Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 67, Issue 24, Pages 6847-6855Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.9b01608
Keywords
chitosanase; carbohydrate binding module; chitooligosaccharide; one-step immobilization-purification; packed-bed reactor
Funding
- National Natural Science Foundation of China [31701537]
- Shu Guang Project of Shanghai Municipal Education Commission [15SG28]
- Chen Guang Project of Shanghai Municipal Education Commission [17CG28]
- Shanghai Education Development Foundation
- Shanghai Sailing Program [17YF1403500]
- Fundamental Research Funds for the Central Universities [222201814031, 22221818014]
- National Key Research and Development Program of China [2018YFC0311200]
- 111 Project [B18022]
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Chitooligosaccharide has been reported to possess diverse bioactivities. The development of novel strategies for obtaining optimum degree of polymerization (DP) chitooligosaccharides has become increasingly important. In this study, two glycoside hydrolase family 46 chitosanases were studied for immobilization on curdlan (insoluble beta-1,3-glucan) using a novel carbohydrate binding module (CBM) family 56 domain from a beta-1,3-glucanase. The CBM56 domain provided a spontaneous and specific sorption of the fusion proteins onto a curdlan carrier, and two fusion enzymes showed increased enzyme stability in comparison with native enzymes. Furthermore, a continuous packed-bed reactor was constructed with chitosanase immobilized on a curdlan carrier to control the enzymatic hydrolysis of chitosan. Three chitooligosaccharide products with different molecular weights were prepared in optimized reaction conditions. This study provides a novel CBM tag for the stabilization and immobilization of enzymes. The controllable hydrolysis strategy offers potential for the industrial-scale preparation of chitooligosaccharides with different desired DPs.
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