Münir TUNCER, Andrew S. BALL

3414

Co-operative actions and degradation analysis of purified lignocellulose-degrading enzymes from Thermomonospora fusca BD25 on wheat straw

In industrial hydrolysis processes the lignocellulose-degrading enzymes may have a potential application as an alternative to chemical treatments because they produce high specificity, mild reaction conditions, no toxic chemical hydrolysis inhibitors, and no loss of substrate due to chemical modifications. The amounts of reducing sugars released from the degradation of wheat straw by the action of endoxylanase, peroxidase, b-xylosidase, and a-L-arabinofuranosidase, which were produced by T. fusca BD25,were equal to 3.0 percent, 0.2 percent, 0.3 percent, and 0.2 percent hydrolysis (as xylose equivalents) of the substrate used, respectively, after 10 h of incubation. In the same conditions, the hydrolysis rate of endoglucanase, which was a commercial preparation from Trichoderma viride was 4.9 percent. However, in order, addition of peroxidase, endoglucanase, b -xylosidase, and a-L-arabinofuranosidase preparations to the endoxylanase preparation significantly enhanced the reducing sugar yields (1.33-, 1.52-, 1.61-, and 1.71-fold, respectively) and the hydrolysis of wheat straw (4.3 percent, 12.3 percent, 13.5 percent, and 14.7 percent, respectively). The concentrations of phenolic-compounds as lignin-equivalents released from wheat straw by the actions of lignocellulose-degrading enzyme preparations either acting alone or in combinations ranged from 2.5 to 129.3 mg mL-1 (as p-coumaric acid equivalents). The combination of purified lignocellulose-degrading enzymes significantly increased the degradation of straw 1.33- to 1.71-fold. The results highlight the role of lignocellulose-degrading enzymes in the degradation of wheat straw and suggest that the use of enzyme cocktails may significantly improve the hydrolysis of wheat straw in industrial processes.
Anahtar Kelimeler:

Key words: Degradation, endoxylanase, lignocellulose, peroxidase, pulp, wheat straw

Co-operative actions and degradation analysis of purified lignocellulose-degrading enzymes from Thermomonospora fusca BD25 on wheat straw

In industrial hydrolysis processes the lignocellulose-degrading enzymes may have a potential application as an alternative to chemical treatments because they produce high specificity, mild reaction conditions, no toxic chemical hydrolysis inhibitors, and no loss of substrate due to chemical modifications. The amounts of reducing sugars released from the degradation of wheat straw by the action of endoxylanase, peroxidase, b-xylosidase, and a-L-arabinofuranosidase, which were produced by T. fusca BD25,were equal to 3.0 percent, 0.2 percent, 0.3 percent, and 0.2 percent hydrolysis (as xylose equivalents) of the substrate used, respectively, after 10 h of incubation. In the same conditions, the hydrolysis rate of endoglucanase, which was a commercial preparation from Trichoderma viride was 4.9 percent. However, in order, addition of peroxidase, endoglucanase, b -xylosidase, and a-L-arabinofuranosidase preparations to the endoxylanase preparation significantly enhanced the reducing sugar yields (1.33-, 1.52-, 1.61-, and 1.71-fold, respectively) and the hydrolysis of wheat straw (4.3 percent, 12.3 percent, 13.5 percent, and 14.7 percent, respectively). The concentrations of phenolic-compounds as lignin-equivalents released from wheat straw by the actions of lignocellulose-degrading enzyme preparations either acting alone or in combinations ranged from 2.5 to 129.3 mg mL-1 (as p-coumaric acid equivalents). The combination of purified lignocellulose-degrading enzymes significantly increased the degradation of straw 1.33- to 1.71-fold. The results highlight the role of lignocellulose-degrading enzymes in the degradation of wheat straw and suggest that the use of enzyme cocktails may significantly improve the hydrolysis of wheat straw in industrial processes.
Keywords:

Key words: Degradation, endoxylanase, lignocellulose, peroxidase, pulp, wheat straw,

PDF

___

  • Tien M. Properties of ligninase from Phanerochaete chrysosporium and their possible applications. CRC Critical Review of Microbiology 15: 141-168, 1987.
  • Eriksson K-EL, Blanchette RA, Ander P. Microbial and enzymatic degradation of wood and wood components. Springer-Verlag, NewYork; 1990: p. 416.
  • Sinner M, Parameswaran N, Yamazaki N et al. Specific enzymatic degradation of polysaccharides in delignified wood cell walls. Applied Polymer Symposium 28: 993-1024, 1976. 8. Yu EKC, Saddler JN. Biomass conversion to butanediol by simultaneous saccharification and fermentation. Trends in Biotechnology 3: 100-104, 1985. 9. Biely P. Microbial xylanolytic systems. Trends in Biotechnology 3: 286-290, 1985.
  • Viikari L, Pauna M, Kantelinen A et al. M. Bleaching with enzymes. In: Proceedings of the third international conference on biotechnology in the pulp and paper industry. Stockholm, 1986: pp. 67-69.
  • Viikari L, Kantelinen A, Sundquist J et al. Xylanases in bleaching: From an idea to the industry. FEMS Microbiology Reviews 13: 335-350, 1994.
  • Nissen AM, Anker L, Munk N et al. Xylanases for the pulp and paper industry. In: Visser J, Beldman G, Kusters-van-Someren MA et al. eds. Xylans and xylanases. Elsevier, Amsterdam, London, New York, Tokyo; 1992: pp 325-337.
  • Senior DJ, Hamilton J, Bernier RL Jr. Use of Streptomyces lividans xylanase for bleaching of kraft pulps. In: Visser J, Beldman G, Kusters-van-Someren MA et al. eds. Xylans and xylanases. Elsevier, Amsterdam, London, New York, Tokyo; 1992: pp 555-558.
  • Reid ID, Paice MG. Effects of manganese peroxidase on residual lignin of softwood kraft pulp. Applied and Environmental Microbiology 64: 2273-2274, 1998.
  • Zhang ZS, Wang Y, Ruan JS. Reclassification of Thermomonospora and Microtetraspora. International Journal of Systematic Bacteriology 48: 411-422, 1998.
  • Tuncer M, Rob A, Ball AS et al. Optimization of production of extracellular non-haem peroxidases by Thermomonospora fusca BD25 in aerobic bio-reactor conditions. Biochemical Society Transactions 25: S 65, 1997.
  • Tuncer M, Rob A, Ball AS et al. Optimisation of extracellular lignocellulolytic enzyme production by a thermophilic actinomycete Thermomonospora fusca BD25. Enzyme and Microbial Technology 25: 38-47, 1999.
  • Tuncer M, Ball AS. Co-operative actions and degradation analysis of purified xylan-degrading enzymes from Thermomonospora fusca BD25 on oat-spelt xylan. Journal of Applied Microbiology 94: 1030-1035, 2003.
  • Tuncer M, Ball AS. Purification and partial characterization of a-L-arabinofuranosidase produced by Thermomonospora fusca BD25. Folia Microbiologica 48: 168-172, 2003.
  • Miller GL. Use of dinitroslisylic acid reagent for determination of reducing sugar. Analytical Chemistry 31: 426-428, 1959.
  • Bachmann SL, McCarthy AJ. Prufication and characterization of a thermostable b-Xylosidase from Thermomonospora fusca. Journal of General Microbiology 135: 293-299, 1989.
  • MacKenzie CR, Bilous D, Schnieder H et al. Induction of cellulolytic and xylanolytic enzyme systems in Streptomyces spp. Applied and Environmental Microbiology 53: 2835-2839, 1987.
  • Ramachandra M, Crawford DL, Hertel G. Characterization of an extracellular lignin peroxidase of the lignocellulolytic actinomycete Streptomyces viridosporus. Environmental Microbiology 54: 3057-3063, 1988. Applied and
  • Rob A, Ball AS, Tuncer M et al. Thermostable novel non-haem extracellular glycosylated peroxidase from Thermomonospora fusca BD25. Biotechnology and Applied Biochemistry. 24: 161- 170, 1996.
  • Lowry OH, Rosebrough NJ, Farr AL et al. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193: 265-275, 1951.
  • Puls J, Schuseil J. Chemistry of hemicelluloses: Relationship between hemicellulose structure and enzymes required for hydrolysis. In: Coughlan MP, Hazlewood GP eds. Hemicellulose and hemicellulases. Portland Press, London; 1993: pp. 1-27.
  • Tenkanen M, Schuseil J, Puls J et al. Production, purification and characterization of an esterase liberating phenolic acids from lignocellulosics. Journal of Biotechnology 18: 69-84, 1991.
  • Castanares A, McCrea SI, Wood TM. Purification and properties of a feruloyl/p-coumaroyl esterase from the fungus Penicillium pinophilum. Enzyme and Microbial Technology 14: 875-884, 1992.
  • MacKenzie CR, Bilous D. Ferulic acid esterase activity from Schizophillum commune. Applied and Environmental Microbiology 54: 1170-1173, 1988.
  • Faulds CB, Williamson G. The purification and characterization of 4-hydroxy-3-methoxycinnamic (ferulic) acid esterase from Streptomyces olivochromogenes. Journal of General Microbiology 137: 2339-2345, 1991.
  • Mueller-Harvey I, Hartley RD, Harris PJ et al. Linkage of p- coumaryl and feruloyl groups to cell wall polysaccharides of barley straw. Carbohydrate Research 148: 71-85, 1986.
  • Greve LC, Labavitch JM, Hungate RE. a-L-arabinofuranosidases from Ruminococcus albus 8: purification and possible role in hydrolysis of alfalfa cell wall. Applied and Environmental Microbiology 47: 1135-1140, 1984.
  • Wood TM, McCrae SI. Arabinoxylan-degrading enzyme- system of the fungus Aspergillus awamori: purification and properties of an α-L-arabinofuranosidase. Applied Microbiology and Biotechnology 45: 538-545, 1996.
  • Bachmann SL, McCarthy AJ. Purification and co-operative activity of enzymes constituting the xylan-degrading system of Thermomonospora fusca. Applied and Environmental Microbiology 57: 2121-2130, 1991.
  • Filho EXF, Puls J, Coughlan MP. Purification and characterisation of two arabinofuranosidases from solid-state cultures of the fungus Penicillium capsulatum. Applied and Environmental Microbiology 62: 168-173, 1996.
  • Berens S, Kaspari H, Klemme JH. Purification and characterization of 2 different xylanases from the thermophilic actinomycete Microtetraspora flexuosa SIIX. Antonie Van Leeuwenhoek, International Journal of Gen. Mol. Microbiol. 69: 235-241, 1996.
  • Stutzenberger FJ, Bodine AB. Thermostable b-xylosidase from Thermomonospora curvata. Journal of Industrial Microbiology and Biotechnology 20: 55-60, 1998.
  • Ball AS, McCarthy AJ. Production and properties of xylanases from actinomycetes. Journal of Applied Bacteriology 66: 439- 444, 1989.
  • Ball AS, McCarthy AJ. Saccharification of straw by actinomycete enzymes. Journal of General Microbiology 134: 2139-2147, 1988.
Turkish Journal of Biology-Cover
  • ISSN: 1300-0152
  • Yayın Aralığı: Yılda 6 Sayı
  • Yayıncı: TÜBİTAK
Arşiv
Sayıdaki Diğer Makaleler

Propagation of Endangered Thermopsis turcica Tan, Vural & Küçüködük Using Conventional and In Vitro Techniques

Süleyman CENKCİ, Mehmet TEMEL, Mustafa KARGIOĞLU, Sergun DAYAN

Eicosanoids act in nodulation reactions to the bacterium Serratia marcescens in the Hemipteran pest Eurygaster integriceps

Hasan TUNAZ

Biological activities of Vitis vinifera L. leaves

Berrin ÖZÇELIK, Didem Deliorman ORHAN, Nilüfer ORHAN, Fatma ERGUN

Biological Screening of Vitis vinifera L. Leaf Fractions

Didem Deliorman ORHAN, Nilüfer ORHAN, Berrin ÖZÇELIK, Fatma ERGUN

Co-operative actions and degradation analysis of purified lignocellulose-degrading enzymes from Thermomonospora fusca BD25 on wheat straw

Münir TUNCER, Andrew S. BALL

Comparative Susceptibilities of Six Insect Cell Lines to Infection by Malacosoma neustria Nucleopolyhedrovirus (ManeNPV)

İsmail DEMİR, Nurten GÜREL, Remziye NALÇACIOĞLU, Zihni DEMİRBAĞ

The Effect of Environmental Factors on the Growth and size Structure of two Dominant Phytoplankton Species in the Büyükçekmece Reservoir (İstanbul,Turkey)

Yelda AKTAN, Cenk GÜREVİN, Zeynep DORAK

Genotoxic Effects of Herbicide Illoxan (Diclofop-Methyl) on Allium cepa L.

Deniz YÜZBAŞIOĞLU, Fatma ÜNAL, Cengiz SANCAK

Propagation of endangered Thermopsis turcica Kit Tan, Vural & Küçüködük using conventional and in vitro techniques

Sergun DAYAN, Süleyman CENKCİ, Mehmet TEMEL, Mustafa KARGIOĞLU

Propagation of Endangered Thermopsis turcica Tan, Vural & Küçüködük Using Conventional and In Vitro Techniques

Süleyman CENKCİ, Mehmet TEMEL, Mustafa KARGIOĞLU, Sergun DAYAN