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Endo-type chitinase is the principal enzyme involved in the breakdown of  N -acetyl- d -glucosamine-based oligomeric and polymeric materials through hydrolysis. The gene (966-bp) encoding a novel endo-type chitinase (ChiJ), which is comprised of an N-terminal chitin-binding domain type 3 and a C-terminal catalytic glycoside hydrolase family 19 domain, was identified from a fibrolytic intestinal symbiont of the earthworm  Eisenia fetida ,  Cellulosimicrobium funkei  HY-13. The highest endochitinase activity of the recombinant enzyme (rChiJ: 30.0 kDa) toward colloidal shrimp shell chitin was found at pH 5.5 and 55 °C and was considerably stable in a wide pH range (3.5–11.0). The enzyme exhibited the highest biocatalytic activity (338.8 U/mg) toward ethylene glycol chitin, preferentially degrading chitin polymers in the following order: ethylene glycol chitin > colloidal shrimp shell chitin > colloidal crab shell chitin. The enzymatic hydrolysis of  N -acetyl-β- d -chitooligosaccharides with a degree of polymerization from two to six and colloidal shrimp shell chitin yielded primarily  N,N  ′ -diacetyl-β- d -chitobiose together with a small amount of  N -acetyl- d -glucosamine. The high chitin-degrading ability of inverting rChiJ with broad pH stability suggests that it can be exploited as a suitable biocatalyst for the preparation of  N,N  ′ -diacetyl-β- d -chitobiose, which has been shown to alleviate metabolic dysfunction associated with type 2 diabetes.

Novel Bi-Modular GH19 Chitinase with Broad pH Stability from a Fibrolytic Intestinal Symbiont of Eisenia fetida, Cellulosimicrobium funkei HY-13