Abstract
The study was targeted to saccharify foodwastes with the cellulolytic and amylolytic enzymes obtained from culture supernatant ofTrichoderma harzianum FJ1 and analyze the kinetics of the saccharification in order to enlarge the utilization in industrial application.T. harzianum FJ1 highly produced various cellulolytic (filter paperase 0.9, carboxymethyl cellulase 22.0, β-glucosidase 1.2, Avicelase 0.4, xylanase 30.8, as U/mL-supernatant) and amylolytic (α-amylase 5.6, β-amylase 3.1, glucoamylase 2.6, as U/mL-supernatant) enzymes. The 23–98 g/L of reducing sugars were obtained under various experimental conditions by changing FPase to between 0.2–0.6 U/mL and foodwastes between 5–20% (w/v), with fixed conditions at 50°C, pH 5.0, and 100 rpm for 24 h. As the enzymatic hydrolysis of foodwastes were performed in a heterogeneous solid-liquid reaction system, it was significantly influenced by enzyme and substrate concentrations used, where the pH and temperature were fixed at their experimental optima of 5.0 and 50°C, respectively. An empirical model was employed to simplify the kinetics of the saccharification reaction. The reducing sugars concentration (X, g/L) in the saccharification reaction was expressed by a power curve (X=K·t n) for the reaction time (t), where the coefficient,K andn, were related to functions of the enzymes concentrations (E) and foodwastes concentrations (S), as follow:K=10.894 Ln(E·S 2)-56.768,n=0.0608·(E/S)−0.2130. The kinetic developed to analyze the effective saccharification of foodwastes composed of complex organic compounds could adequately explain the cases under various saccharification conditions. The kinetics results would be available for reducing sugars production processes, with the reducing sugars obtained at a lower cost can be used as carbon and energy sources in various fermentation industries.
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Allen, S. G., D. Schulman, J. Lichwa, and M. J. Antal Jr (2001) A comparison between hot liquid water and steam fractionation of corn fiber.Ind. Eng. Chem. Res. 40: 2934–2941.
Anuradha, R., A. K. Suresh, and K. V. Venkatesh (1999) Simultaneous saccharification and fermentation of starch to lactic acid.Process Biochem. 35: 367–375.
Bhat, M. K. and S. Bhat (1997) Cellulose degrading enzymes and their potential industrial applications.Biotechnology Adv. 15: 583–620.
Converse, A. O., H. Ooshima, and D. S. Burns (1990) Kinetics of enzymatic hydrolysis of lignocellulosic materials based on surface area of cellulose accessible to enzyme and enzyme adsorption on lignin and cellulose.Appl. Biochem. Biotechnol. 24/25: 67–73.
Desai, S. G. and A. O. Converse (1997) Substrate reactivity as a function of the extent of reaction in the enzymatic hydrolysis of lignocellulose.Biotechnol. Bioeng. 56: 650–655.
Gan, Q., S. J. Allen, and G. Taylor (2003) Kinetic dynamics in heterogeneous enzymatic hydrolysis of cellulose: An overview, an experimental study and mathematical modeling.Process Biochem. 38: 1003–1018.
Gawande, P. V. and M. Y. Kamat (1998) Preparation, characterization and application ofAspergillus sp. xylanase immobilized on Eudragit S-100.J. Biotechnol. 66: 165–175.
Ingesson, H., G. Zacchi, B. Yang, A. R. Esteghlalian, and J. N. Saddler (2001) The effect of shaking regime on the rate and extent of enzymatic hydrolysis of cellulose.J. Biotechnol. 88: 177–182.
Jl, G. E., H. K. Han, S. W. Yun, and S. L. Rhim (1992) Isolation of amylolyticBifidobacterium sp. Int-57 and characterization of amylase.J. Microbiol. Biotechnol. 2: 85–91.
Kim, E. K., D. C. Irwin, L. P. Walker, and D. B. Wilson (1998) Factorial optimization of a six-cellulase mixture.Biotechnol. Bioeng. 58: 494–501.
Kim, K. C., S. S. Yoo, Y. A. Oh, and S. J. Kim (2003) Isolation and characteristics ofTrichoderma harzianum FJ1 producing cellulases and xylanase.J. Microbiol Biotechnol. 12: 1–8.
Lee, H. K. and S. I. Hong (1987) Effect of inhibitor on enzymatic hydrolysis of cellulose.Hwahak Konghak 25: 109–114.
Lee, J. H., S. O. Lee, G. O. Lee, E. S. Seo, S. S. Chang, S. K. Yoo, D. W. Kim, D. F. Day, and D. Kim (2003) Transglycosylation reaction and raw starch hydrolysis by novel carbohydrolase fromLipomyces starkeyi.Biotechnol. Bioprocess Eng. 8: 106–111.
Lin, J. Q., S. M. Lee, and Y. M. Koo (2001) Hydrolysis of paper mill sludge using an improved enzyme system.J. Microbiol. Biotechnol. 11: 362–368.
Mansfield, S. D., C. Mooney, and J. N. Saddler (1999) Substrate and enzyme characteristics that limit cellulose hydrolysis.Biotechnol. Prog. 15: 804–816.
Medve, J., J. Karlsson, D. Lee, and F. Tjerneld (1998) Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and Endoglucoanase II fromTrichoderma reesei: Adsorption, sugar production pattern, and synergism of the enzymes.Biotechnol. Bioeng. 59: 621–634.
Min, S. Y., B. G. Kim, C. Lee, H. G. Hur, and J. H. Ahn (2002) Purification, characterization, and cDNA cloning of xylanase from fungusTrichoderma strain SY.J. Microbiol. Biotechnol. 12: 890–894.
Ooshima, H., D. S. Burns, and A. O. Converse (1990) Adsorption of cellulase fromTrichoderma reesei on cellulose and lignacious residue in wood pretreated by dilute sulfuric acid with explosive decompression.Biotechnol. Bioeng. 36: 446–452.
Ooshima, H., M. Kurakake, J. Kato, and Y. Harano (1991) Enzymatic activity of cellulase adsorbed on cellulose and its change during hydrolysis.Appl. Biochem. Biotechnol. 31: 253–266.
Park, E. Y., Y. Ikeda, and N. Okuda (2002) Empirical evaluation of cellulose on enzymatic hydrolysis of waste office paper.Biotechnol. Bioprocess Eng. 7: 268–274.
Sethi, B., S. Mishra, and V. S. Bisaria (1998) Adsorption characteristics of cellulases from a constitutive mutant ofTrichoderma reesei.J. Ferment. Bioeng. 86: 233–235.
Svetlana, V., R. M. Mark, and F. O. David (1997) Kinetic model for batch cellulase production byTrichoderma reesei RUT C30.J. Biotechnol. 54: 83–94.
Sohn, C. B., M. H. Kim, J. S. Bae, and C. H. Kim (1992) β-Amylase system capable of hydrolyzing raw starch granules fromBacillus polymyxa No. 26 and bacterial identification.J. Microbiol. Biotechnol. 2: 183–188.
Son, C. J., S. Y. Chung, J. E. Lee, and S. J. Kim (2002) Isolation and cultivation characteristics ofAcetobacter xylinum KJ-1 producing bacterial cellulose in shaking cultures.J. Microbiol. Biotechnol. 12: 722–728.
Sun, Y., and J. Cheng (2002) Hydrolysis of lignocellulosic materials for ethanol production: A review.Bioresource Technol. 83: 1–11.
Techapun, C., N. Poosaran, M. Watanabe, and K. Sasaki (2003) Thermostable and alkaline-tolerant microbial cellulase-free xylanases produced from agricultural wastes and the properties required for use in pulp bleaching bioprocesses: A review.Process Biochem. 38: 1327–1340.
Tengborg, C., M. Galbe, and G. zacchi (2001) Influence of enzyme loading and physical parameters on the enzymatic hydrolysis of steam-pretreated softwood.Biotechnol. Prog. 17: 110–117.
Thomas, M. W. and K. M. Bhat (1988) Methods for measuring cellulase activities.Method. Enzymol. 160: 87–112.
Wan Mohtar, Y., M. I. Massadeh, and J. Kader (2000) Solid substrate and submerged culture fermentation of sugar cane bagasse for the production of cellulase and reducing sugars by a local isolate,Aspergillus terreus SUK-1.J. Microbiol. Biotechnol. 10: 770–775.
Wu, J. and L. K. Ju (1998) Enhancing enzymatic saccharification of waste newsprint by surfactant addition.Biotechnol. Prog. 14: 649–652.
Yoo, S. S., K. C. Kim, Y. A. Oh, S. Y. Chung, and S. J. Kim (2002) The high production of cellulolytic enzymes using cellulosic wastes by a fungus, strain FJ1,Kor. J. Microbiol. Biotechnol. 30: 172–176.
Zhang, S., D. E. Wolfgang, and D. B. Wilson (1999) Substrate heterogeneity causes the nonlinear kinetics of insoluble cellulose hydrolysis.Biotechnol. Bioeng. 66: 35–41.
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Kim, KC., Kim, SW., Kim, MJ. et al. Saccharification of foodwastes using cellulolytic and amylolytic enzymes fromTrichoderma harzianum FJ1 and its kinetics. Biotechnol. Bioprocess Eng. 10, 52–59 (2005). https://doi.org/10.1007/BF02931183
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DOI: https://doi.org/10.1007/BF02931183