Special Issue "Modular Structures of Carbohydrate-Active Enzymes and Their Applications"
Deadline for manuscript submissions: 20 August 2022 | Viewed by 408
Interests: lignin conversion; biomass pretreatment and characterization; lignin and carbohydrate active enzyme
The bioconversion of lignocellulosic biomass into simple sugars for subsequent fermentation is an essential platform for the sustainable production of biofuels and biochemicals. However, the degradation of polysaccharides in biomass to sugar is difficult, and it has become a rate-limiting step in the industrial process.
The crystallinity and insoluble forms of polysaccharides appear to be a barrier for enzymatic hydrolysis. Several studies have shown that carbohydrate-active enzymes, i.e., cellulases and xylanases, have modular structures, making the enzymes more active on the insoluble substrate than a single-catalytic domain enzyme. The additional modules include carbohydrate-binding modules (CBMs), fibronectin-like domains, and other modules with unknown functions. The functions of CBMs are to bring the enzymes to the insoluble substrate, concentrate the enzyme on the substrate surfaces, and prolong the adsorption. Fibronectin-like domains have been reported to be involved in anchoring enzymes to the large substrates or stabilizing the entire protein structure, for example. These modules are linked with a catalytic module(s) via short-peptide linkers to make the enzyme(s) modular, and the linkers are glycosylated to prevent proteolytic cleavage. The linkers are also believed to promote polysaccharide binding during catalysis.
Interestingly, some microorganisms develop their sophisticated enzyme system to degrade the crystalline form of polysaccharides efficiently. For example, the multienzyme “cellulosome” has shown the efficient degradation of crystalline cellulose. Additionally, it contains enzyme components that actively degrade other polysaccharides, including xylan, starch, pectin, and mannan. Cellulosomal enzymes have a specialized module called dockerin, which interacts with the cohesin on the scaffolding protein. The assembly of the enzymes into the complex leads to enzyme proximity and synergy among the enzymes. However, mimicking the complex formation of the naturally occurring cellulosome complex is difficult. The limitations include an efficient protein expression system, proper glycosylation, protein folding, and ways to choose enzymes and orders of the enzymes for construction.
This Special Issue focuses on the modular structure of carbohydrate-active enzymes, the architecture of the entire protein structures, and their biological functions during catalysis. We welcome the submission of research articles, reviews, and perspectives related, but not limited to, the following themes of interest:
- Protein expression and development of hosts for expressing enzymes
- Enzymology of carbohydrates active enzymes and the cellulosome system
- Application of CBMs in protein purification, biomass characterization, or biomarker/reporter
- Application of carbohydrate-active enzymes in agriculture, food, feed, and the biofuel/chemical industry
- Modular structures and substrate–enzyme interactions
- Techniques for increasing enzymatic activity and stability
- Computational tools for designing enzymes
- Effects of pretreatment methods on biomass structure and enzymactic acitivity
Dr. Paripok Phitsuwan
Dr. Ken-Lin Chang
Manuscript Submission Information
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- plant biomass
- circular bioeconomy
- green solvent
- gene manipulation
- enzyme kinetics
- molecular docking
- protein assembly
- polysaccharide degradation
- binding interaction