2006, 1995.
H. Wang and R. W. Jones, “Properties of the Macrophomina phaseolina endoglucanase (EGL 1) gene product in bacterial and yeast expression systems,” Applied Biochemistry and Biotechnology Part A, vol. 81, no. 3, pp. 153–160, 1999.
A. Miettinen-Oinonen, “Cellulases in the textile industry,” in Industrial Enzymes: Structure, Function and Applications, J. Polaina and A. P. MacCabe, Eds., pp. 51–64, Springer, Dordrecht, The Netherlands, 2007.
L. Afouda, G. Wolf, and K. Wydra, “Development of a sensitive serological method for specific detection of latent infection of Macrophomina phaseolina in cowpea,” Journal of Phytopathology, vol. 157, no. 1, pp. 15–23, 2009.
S. Kaur, “Carbohydrate degrading enzyme production by plant pathogenic mycelia and microsclerotia isolates of Macrophomina phaseolina through koji fermentation,” Industrial Crops and Products, vol. 36, no. 1, pp. 140–148, 2012.
B. M. Gerken, A. Nicolai, D. Linke, H. Zorn, R. G. Berger, and H. Parlar, “Effective enrichment and recovery of laccase C using continuous foam fractionation,” Separation and Purification Technology, vol. 49, no. 3, pp. 291–294, 2006.
V. Burapatana, E. A. Booth, I. M. Snyder, A. Prokop, and R. D. Tanner, “A proposed mechanism for detergent-assisted foam fractionation of lysozyme and cellulase restored with β-cyclodextrin,” Applied Biochemistry and Biotechnology, vol. 137-140, no. 1-12, pp. 777–791, 2007.
J. N. Dos Prazeres, A. P. Simiqueli, G. M. Pastore et al., “Recovery of extracellular alkaline lipases of Fusarium spec. by foam fractionation,” Fresenius Environmental Bulletin, vol. 16, no. 11 B, pp. 1503–1508, 2007.
V. Burapatana, E. A. Booth, A. Prokop, and R. D. Tanner, “Effect of buffer and pH on detergent-assisted foam fractionation of cellulase,” Industrial and Engineering Chemistry Research, vol. 44, no. 14, pp. 4968–4972, 2005.
F. Uraizee and G. Narsimhan, “Effects of kinetics of adsorption and coalescence on continuous foam concentration of proteins: comparison of experimental results with model predictions,” Biotechnology and Bioengineering, vol. 51, pp. 384–398, 1996.
J. Merz, G. Schembecker, S. Riemer, M. Nimtz, and H. Zorn, “Purification and identification of a novel cutinase from Coprinopsis cinerea by adsorptive bubble separation,” Separation and Purification Technology, vol. 69, no. 1, pp. 57–62, 2009.
D. Linke, H. Zorn, B. Gerken, H. Parlar, and R. G. Berger, “Laccase isolation by foam fractionation—new prospects of an old process,” Enzyme and Microbial Technology, vol. 40, no. 2, pp. 273–277, 2007.
H. Zorn, D. E. Breithaupt, M. Takenberg, W. Schwack, and R. G. Berger, “Enzymatic hydrolysis of carotenoid esters of marigold flowers (Tagetes erecta L.) and red paprika (Capsicum annuum L.) by commercial lipases and Pleurotus sapidus extracellular lipase,” Enzyme and Microbial Technology, vol. 32, no. 5, pp. 623–628, 2003.
D. Linke, M. Nimtz, R. G. Berger, and H. Zorn, “Separation of extracellular esterases from pellet cultures of the basidiomycete Pleurotus sapidus by foam fractionation,” Journal of the American Oil Chemists' Society, vol. 86, no. 5, pp. 437–444, 2009.
D. C. Clark, “Application of state-of-the-art fluorescence and interferometric techniques to study coalescence in food dispersions,” in Characterization of Food: Emerging Methods, A. G. Gaonkar, Ed., pp. 23–57, Elsevier, Amsterdam, The Netherlands, 1995.
P. J. Wilde, F. A. Husband, D. Cooper et al., “Interfacial mechanisms underlying lipid damage of beer foam,” in Food Colloids, Biopolymers and Materials, E. Dickinson and T. van Vliet, Eds., pp. 200–206, The Royal Society of Chemistry, Cambridge, UK, 2003.
J. Varley, A. K. Brown, J. W. R. Boyd, P. W. Dodd, and S. Gallagher, “Dynamic multi-point measurement of foam behaviour for a continuous fermentation over a range of key process variables,” Biochemical Engineering Journal, vol. 20, no. 1, pp. 61–72, 2004.
A. R. Mackie, A. P. Gunning, P. J. Wilde, and V. J. Morris, “Orogenic displacement of protein from the air/water interface by competitive adsorption,” Journal of Colloid and Interface Science, vol. 210, no. 1, pp. 157–166, 1999.
H. Chahinian, L. Nini, E. Boitard, J. P. Dubès, L. C. Comeau, and L. Sarda, “Distinction between esterases and lipases: a kinetic study with vinyl esters and TAG,” Lipids, vol. 37, no. 7, pp. 653–662, 2002.