Chitinase production was observed under varying environmental conditions, i.e., pH (4-9), temperature (25-37 ºC) and agitation (150 and 200 rpm). Optimum pH, temperature and agitation for maximum enzyme production were 7.0-8.0, 30 ºC and 150 rpm, respectively. NaCl inclusion at 0.5% enhanced chitinase production by 35% in chitin minimal medium. Serratia marcescens GG5 inhibited the growth of Fusarium oxysporum, Rhizopus nigricans and Mucor rouxi on sabourouds agar medium supplemented with the 0.1% of swollen chitin.

Chitinases (EC 3.2.1.14) are glycosyl hydrolases that catalyze the hydrolytic degradation of chitin, an insoluble linear β-1,4-linked polymer of N-acetyl-D-glucosamine (GlcNAc) (Bhattacharya et al., 2007). Chitin is widely distributed in nature and forms a major constituent of the shells of crustaceans, such as crabs and shrimps, the exoskeletons of insects, and cell walls of a variety of fungi. After cellulose, chitin is the most abundant organic compound present on earth (Kurita, 2001). During the previous decade, chitinases have received increased attention because of their wide range of applications. Practical applications of chitinases include use in the preparation of protoplasts from fungi, as a protective agent against plant-pathogenic fungi, chito-oligomers produced by enzymatic hydrolysis of chitin have been of interest in recent years due to their broad applications in medical, agricultural and industrial applications, such as antibacterial, antifungal, hypocholesterolemic, antihypertensive activity, and as a food quality enhancer (Bhattacharya et al., 2007). Interest in chitin degrading enzymes and their application in control of fungal pathogens have advanced significantly, because chitin is a major structural component of fungal cell wall. Biological control of pathogenic fungi provides an attractive alternative for management of fungal disease without the negative impact of synthetic antifungal agents that can cause environmental pollution and may induce pathogen resistance (Chang et al., 2003). Chitinase researchers (Dahiya et al., 2005; Singh et al., 2005; and Singh et al., 2008). However, for commercial applications, chitinases should be produced rapidly and in high titre using simple and inexpensive substrates (Dahiya et al., 2005). Chitin bioconversion has been proposed as a waste treatment alternative to the disposal of shellfish waste and some pretreated chitin was used as substrate for the production of microbial chitinases (Wang et al., 2002).

Serratia marcescens GG5 was isolated from mushroom (Agaricus bisporous) stalk that was obtained from Amar Mushroom Farm, Haryana, India (Singh et al., 2005). The organism was maintained as a suspension in 20% glycerol at –70 °C and was routinely cultured on M9 medium (0.7% Na₂HPO₄, 0.3% KH₂PO₄, 0.1% NH₄Cl and 0.05% NaCl and pH 7.0) supplemented with 0.5% swollen chitin. The growth of the organism was measured by determining the absorbance at 600 nm. Before determination of absorbance, an aliquot was passed through a coarse grade sintered glass filter (G-2) which retained the particles of chitin but not bacteria.

Life Sciences Journal, Chitinase Production, Industrial Applications, Agricultural Applications, Medical Applications, Anti Fungal Compounds, Chitinolytic Enzyme, Fungal Diseases, Catalytic Properties, Antifungal Chitinases, Carbon Sources.