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Chitinases


Chitinases by Creative Enzymes

Chitinases are enzymes that catalyze the degradation of chitin. They have been detected in many organisms, including bacteria, fungi, plants, invertebrates and vertebrates. Chitinases are broadly classified as endo- and exochitinases. The combination of endo- and exochitinases results in a synergistic increase in the chitinolytic activity. Chitinases are widely used in research and industrial applications. For example, DIS-1010 can be used in food industry for extraction of chitosan or digestion of seafood shells; NATE-0124 has been used in a study to investigate the differential release of high mannose structural isoforms by fungal and bacterial endo-β-N-acetylglucosaminidases. Furthermore, NATE-0124 has also been used in a study to investigate a hevein-like protein and a class I chitinase with antifungal activity from leaves of the paper mulberry.

Chitinase Selection Guide

Cat. No Product Name  
DIS-1010 Chitinase from Aspergillus niger
A food-grade product
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NATE-0123 Native Streptomyces griseus Chitinase
For studying the effect of the allosamidin on the regulatory system.
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NATE-0124 Native Trichoderma viride Chitinase
For studing a hevein-like protein and a class I chitinase with antifungal activity from leaves of the paper mulberry.
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NATE-1201 Chitinase from Clostridium thermocellum, Recombinant Get a quote
NATE-1377 Chitinase 18A from Bacillus cereus, Recombinant Get a quote
NATE-1378 Chitinase 18A from Bacillus licheniformis, Recombinant Get a quote
NATE-1379 Chitinase 18A from Clostridium thermocellum, Recombinant Get a quote
CSUB-0159 4-Nitrophenyl N,N'-diacetyl-β-D-chitobioside
A reagent for biochemical assays of chitinases
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CSUB-0160 Chitin azure
A substrate for photospectrometric assays of chitinases
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Supported by the outstanding research team, Creative Enzymes provide various Chitinases for a variety of applications. To discuss the details of these products, please call 1-631-562-8517 or e-mail us at: info@creative-enzymes.com, or use our contact page: Contact.

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