Aggregation-induced emission enhancement (AIEE) of N,N′-Bis(Salicylidene)-p-Phenylenediamine Schiff base: Synthesis, photophysical properties and its DFT studies
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Author list: Miengmern N., Koonwong A., Sriyab S., Suramitr A., Poo-arporn R.P., Hannongbua S., Suramitr S.
Publisher: Springer
Publication year: 2019
Journal: Applied Microbiology and Biotechnology (0175-7598)
Volume number: 210
Issue number: 5
Start page: 493
End page: 500
Number of pages: 8
ISSN: 0175-7598
eISSN: 1432-0614
Languages: English-Great Britain (EN-GB)
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Abstract
PcMulGH9, a novel glycoside hydrolase family 9 (GH9) from Paenibacillus curdlanolyticus B-6, was successfully expressed in Escherichia coli. It is composed of a catalytic domain of GH9, two domains of carbohydrate-binding module family 3 (CBM3) and two domains of fibronectin type 3 (Fn3). The PcMulGH9 enzyme showed broad activity towards the β-1,4 glycosidic linkages of cellulose, mannan and xylan, including cellulose and xylan contained in lignocellulosic biomass, which is rarely found in GH9. The enzyme hydrolysed substrates with bifunctional endo-/exotypes cellulase, mannanase and xylanase activities, but predominantly exhibited exo-activities. This enzyme released cellobiose as a major product from cellohexaose, while mannotriose and xylotriose were major hydrolysis products from mannohexaose and xylohexaose, respectively. Moreover, PcMulGH9 could hydrolyse untreated corn hull and rice straw into xylo- and cello-oligosaccharides. Enzyme kinetics, site-directed mutagenesis and molecular docking revealed that Met394, located at the binding subsite + 2, was involved in broad substrate specificity of PcMulGH9 enzyme. This study offers new knowledge of the multifunctional cellulase/mannanase/xylanase in GH9. The PcMulGH9 enzyme showed a novel function of GH9, which increases its potential for saccharification of lignocellulosic biomass into value-added products, especially oligosaccharides. © 2020, Springer-Verlag GmbH Germany, part of Springer Nature.
Keywords
Carbohydrate-binding module family 3, Endo-/exotype enzyme, Glycoside hydrolase family 9, Oligosaccharide
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