Aggregation-induced emission enhancement (AIEE) of N,N′-Bis(Salicylidene)-p-Phenylenediamine Schiff base: Synthesis, photophysical properties and its DFT studies

บทความในวารสาร

ผู้เขียน/บรรณาธิการ

กลุ่มสาขาการวิจัยเชิงกลยุทธ์

ไม่พบข้อมูลที่เกี่ยวข้อง

รายละเอียดสำหรับงานพิมพ์

รายชื่อผู้แต่ง: Miengmern N., Koonwong A., Sriyab S., Suramitr A., Poo-arporn R.P., Hannongbua S., Suramitr S.

ผู้เผยแพร่: Springer

ปีที่เผยแพร่ (ค.ศ.): 2019

วารสาร: Applied Microbiology and Biotechnology (0175-7598)

Volume number: 210

Issue number: 5

หน้าแรก: 493

หน้าสุดท้าย: 500

จำนวนหน้า: 8

นอก: 0175-7598

eISSN: 1432-0614

URL: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85078363675&doi=10.1007%2fs00253-020-10388-3&partnerID=40&md5=1661ede3e2002a86a90f9380abf8120f

ภาษา: English-Great Britain (EN-GB)

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บทคัดย่อ

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.

คำสำคัญ

Carbohydrate-binding module family 3, Endo-/exotype enzyme, Glycoside hydrolase family 9, Oligosaccharide