Abstract
Melanocarpus albomyces steryl esterase STE1 is considered to be an interesting tool for several industrial applications due to its broad substrate specificity. STE1 was produced in the filamentous fungus Trichoderma reesei in a laboratory bioreactor at an estimated production level of 280 mg l−l. The properties of the purified recombinant enzyme (rSTE1), such as substrate specificity, molecular mass, pH optimum and stability and thermostability, were characterized and compared to the corresponding properties of the native enzyme. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis showed one band with a molecular weight of 60 kDa for rSTE1, whereas analytical gel filtration showed a dimeric structure with a molecular weight of 120 kDa. The rSTE1 was somewhat less stable under different conditions and had slightly lower activities on various substrates than the native STE1. The effects of rSTE1 on the properties of paper sheets and polyethylene terephthalate (PET) fabric were preliminarily evaluated. Due to the hydrolysis of triglycerides and steryl esters by the rSTE1 treatment, the tensile strength and hydrophilicity of the paper were increased. The rSTE1 treatment increased significantly the polarity of PET by hydrolysing the ester bonds in the polyester backbone. Dyeing of PET with methylene blue was also slightly improved after rSTE1 treatment.
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References
Andersen BK, Borch K, Abo M, Damgaard B (1999) Method of treating polyester fabrics. US Patent 5,997,584
Brush TS, Chapman R, Kurzman R, Williams DP (1999) Purification and characterization of extracellular lipases from Ophiostoma piliferum. Bioorg Med Chem 7:2131–2138
Calero-Rueda O, Plou FJ, Ballesteros A, Martínez AT, Martínez MJ (2002) Production, isolation and characterization of a sterol esterase from Ophiostoma piceae. Biochim Biophys Acta 1599:28–35
Chen T, Wang Z, Gao Y, Breuil C, Hatton JV (1994) Wood extractives and pitch problems: analysis and partial removal by biological treatment. APPITA 47:463–466
Chen S, Lin Y, Zhang Y, Wang XH, Yang JL (2001) Enzymatic pitch control at Nanping paper mill. Tappi J 84:44–47
Farrell RL, Hata K, Wall MB (1997) Solving pitch problems in pulp and paper processes by the use of enzymes or fungi. In: Scheper T (ed) Advances in Biochemical Engineering/Biotechnology, vol 57. Springer, Berlin Heidelberg New York, pp 197–212
Fischer K, Akhtar M, Blanchette RA, Burnes TA, Messner K, Kirk TK (1994) Reduction of resin content in wood chips during experimental biological pulping processes. Holzforschung 48:285–290
Fojan P, Jonson PH, Petersen MTN, Petersen SB (2000) What distinguishes an esterase from a lipase: a novel structural approach. Biochimie 82:1033–1041
Fujita Y, Awaji H, Taneda H, Matsukura M, Hata K, Shimoto H, Sharyo M, Sakaguchi H, Gibson K (1992) Recent advances in enzymatic pitch control. Tappi J 75:117–122
Gao Y, Breuil C (1998) Properties and substrate specificities of an extracellular lipase purified from Ophiostoma piceae. World J Microbiol Biotechnol 14:421–429
Gübitz GM, Cavago-Paulo A (2003) New substrates for reliable enzymes: enzymatic modification of polymers. Curr Opin Biotechnol 14:577–582
Gutiérrez A, del Río JC, Martínez MJ, Martínez AT (2001) The biotechnological control of pitch in paper pulp manufacturing. Trends Biotechnol 19:340–348
Hata K, Matsukura M, Taneda H, Fujita Y (1996) Mill-scale application of enzymatic pitch control during paper processing. In: Jeffries TW, Viikari L (eds) Enzymes for pulp and paper processing. American Chemical Society, Washington, DC, pp 280–296
Hsieh Y-L, Cram LA (1998) Enzymatic hydrolysis to improve wetting and absorbency of polyester fabrics. Tex Res J 68:311–319
Kaiser R, Erman M, Duax WL, Ghosh D, Jörnvall H (1994) Monomeric and dimeric forms of cholesterol esterase from Candida cylindracea. FEBS Lett 337:123–127
Kallioinen A, Siika-aho M, Pere J, Vaari A, Viikari L (2004) Evaluation of bacterial pretreatment of spruce woodchips for mechanical pulping. Appita J 57:488–492
Kamei T, Suzuki H, Asano K, Matsuzaki M, Nakamura S (1979) Cholesterol esterase produced by Streptomyces lavendulae. Purification and properties as a lipolytic enzyme. Chem Pharm Bull 27:1704–1707
Kantelinen A, Jokinen O, Sarkki M-L, Pettersson C, Sundberg K, Eckerman C, Ekman R, Holmbom B (1995) Effects of enzymes on the stability of colloidal pitch. In: Proceedings of the 8th International Symposium on Wood and Pulping Chemistry, vol I, Helsinki, pp 605–612
Kokkonen P, Korpela A, Sundberg A, Holmbom B (2002) Effects of different types of lipophilic extractives on paper properties. Nord Pulp Pap Res J 17:382–386
Kontkanen H, Tenkanen M, Fagerström R, Reinikainen T (2004) Characterisation of steryl esterase activities in commercial lipase preparations. J Biotechnol 108:51–59
Kontkanen H, Tenkanen M, Reinikainen T (2006a) Purification and characterisation of a novel steryl esterase from Melanocarpus albomyces. Enzyme Microb Technol (in press)
Kontkanen H, Reinikainen T, Saloheimo M (2006b) Cloning and expression of a Melanocarpus albomyces steryl esterase gene in Pichia pastoris and Trichoderma reesei. Biotechnol Bioeng (accepted)
Leone R, Breuil C (1999) Biodegradation of aspen steryl esters and waxes by two filamentous fungi with or without other carbon sources. World J Microbiol Biotechnol 15:723–727
Madhosingh C, Orr W (1981) Sterol ester hydrolase in Fusarium oxysporum. Lipids 16:125–132
Martínez-Iñigo MJ, Gutiérrez A, del Río JC, Martínez MJ, Martínez AT (2000) Time course of fungal removal of lipophilic extractives from Eucalyptus globulus wood. J Biotechnol 84:119–126
Miettinen-Oinonen A, Puolakka A, Nousiainen P, Buchert J (2005) Modification of polyester with cutinase. A poster. In: EU COST 847 Final workshop 20.–22.2.2005, Gran Canaria, Spain
Montenecourt BS, Eveleigh DE (1979) Selective screening methods for the isolation of high yielding mutants of Trichoderma reesei. Adv Chem Ser 181:289–301
Mustranta A, Buchert J, Spetz P, Holmbom B (2001) Treatment of mechanical pulp and process waters with lipase. Nord Pulp Pap Res J 16:140–144
Nylund J, Sundberg K, Shen Q, Rosenholm JB (1998) Determination of surface energy and wettability of wood resins. Colloids Surf A Physicochem Eng Asp 133:261–268
Örså F, Holmbom B (1994) A convenient method for the determination of wood extractives in papermaking process waters and effluents. J Pulp Pap Sci 20:J361–J366
Otero D, Sundberg K, Blanco A, Negro C, Tijero J, Holmbom B (2000) Effects of wood polysaccharides on pitch deposition. Nord Pulp Pap Res J 15:607–613
Qin M, Hannuksela T, Holmbom B (2003) Physico-chemical characterisation of TMP resin and related model mixtures. Colloids Surf A Physicochem Eng Asp 221:243–254
Rocheleau MJ, Sitholé BB, Allen LH, Iverson S, Farrel R, Noel Y (1998) Fungal treatment of aspen chips for wood resin reduction: a laboratory evaluation. J Pulp Pap Sci 24:37–42
Rúa ML, Schmidt-Dannert C, Wahl S, Sprauer A, Schmid RD (1997) Thermoalkalophilic lipase of Bacillus thermocatenulatus. Large-scale production, purification and properties: aggregation behaviour and its effect on activity. J Biotechnol 56:89–102
Sihvonen AL, Sundberg K, Sundberg A, Holmbom B (1998) Stability and deposition tendency of colloidal wood resin. Nord Pulp Pap Res J 13:64–67
Sugihara A, Shimada Y, Nomura A, Terai T, Imayasu M, Nagai Y, Nagao T, Watanabe Y, Tominaga Y (2002) Purification and characterization of a novel cholesterol esterase from Pseudomonas aeruginosa, with its application to cleaning lipid-stained contact lenses. Biosci Biotechnol Biochem 66:2347–2355
Sundberg K, Thornton J, Holmbom B, Ekman R (1996) Effects of wood polysaccharides on the stability of colloidal wood resin. J Pulp Pap Sci 22:J226–J230
Sundberg A, Holmbom B, Willför S, Pranovich A (2000) Weakening of paper strength by wood resin. Nord Pulp Pap Res J 15:46–53
Svendsen A, Borch K, Barfoed M, Nielsen TB, Gormsen E, Patkar SA (1995) Biochemical properties of cloned lipases from the Pseudomonas family. Biochim Biophys Acta 1259:9–17
Taketani S, Nishino T, Katsuki H (1981) Purification and properties of sterol-ester hydrolase from Saccharomyces cerevisiae. J Biochem 89:1667–1673
Tenkanen M, Kontkanen H, Isoniemi R, Spetz P, Holmbom B (2002) Hydrolysis of steryl esters by a lipase (Lip 3) from Candida rugosa. Appl Microbiol Biotechnol 60:120–127
Touchette RV, Jenness LC (1960) Effect of surface active agents on drainage and physical strength properties of sulfite pulp. Tappi 43:484–489
Uwajima T, Terada O (1976) Purification and properties of cholesterol esterase from Pseudomonas fluorescens. Agric Biol Chem 40:1957–1964
Vertommen MAME, Nierstrasz VA, van der Veer M, Warmoeskerken MMCG (2005) Enzymatic modification of poly(ethylene terephthalate). J Biotechnol 120(4):376–386
Vippola M (2002) Microstructural study of aluminum phosphate sealed plasma sprayed alumina and chromia coatings. Doctoral thesis, 360, Tampere University of Technology, 128 pp
Wearing JT, Barbe MC, Ouchi MD (1985) The effect of white-water contamination on newsprint properties. J Pulp Pap Sci 11:J113–J121
Yoon M-Y, Kellis J, Poulose AJ (2002) Enzymatic modification of polyester. AATCC Rev 2:33–36
Zhang X (2000) The effects of white-water dissolved and colloidal fractions on paper properties and effects of various enzyme treatments on the removal of organic components. Pulp Pap Can 101:59–62
Acknowledgements
This work was financed by the Raisio Group Foundation. The study of using the enzyme for polyester modification was carried out in the framework of the RTD project “Biotechnical quality improvement of synthetic textile fibres” (G5RD-CT-2001-00560) funded by the European Commission. Michael Bailey and Merja Aarnio are acknowledged for the fermentation. Kati Uotila is thanked for treatments and analyses of polyester fabrics. Arja Puolakka from Tampere University of Technology is thanked for contact angle measurements of polyester.
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Kontkanen, H., Saloheimo, M., Pere, J. et al. Characterization of Melanocarpus albomyces steryl esterase produced in Trichoderma reesei and modification of fibre products with the enzyme. Appl Microbiol Biotechnol 72, 696–704 (2006). https://doi.org/10.1007/s00253-006-0321-x
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DOI: https://doi.org/10.1007/s00253-006-0321-x