High level expression of a novel β-mannanase from Chaetomium sp. exhibiting efficient mannan hydrolysis

Katrolia, Priti; Zhou, Peng; Zhang, Pan; Yan, Qiaojuan; Li, Yinan; Jiang, Zhengqiang; Xu, Hui

doi:10.1016/j.carbpol.2011.08.008

Cited by 58 publications

(24 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The k cat /K m of the three mutants was significantly improved compared to ManAK. This was superior to the previously reported catalytic efficiency of mannanases, such as those from Penicillium canescens ( Sinitsyna et al, 2008 ) and Rhizomucor miehei ( Katrolia et al, 2012 ). The substrate affinity of the three mutants was greatly enhanced due to the significant decrease in K m values, which might increase the k cat /K m values.…”

Section: Discussioncontrasting

confidence: 75%

Improvement of the Catalytic Ability of a Thermostable and Acidophilic β-Mannanase Using a Consensus Sequence Design Strategy

et al. 2021

View full text Add to dashboard Cite

In order to improve the catalytic efficiency of a thermostable and acidophilic β-mannanase (ManAK; derived from marine Aspergillus kawachii IFO 4308), three mutants were designed by amino acid sequence consensus analysis with a second β-mannanase (ManCbs), which also belongs to the glycoside hydrolase family 5 (GH5) and has excellent catalytic efficiency. Three mutants were constructed and their biochemical characteristics were measured after heterologous expression in Pichia pastoris. The results revealed that the kcat/Km values of the three recombinant mannanases ManAKC292V, ManAKL293V, and ManAKL294H were enhanced by 303.0, 280.4, and 210.1%, respectively. Furthermore, ManAKL293V showed greater thermostability than ManAK, retaining 36.5% of the initial enzyme activity after incubation at 80°C for 5min. This study therefore provides a rational design strategy based on consensus sequence analysis to develop industrially valuable β-mannanase for future applications in marine aquafeed.

show abstract

Section: Discussioncontrasting

confidence: 75%

Improvement of the Catalytic Ability of a Thermostable and Acidophilic β-Mannanase Using a Consensus Sequence Design Strategy

et al. 2021

View full text Add to dashboard Cite

show abstract

“…Most mannanases, especially those from Bacillus subtilis, are apparently stable at 40 to 60 o C, but inactive or nearly inactive at low temperature (Katrolia et al, 2012;Kim et al, 2011;Pan et al, 2011;Benech et al, 2007). Up to date, only about ten low-temperature or cold-active β-mannanases have been reported.…”

Section: Discussionmentioning

confidence: 99%

A low-temperature active endo-β-1,4-mannanase from Bacillus subtilis TD7 and its gene expression in Escherichia coli

Liu

Jiang

et al. 2018

Appl Env Biotechnol

View full text Add to dashboard Cite

A low-temperature active endo-β-1,4-mannanase (YBMan) from Bacillus subtilis TD7 was isolated, characterized and successfully expressed in Escherichia coli to enhance the yield of mannanase for a potential application as a gel-breaker in guar gum-based fracturing fluids in oilfields. YBMan showed good compatibility with a wide temperature range and retained about 70% relative activity at 20 o C compared to its optimal temperature (65 o C). This is the highest relative activity among reported low-temperature active mannanases against guar gum. The gene (1104 bp) of strain TD7 coding a protein with 367 amino acid residues was cloned and its expression generated two recombinant mannanases, TBMan-1 and TBMan-2. Compared to the wild type, the protein yield of TBMan-1 from a one-liter shake flask broth increased 5.6-fold, and the specific activity (crude enzyme) increased 6.4-fold. The total enzyme activity increased 35.8-fold with a total activity of approximately 79550 U. Moreover, TBMan-1 had at 20 o C still about 80% relative activity. The enzyme was evaluated also for its application as gel-breaker and showed excellent ability for viscosity reduction with guar gum at 20 o C. Low-temperature activity and high yield make the recombinant β-mannanase attractive for applications with guar-based hydraulic fracturing fluids and other biotechnological aspects.

show abstract

“…However, the highest titers of β-mannanase have been reported from Rhizomucor miehei (79,680 U mL −1) and Chaetomium sp. CQ31 (50,030 U/ml) following cloning and expression of their β-mannanase enzyme gene in Pichia pastoris (Katrolia et al, 2012;Li et al, 2018).…”

Section: Production Yield Improvement and Purification Of β-Mannanasesmentioning

confidence: 99%

Applications of Microbial β-Mannanases

Dawood

2020

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

Mannans are main components of hemicellulosic fraction of softwoods and they are present widely in plant tissues. β-mannanases are the major mannan-degrading enzymes and are produced by different plants, animals, actinomycetes, fungi, and bacteria. These enzymes can function under conditions of wide range of pH and temperature. Applications of β-mannanases have therefore, been found in different industries such as animal feed, food, biorefinery, textile, detergent, and paper and pulp. This review summarizes the most recent studies reported on potential applications of β-mannanases and bioengineering of β-mannanases to modify and optimize their key catalytic properties to cater to growing demands of commercial sectors.

show abstract

High level expression of a novel β-mannanase from Chaetomium sp. exhibiting efficient mannan hydrolysis

Cited by 58 publications

References 36 publications

Improvement of the Catalytic Ability of a Thermostable and Acidophilic β-Mannanase Using a Consensus Sequence Design Strategy

Improvement of the Catalytic Ability of a Thermostable and Acidophilic β-Mannanase Using a Consensus Sequence Design Strategy

A low-temperature active endo-β-1,4-mannanase from Bacillus subtilis TD7 and its gene expression in Escherichia coli

Applications of Microbial β-Mannanases

Contact Info

Product

Resources

About