Rational pH-engineering of the thermostable xylanase based on computational model

Liu, Liangwei; Wang, Bao; Chen, Hongge; Wang, Suya; Wang, Mingdao; Zhang, Shimin; Song, Andong; Shen, Jinwen; Wu, Kun; Jia, Xuchao

doi:10.1016/j.procbio.2009.02.013

Cited by 12 publications

(3 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The best hits at each site were then recombined one by one in a stepwise process. After screening 8 × 10 3 clones a mutant was produced with T 50 60 (temperature required to reduce the initial enzymatic activity by 50% within 60 minutes) of 93°C compared to 48°C of the WT. Highly mobile amino acids with the highest B-factors in B. subtilis lipase A are shown as sticks and can be selected as hotspots to design more thermostable enzyme variants according to [35].…”

Section: Stochastic Approachesmentioning

confidence: 99%

“…A larger number of salt bridges was suggested as a key factor that contributes to stability under extreme pH. Consequently, switching from basic to acidic amino acids was used to improve the charge balance and stability under acidic conditions, and vice versa, in various enzymes -α-amylase from B. subtilis [59], xylanase B from Thermotoga maritima [60], xylanase C from Aspergillus kawachii [61], alkaline cellulase K [62], and M-protease [63].…”

Section: Empirical Rational Designmentioning

confidence: 99%

See 1 more Smart Citation

Robust enzyme design: Bioinformatic tools for improved protein stability

Suplatov

Voevodin

Švedas

2014

Biotechnology Journal

View full text Add to dashboard Cite

The ability of proteins and enzymes to maintain a functionally active conformation under adverse environmental conditions is an important feature of biocatalysts, vaccines, and biopharmaceutical proteins. From an evolutionary perspective, robust stability of proteins improves their biological fitness and allows for further optimization. Viewed from an industrial perspective, enzyme stability is crucial for the practical application of enzymes under the required reaction conditions. In this review, we analyze bioinformatic-driven strategies that are used to predict structural changes that can be applied to wild type proteins in order to produce more stable variants. The most commonly employed techniques can be classified into stochastic approaches, empirical or systematic rational design strategies, and design of chimeric proteins. We conclude that bioinformatic analysis can be efficiently used to study large protein superfamilies systematically as well as to predict particular structural changes which increase enzyme stability. Evolution has created a diversity of protein properties that are encoded in genomic sequences and structural data. Bioinformatics has the power to uncover this evolutionary code and provide a reproducible selection of hotspots - key residues to be mutated in order to produce more stable and functionally diverse proteins and enzymes. Further development of systematic bioinformatic procedures is needed to organize and analyze sequences and structures of proteins within large superfamilies and to link them to function, as well as to provide knowledge-based predictions for experimental evaluation.

show abstract

Section: Stochastic Approachesmentioning

confidence: 99%

Section: Empirical Rational Designmentioning

confidence: 99%

Robust enzyme design: Bioinformatic tools for improved protein stability

Suplatov

Voevodin

Švedas

2014

Biotechnology Journal

View full text Add to dashboard Cite

show abstract

“…It was also shown that replacing a basic amino acid with an acidic one improved the protein stability and catalytic efficiency under an acidic environment ( Yang et al, 2013 ). And vice versa, replacing acidic residues with less acidic or more basic (like glutamic acid with glutamine) led to a change of the pH optima ( Suplatov et al, 2014 ; Fushinobu et al, 1998 ; Liu et al, 2009 ). Additional potential strategy for both pH adaptation and salinity adaptation is pKa modulation ( Beliën et al, 2009 ; Xu et al, 2013 ; Gutteridge and Thornton, 2005 ; Francois et al, 2006 ; Andreeva and James, 1991 ).…”

Section: Introductionmentioning

confidence: 99%

Living in trinity of extremes: Genomic and proteomic signatures of halophilic, thermophilic, and pH adaptation

Amangeldina,

Tan,

Berezovsky

2024

Current Research in Structural Biology

View full text Add to dashboard Cite

Properties and applications of microbial β-D-xylosidases featuring the catalytically efficient enzyme from Selenomonas ruminantium

Jordan

Wagschal

2010

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Xylan 1,4-beta-D-xylosidase catalyzes hydrolysis of non-reducing end xylose residues from xylooligosaccharides. The enzyme is currently used in combination with beta-xylanases in several large-scale processes for improving baking properties of bread dough, improving digestibility of animal feed, production of D-xylose for xylitol manufacture, and deinking of recycled paper. On a grander scale, the enzyme could find employment alongside cellulases and other hemicellulases in hydrolyzing lignocellulosic biomass so that reaction product monosaccharides can be fermented to biofuels such as ethanol and butanol. Catalytically efficient enzyme, performing under saccharification reactor conditions, is critical to the feasibility of enzymatic saccharification processes. This is particularly important for beta-xylosidase which would catalyze breakage of more glycosidic bonds of hemicellulose than any other hemicellulase. In this paper, we review applications and properties of the enzyme with emphasis on the catalytically efficient beta-D-xylosidase from Selenomonas ruminantium and its potential use in saccharification of lignocellulosic biomass for producing biofuels.

show abstract

Rational pH-engineering of the thermostable xylanase based on computational model

Cited by 12 publications

References 25 publications

Robust enzyme design: Bioinformatic tools for improved protein stability

Robust enzyme design: Bioinformatic tools for improved protein stability

Living in trinity of extremes: Genomic and proteomic signatures of halophilic, thermophilic, and pH adaptation

Properties and applications of microbial β-D-xylosidases featuring the catalytically efficient enzyme from Selenomonas ruminantium

Contact Info

Product

Resources

About