Chitin, the most abundant bio-polymer in seawater, may be utilized by various microorganisms as a carbon source. Vibrios have been regarded one of main groups chitin consumers marine cycle and chitinase producers. The organisms are widely distributed aquatic environment. However, co-working mechanism between their chitinases, whether chitinase’s diversity contributes to adaption environment, ne...

Abstract Background This study was carried out to investigate the antifungal activity of chitinase produced by Streptomyces species isolated from grassland soils against selected pathogenic fungi, namely: Magnaporthe oryzae , Fusarium graminearum Rhizoctonia solani Puccinia and Botyrtis cinerea . Chitinase albus purified consecutively with dialysis, gel filtration ion- exchange chromatography, ...

Shrimp shell waste are potential to be processed further into value-added products, such as N-acetylglucosamine (GlcNAc). In the production of GlcNAc, biological approach is preferred and environmentally friendly chemical treatment. Chitinase an enzyme that plays a vital role in bioprocessing shrimp GlcNAc. Previously, Bacillus cereus SMG 1.1 was isolated from fermented paste (terasi) showed ab...

Baculovirus chitinases and other family 18 glycohydrolases have been shown to possess both exo- and endochitinase activities when assayed against fluorescent chito-oligosaccharides. Homology modelling of the chitinase of Epiphyas postvittana nucleopolyhedrovirus (EppoNPV) against Serratia marcescens chitinase A indicated that the enzyme possesses an N-terminal polycystic kidney 1 (PKD1) domain ...

A chitinase-producing bacteria was locally isolated from rhinoceros beetle (Oryctes rhinoceros) larvae gut discovered in mushroom compost. strain selected the source and labeled as RBLG1. It identified using 16s rDNAsequencing has strong homology to Bacillus cereus. Chitinase produced RBLG1 purified ammonium sulfate precipitation, ion exchange chromatography, gel filtration. The chitinase shows...

A new chitinase inhibitor, CI-4, was isolated from the culture broth of a marine bacterium Pseudomonas sp. IZ208. The structure of CI-4 was determined to be cyclo(L-Arg-D-Pro) by spectral studies and comparison with a synthetic sample. CI-4 showed inhibitory activity against chitinase.

A chitinase isolated from Coccidioides immitis was subjected to amino-terminal protein sequence analysis. The resulting 18-amino-acid sequence was compared with the previously reported amino acid sequence of coccidioidal immunodiffusion-complement fixation (IDCF) antigen. From the homology of the two sequences, the results support the identification of the IDCF antigen with a chitinase.

A chitinase gene from Bacillus cereus was cloned and expressed in Escherichia coli. The purified recombinant chitinase had much higher (128 fold) specificity to pNP-beta-(GlcNAc)(3) than to pNP-beta-(GlcNAc), suggesting endochitinase. Thirty-three amino acids in the N-terminal were recognized and cut off during expression, which consequently made the M(r) not correspond to that predicted.

The first synthesis of the cyclopentapeptide family 18 chitinase inhibitor argifin has been achieved by a combination of solid phase and solution chemistry. Synthetic argifin is a nanomolar inhibitor of chitinase B1 from Aspergillus fumigatus and the high-resolution X-ray structure of the synthesized material in complex with the same enzyme is identical to that previously obtained for the natur...

The chiA gene from Aeromonas caviae encodes an extracellular chitinase, 865 amino acids long, that shows a high degree of similarity to chitinase A of Serratia marcescens. Expression in Escherichia coli yielded an enzymatically active protein from which a leader sequence was removed, presumably during transport of the enzyme across the cell membrane.