High-level expression of an engineered β-mannanase (mRmMan5A) in Pichia pastoris for manno-oligosaccharide production using steam explosion pretreated palm kernel cake

Li, Yanxiao; Yi, Ping; Li, Jun; Yan, Qiaojuan; Jiang, Zhengqiang

doi:10.1016/j.biortech.2018.01.138

Cited by 55 publications

(27 citation statements)

References 42 publications

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“…After cultivation for approximately 168 h, the enzyme activity reached 17 500 U ml −1 culture. This level was apparently higher than the strains of Aspergillus flavus generated by the UV mutagenesis method (Olaniyi et al ), and also higher than those simply cloning mannanase genes from A. niger and Rhizomucor miehei and heterologously expressed in P. pastoris (Do et al ; Li et al ), and even higher than the structure‐based rational design mannanase from A. niger (Huang et al ).…”

Section: Discussionmentioning

confidence: 89%

“…from natural environments, UV-mediated mutagenesis and optimizing cultivation conditions have been used to acquire strains that produce high levels of mannanase (Olaniyi et al 2014;Elsharouny et al 2015;Shimizu et al 2015;Ahirwar et al 2016). Currently, genetic engineering techniques are more popularly used by researchers for microbe breeding (Mao and Zhang 2006;Huang et al 2014;Li et al 2018), and improving the gene dosage in the host genome has been proven to be an efficient method to obtain a high expression level of the target gene (Men endez et al 2000;Shu et al 2016).…”

Section: Introductionmentioning

confidence: 99%

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Manno‐oligosaccharide preparation by the hydrolysis of konjac flour with a thermostable endo‐mannanase from Talaromyces cellulolyticus

Yang

Chen

Zhou

et al. 2019

J of Applied Microbiology

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Aims A thermostable endo‐mannanase from the fungus Talaromyces cellulolyticus was identified to facilitate manno‐oligosaccharide preparation from Konjac (Amorphophallus konjac) flour. Methods and Results A putative endo‐1,4‐β‐mannanase from the T. cellulolyticus was obtained and efficiently expressed by improving its gene dosage in the genome of the host. After cultivation in a bench‐top bioreactor for about 120 h, the protein content and enzyme activity of mannanase increased to 3·4 g l−1 and 17 500 U ml−1 respectively. Enzymatic characterization showed that this enzyme has an optimal temperature of 80°C, optimal pH of 5·0. Under the optimized hydrolysis conditions of pH 5·0, 70°C, and an enzyme concentration of 200 U l−1 solution, this enzyme could efficiently hydrolyse 0·5% konjac flour into manno‐oligosaccharides (MOSs) with the degree of polymerization range from 3 to 7. The possible mechanism by which the enzyme produced MOSs was also discussed. Conclusion Talaromyces cellulolyticus endo‐mannanase is thermostable and has a broad pH range adaptability. Method of improving the dosage of mannanase gene in the genome could realized its high‐level impression. This enzyme could efficiently hydrolyse konjac flour into manno‐oligosaccharide products. Significance and Impact of the Study This study has enriched endo‐mannanase resources, facilitated its bulk production and provided a strong reference for its application in manno‐oligosaccharide preparation from the natural glucomannan of konjac flour.

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Section: Discussionmentioning

confidence: 89%

Section: Introductionmentioning

confidence: 99%

Manno‐oligosaccharide preparation by the hydrolysis of konjac flour with a thermostable endo‐mannanase from Talaromyces cellulolyticus

Yang

Chen

Zhou

et al. 2019

J of Applied Microbiology

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“…P. pastoris has been widely used to produce heterologous protein with its advantages of secretory expression with less background extracellular protein [11]. Recently, multiple strategies have been developed for efficient expression of heterologous protein in P. pastoris, such as optimizing the expression vector, increasing the copy number of target gene, co-expressing molecular chaperone, optimizing the fermentation conditions, and so on [12,13].…”

Section: Introductionmentioning

confidence: 99%

Multiple strategies to improve the yield of chitinase a from Bacillus licheniformis in Pichia pastoris to obtain plant growth enhancer and GlcNAc

et al. 2020

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Chitinase and chitin-oligosaccaride can be used in multiple field, so it is important to develop a high-yield chitinase producing strain. Here, a recombinant Pichia pastoris with 4 copies of ChiA gene from Bacillus licheniformis and co-expression of molecular chaperon HAC1 was constructed. The amount of recombinant ChiA in the supernatant of high-cell-density fermentation reaches a maximum of 12.7 mg/mL, which is 24-fold higher than that reported in the previous study. The recombinant ChiA can hydrolyze 30% collodidal chitin with 74% conversion ratio, and GlcNAc is the most abundant hydrolysis product, followed by N, N′-diacetylchitobiose. Combined with BsNagZ, the hydrolysate of ChiA can be further transformed into GlcNAc with 88% conversion ratio. Additionally, the hydrolysate of ChiA can obviously accelerate the germination growth of rice and wheat, increasing the seedling height and root length by at least 1.6 folds within 10 days.

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“…Furthermore, hemicellulose is the second most abundant component of lignocellulose and is mainly composed of xylan, mannan, and xyloglucan. Hemicelluloses can be hydrolyzed into pentoses (xylose and arabinose) and hexoses (glucose, mannose and galactose) at high yield which is important for bio-refinery applications [37,38]. Besides the enzymes degrading the main chains of the structural polysaccharides in plant cell walls, various glycosidases have been found to be essential for obtaining fermentable sugars from lignocellulose [39].…”

Section: Discussionmentioning

confidence: 99%

“…One unit of enzyme activity was defined as the amount of enzyme that produced 1 µmol of pNP in 1 min from the substrate under the above conditions. In addition, β-mannase activity (Man) was determined by the DNS method using mannose as the standard according to the methods of Li et al [38]. The amylolytic activity (Amy) was assayed by the DNS method using maltose as the standard as reported by He et al [58].…”

Section: Enzymatic Assaysmentioning

confidence: 99%

Low-Cost Cellulase-Hemicellulase Mixture Secreted by Trichoderma harzianum EM0925 with Complete Saccharification Efficacy of Lignocellulose

Zhang

Yang

Luo

et al. 2020

IJMS

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Fermentable sugars are important intermediate products in the conversion of lignocellulosic biomass to biofuels and other value-added bio-products. The main bottlenecks limiting the production of fermentable sugars from lignocellulosic biomass are the high cost and the low saccharification efficiency of degradation enzymes. Herein, we report the secretome of Trichoderma harzianum EM0925 under induction of lignocellulose. Numerously and quantitatively balanced cellulases and hemicellulases, especially high levels of glycosidases, could be secreted by T. harzianum EM0925. Compared with the commercial enzyme preparations, the T. harzianum EM0925 enzyme cocktail presented significantly higher lignocellulolytic enzyme activities and hydrolysis efficiency against lignocellulosic biomass. Moreover, 100% yields of glucose and xylose were obtained simultaneously from ultrafine grinding and alkali pretreated corn stover. These findings demonstrate a natural cellulases and hemicellulases mixture for complete conversion of biomass polysaccharide, suggesting T. harzianum EM0925 enzymes have great potential for industrial applications.

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High-level expression of an engineered β-mannanase (mRmMan5A) in Pichia pastoris for manno-oligosaccharide production using steam explosion pretreated palm kernel cake

Cited by 55 publications

References 42 publications

Manno‐oligosaccharide preparation by the hydrolysis of konjac flour with a thermostable endo‐mannanase from Talaromyces cellulolyticus

Manno‐oligosaccharide preparation by the hydrolysis of konjac flour with a thermostable endo‐mannanase from Talaromyces cellulolyticus

Multiple strategies to improve the yield of chitinase a from Bacillus licheniformis in Pichia pastoris to obtain plant growth enhancer and GlcNAc

Low-Cost Cellulase-Hemicellulase Mixture Secreted by Trichoderma harzianum EM0925 with Complete Saccharification Efficacy of Lignocellulose

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