Xylanases are a class of glycosidic hydrolases that catalyze the degradation of xylan, mainly derived from microorganisms such as Aspergillus niger, Their core function is to break the β-1,4 glycosidic bonds in the xylan molecule, converting the complex polysaccharide into xylooligosaccharides or monosaccharides. Xylanases are one of the key enzymes in xylan breakdown, and can be divided into endoxanthiases and exoxanthiases based on their mode of action. Endoxanthiases and exoxanthiases are mainly distinguished by their site of action, mode of hydrolysis, and main products.
1. Site of Action
Endoxanthiases: Attack the glycosidic bonds within the long xylan chain, not limited to the ends.
Exoxanthiases: Act only on the ends of the xylan chain, including reducing and non-reducing ends, without involving intra-chain bonds.
2. Mode of Hydrolysis
Endoxanthiases: Randomly break intra-chain glycosidic bonds, directly splitting the long-chain xylan into multiple short-chain fragments.
Exoxylanases: These enzymes hydrolyze glycosidic bonds sequentially from the ends, gradually shortening the xylan chain length; the hydrolysis process is continuous.
3. Main Products
Endoxylanases: Products are xylooligosaccharides of varying lengths, commonly a mixture of xylobiose to xylohexaose fragments.
Exoxylanases: Products are mainly xylobiose and xylotriose; some enzymes can directly generate xylose monosaccharides.
Endoxylanases act as the "initiator" of xylan degradation, breaking down the complexity of long-chain structures and creating more action sites for exoxylanases. Exoxylanases, acting as the "terminator," refine the degradation of short-chain xylans, improving the overall conversion rate of xylan. Only through the synergistic action of both can xylan be completely degraded.
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