N-Acetyl Glucosamine Obtained from Chitin by Chitin Degrading Factors in Chitinbacter tainanesis

Abstract

A novel chitin-degrading aerobe, Chitinibacter tainanensis, was isolated from a soil sample from southern Taiwan, and was proved to produce N-acetyl glucosamine (NAG). Chitin degrading factors (CDFs) were proposed to be the critical factors to degrade chitin in this work. When C. tainanensis was incubated with chitin, CDFs were induced and chitin was converted to NAG. CDFs were found to be located on the surface of C. tainanensis. N-Acetylglucosaminidase (NAGase) and endochitinase activities were found in the debris, and the activity of NAGase was much higher than that of endochitinase. The optimum pH of the enzymatic activity was about 7.0, while that of NAG production by the debris was 5.3. These results suggested that some factors in the debris, in addition to NAGase and endochitinase, were crucial for chitin degradation.

Characterization of extracellular chitinase from Chitinibacter sp. GC72 and its application in GlcNAc production from crayfish shell enzymatic degradation

“…In the present study, to evaluate the optimum reaction conditions for the obtained chitinase, the effect of pH and temperature on the chitinase was studied. The optimum pH for the chitinase was 6.8, with appreciable enzyme activity observed at pH ranging from 6.0 to 8.4, similar to that noted for the chitinase obtained from C. tainanensis [32]. With regard to pH stability, the optimum pH ranged from 6.8 to 7.6, and the residual enzyme activity was nearly 60% even at a pH of 8.0 (supplementary materials).…”

“…In the present study, the molecular mass of the purified chitinase was estimated to be approximately 65 kDa (Fig. 3b), as revealed by 12% SDS-PAGE, which is different from that of chitinase obtained from Neisseriaceae bacteria [31,32,36]. Furthermore, the apparent molecular mass of the activated chitinase was 130 kDa, indicated by a light yellow band in Fig.…”

“…The partial 16S rRNA gene sequence of strain GC72, published on NCBI (GenBank Accession No. KJ676516), showed the highest similarity of 99% with the type species of the genus Chitinibacter, Chitinibacter suncheonensis SK16 T [31], and 98% similarity with the second type species of the genus Chitinibacter, Chitinibacter tainanensis S1 T [32], suggesting that the isolated strain belonged to the genus Chitinibacter (Fig. 1b).…”

Occupational Exposure to Bioaerosols in Norwegian Crab Processing Plants

“…Because chitin is a major component of crustacean shell (Espie and Roff 1995) and NAGase is a widely distributed enzyme that digests chitin (Chen et al 2011) we would expect NAGase to be present in the processing plants. Our samples were collected in autumn/winter and the levels were higher than levels found in normal Danish homes at that time of year (Frankel et al 2012) so we expect the crab processing to be a contributor to the NAGase levels.…”

“…Endotoxin, a well-known pro-inflammatory mediator, has been confirmed to be present in crab processing plants (Neis 2004), but exposure levels have not been measured previously. Chitin, a polymer of β-(1-4)-linked N-acetylglucosamine (NAG) is present in the shell of crustaceans (Chen et al 2011). Since NAGase is an enzyme known to digest chitin, it is expected to be present in the bioaerosols during crab processing.…”