• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.38 no.3 s.116
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• pp.23-28
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• 2006

Xylan in hemicellulose has been reported as one of the reasons of the yellowing of chemical pulp and paper. But little relevant information is available in literature. In this study, we examined into the influence that glucuronoxylan or glucomannan and metallic ion($Cu^{2+},\;Fe^{2+},\;Fe^{3+},\;Mn^{2+}$) residued in pulp get each or when mixed at yellowing. Filter paper was treated with each metallic ion, glucuronoxylan and the mixture of glucuronoxylan and metal ions, and brightness and CIE $L^*a^*b^*$ was measured after accelerated aging. As the results of measurements, the filter paper processed by 10% glucuronoxylan was dropped $2{\sim}3%$ on the brightness after accelerated aging for 24 hours. Also, the filter paper treated with glucuronoxylan and $Fe^{2+}$ was dropped 7% on the brightness.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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• 2006.06b
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• pp.361-364
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• 2006

Generally, aging of paper is evaluated by folding endurance and degree of yellowing. It was known as that lignin, hemicellulose and metallic ion affect yellowing of mechanical or chemical pulps. Among these elements, especially, the study of hemicellulose that affect at yellowing of pulp is insufficient. In this study, we examined into the influence that glucuronoxylan or glucomannan and metallic ion($Cu^{2+},\;Fe^{2+},\;Fe^{3+},Mn^{2+}$) residued in pulp get each or when mixed at yellowing. Filter paper was treated with each metallic ion, glucuronoxylan and the mixture of glucuronoxylan and metal ions, and brightness and CIE $L^*a^*b^*$ was measured after accelerated aging. As the results of measurements, the filter paper processed by 10% glucuronoxylan was dropped 2-3% on the brightness after accelerated aging for 24 hours. Also, the filter paper treated with glucuronoxylan and $Fe^{2+}$ was dropped 7% on the brightness.

• Journal of Microbiology and Biotechnology
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• v.27 no.1
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• pp.77-83
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• 2017

Lignocellulosic biomass represents a potentially large resource to supply the world's fuel and chemical feedstocks. Enzymatic bioconversion of this substrate offers a reliable strategy for accessing this material under mild reaction conditions. Owing to the complex nature of lignocellulose, many different enzymatic activities are required to function in concert to perform efficient transformation. In nature, large multienzyme complexes are known to effectively hydrolyze lignocellulose into constituent monomeric sugars. We created artificial complexes of enzymes, called rosettazymes, in order to hydrolyze glucuronoxylan, a common lignocellulose component, into its cognate sugar ${\small{D}}$-xylose and then further convert the ${\small{D}}$-xylose into ${\small{D}}$-xylonic acid, a Department of Energy top-30 platform chemical. Four different types of enzymes (endoxylanase, ${\alpha}$-glucuronidase, ${\beta}$-xylosidase, and xylose dehydrogenase) were incorporated into the artificial complexes. We demonstrated that tethering our enzymes in a complex resulted in significantly more activity (up to 71%) than the same amount of enzymes free in solution. We also determined that varying the enzyme composition affected the level of complex-related activity enhancement as well as overall yield.

• Korean Journal of Microbiology
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• v.52 no.4
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• pp.463-470
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• 2016

The enzymatic degradation of xylans is the most versatile way to obtain the high value-added functional compounds or the fermentable sugars for renewable energy. The endo-${\beta}$-xylanases are the major enzymes which hydrolyze the internal ${\beta}$-1,4-linkages of xylan backbones to produce the mixtures of xylooligosaccharides including xylobiose and xylotriose. Among them, glucuronoxylanase GH30 can exclusively hydrolyze the internal ${\beta}$-1,4-linkages of xylans decorated with methylglucuronic acid branches. In the present study, two xylanolytic enzyme (PaXN_10 and PaGuXN_30) genes were cloned from Paenibacillus amylolyticus KCTC 3005, and expressed in Escherichia coli, respectively. PaXN_10 (38.7 kDa) belongs to the endo-${\beta}$-xylanases GH10 family, while PaGuXN_30 (58.5 kDa) is a member of glucuronoxylanase GH30. They share the same optimal reaction conditions at $50^{\circ}C$ and pH 7.0. Enzymatic characterization proposed that P. amylolyticus can utilize the hardwood glucuronoarabinoxylans via the cooperative actions of xylanases GH10 and GH30. The extracellular PaGuXN_30 is secreted into the medium and hydrolyzes glucuronoarabinoxylans to release a series of aldouronic acid mixtures with a methylglucuronic acid branch. The resultant products being transported into the microbial cell are successively degraded into the smaller xylooligosaccharides by the intracellular PaXN_10, which will be utilized for the cellular metabolism.