Chitinase A from Stenotrophomonas maltophilia shows transglycosylation and antifungal activities

Cloning, expression, purification and application of a novel chitinase from a thermophilic marine bacterium Paenibacillus barengoltzii

“…This property is similar to those of several GH family 18 endochitinases from bacteria such as B. licheniformis (Songsiriritthigul et al, 2010), C. shinanonensis (Huang et al, 2012), and S. antarcticus (Lee et al, 2010). However, the chitinase from S. maltophilia was found to hydrolyse colloidal chitin yielding longer chain N-acetyl COSs, and on extended time it hydrolyzed (GlcNAc) 2 (Suma & Podile, 2013). The chitinase from Pennahia argentatus does not exhibit activity towards (GlcNAc) 2 and (GlcNAc) 3 (Ikeda, Miyauchi, Mochizuki, & Matsumiya, 2009).…”

“…(30 °C) (Bendt et al, 2001), S. antarcticus (37 °C) (Lee et al, 2010), and S. maltophilia (40 °C) (Suma & Podile, 2013). However, the optimal temperature of PbChi70 is lower than those of several chitinases from B. cereus IO8 (65 °C, Hammami et al, 2013), B. licheniformis (65 °C) (Sandalli et al, 2008), and T. chitonophagus (80 °C) (Andronopoulou & Vorgias, 2004).…”

“…Most other bacterial chitinases are optimally active at neutral pH 6.0-7.0 (Hammami et al, 2013;Sandalli et al, 2008;Songsiriritthigul et al, 2010;Suma & Podile, 2013). In addition, there are several chitinases which are optimally active at alkaline pH 7.5-9.0 (Bendt et al, 2001;Lee et al, 2010).…”

Purification and biochemical characterization of novel acidic chitinase from Paenicibacillus barengoltzii

“…The chitinase from Stenotrophomonas maltophilia hydrolyzed colloidal chitin to yield N-acetyl COSs with higher DPs, and further converted (GlcNAc)2 to its monomer [40], while the Pennahia argentatus chitinase exhibited no activity towards (GlcNAc)3 as well as (GlcNAc)2 [41]. The unique enzymatic properties may enable this enzyme as great potential in industrial applications, such as production of functional N-acetyl chitooligosaccharides in food or pharmaceutically industries and biodegradation of chitin waste in environmental protection field.…”

Purification, characterization, and molecular cloning of an extracellular chitinase from Bacillus licheniformis stain LHH100 isolated from wastewater samples in Algeria

“…N-acetylglucosaminases hydrolyze GlcNAc 2 into GlcNAc or produce GlcNAc from the nonreducing end of Nacetyl-chitooligosaccharides [7]. To date, various chitinases have been isolated from some microorganism such as B. cereus [8], B. licheniformis [9], and Stenotrophomonas maltophilia [10]. The chitinases so far sequenced are classified into two glycosyl hydrolase families, family 18 and 19, on the basis of the homology of their amino acid sequences and their catalytic mechanisms [11].…”