1. Production of multi-fiber modifying enzyme from Mamillisphaeria sp. for refining of recycled paper pulp
- Author
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Saowanee Apawasin, Thanaporn Laothanachareon, Lily Eurwilaichitr, Phungjai Tinnasulanon, Parichart Khonzue, Sutipa Tanapongpipat, Vasimon Ruanglek, Nakul Rattanaphan, Verawat Champreda, and Atchara Paemanee
- Subjects
Paper ,Proteomics ,Cellulase ,engineering.material ,Applied Microbiology and Biotechnology ,Biochemistry ,Analytical Chemistry ,chemistry.chemical_compound ,Ascomycota ,Hydrolase ,Immersion ,Yeast extract ,Industry ,Glycosyl ,Food science ,Molecular Biology ,Endo-1,4-beta Xylanases ,Bran ,Filter paper ,biology ,Pulp (paper) ,Organic Chemistry ,food and beverages ,Green Chemistry Technology ,General Medicine ,chemistry ,Fermentation ,engineering ,biology.protein ,Xylanase ,Biotechnology - Abstract
Enzymatic modification of pulp is receiving increasing interest for energy reduction at the refining step of the paper-making process. In this study, the production of a multi-fiber modifying enzyme from Mamillisphaeria sp. BCC8893 was optimized in submerged fermentation using a response-surface methodology. Maximal production was obtained in a complex medium comprising wheat bran, soybean, and rice bran supplemented with yeast extract at pH 6.0 and a harvest time of 7 d, resulting in 9.2 IU/mL of carboxymethyl cellulase (CMCase), 14.9 IU/mL of filter paper activity (FPase), and 242.7 IU/mL of xylanase. Treatment of old corrugated container pulp at 0.2-0.3 IU of CMCase/g of pulp led to reductions in refining energy of 8.5-14.8%. The major physical properties were retained, including tensile and compression strength. Proteomic analysis showed that the enzyme was a complex composite of endo-glucanases, cellobiohydrolases, beta-1,4-xylanases, and beta-glucanases belonging to various glycosyl hydrolase families, suggestive of cooperative enzyme action in fiber modification, providing the basis for refining efficiency.
- Published
- 2011