A novel GH6 cellobiohydrolase from Paenibacillus curdlanolyticus B-6 and its synergistic action on cellulose degradation

被引：20

作者：

Baramee, Sirilak ^{[1
]}

Teeravivattanakit, Thitiporn ^{[1
]}

Phitsuwan, Paripok ^{[1
]}

Waeonukul, Rattiya ^{[2
]}

Pason, Patthra ^{[2
]}

Tachaapaikoon, Chakrit ^{[2
]}

Kosugi, Akihiko ^{[3
]}

Sakka, Kazuo ^{[4
]}

Ratanakhanokchai, Khanok ^{[1
]}

机构：

[1] King Mongkuts Univ Technol Thonburi, Sch Bioresources & Technol, Bangkok 10150, Thailand

[2] King Mongkuts Univ Technol Thonburi, Pilot Plant Dev & Training Inst, Bangkok 10150, Thailand

[3] Japan Int Res Ctr Agr Sci, Biol Resources & Postharvest Div, Tsukuba, Ibaraki 3058686, Japan

[4] Mie Univ, Grad Sch Bioresources, Tsu, Mie 5148507, Japan

来源：

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 2017年 / 101卷 / 03期

关键词：

Cellobiohydrolase; Cellulose degradation; Endoglucanase; beta-Glucosidase; Glycoside hydrolase family 6; Paenibacillus curdlanolyticus; CLOSTRIDIUM-THERMOCELLUM; TRICHODERMA-REESEI; THERMOANAEROBACTER-BROCKII; FAMILY; HYDROLYSIS; CELLULASES; ENZYMES; BINDING; CLONING; GENE;

D O I：

10.1007/s00253-016-7895-8

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

We recently discovered a novel glycoside hydrolase family 6 (GH6) cellobiohydrolase from Paenibacillus curdlanolyticus B-6 (PcCel6A), which is rarely found in bacteria. This enzyme is a true exo-type cellobiohydrolase which exhibits high substrate specificity on amorphous cellulose and low substrate specificity on crystalline cellulose, while this showed no activity on substitution substrates, carboxymethyl cellulose and xylan, distinct from all other known GH6 cellobiohydrolases. Product profiles, HPLC analysis of the hydrolysis products and a schematic drawing of the substrate-binding subsites catalysing cellooligosaccharides can explain the new mode of action of this enzyme which prefers to hydrolyse cellopentaose. PcCel6A was not inhibited by glucose or cellobiose at concentrations up to 300 and 100 mM, respectively. A good synergistic effect for glucose production was found when PcCel6A acted together with processive endoglucanase Cel9R from Clostridium thermocellum and beta-glucosidase CglT from Thermoanaerobacter brockii. These properties of PcCel6A make it a suitable candidate for industrial application in the cellulose degradation process.

引用

页码：1175 / 1188

页数：14

共 52 条

[1] A novel thermophilic β-glucosidase from Caldicellulosiruptor bescii: Characterization and its synergistic catalysis with other cellulases [J].