Fresh vegetables can be used as a source of antifungal lactic acid bacteria. Their exploitation as biopreservative will help in prolonging shelf-life of fresh vegetables.

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Biocatalysis, one of the oldest technologies, is becoming a favorable alternative to chemical processes and a vital part of green technology. It is an important revenue generating industry due to a global market projected at $7 billion in 2013 with a growth of 6.7% for enzymes alone. Some microbes are important sources of enzymes and are preferred over sources of plant and animal origin. As a result, more than 50% of the industrial enzymes are obtained from bacteria. The constant search for novel enzymes with robust characteristics has led to improvisations in the industrial processes, which is the key for profit growth. Actinomycetes constitute a significant component of the microbial population in most soils and can produce extracellular enzymes which can decompose various materials. Their enzymes are more attractive than enzymes from other sources because of their high stability and unusual substrate specificity. Actinomycetes found in extreme habitats produce novel enzymes with huge commercial potential. This review attempts to highlight the global importance of enzymes and extends to signify actinomycetes as promising harbingers of green technology.

Aim: Purification and characterization of a chitinase from Microbispora sp. V2. Methods and Results: The chitinase from Microbispora sp. V2 was purified to homogeneity by gel filtration chromatography with 4AE6% recovery. It had a molecular weight of 35 kDa and showed maximum activity towards p-nitrophenyl-b-D D-N,N¢-diacetylchitobiose, indicating a chitobiosidase activity. The enzyme had a pH optimum of 3AE0 and temperature optimum of 60°C. It was stable in a wide pH range from 3AE0 to 11AE0, retaining 61% activity at pH 3AE0 and 52% activity at pH 11AE0. It retained 71% activity at 30°C and 45% activity at 50°C, up to 24 h. The enzyme activity was not inhibited by any of the metal ions tested except Hg 2+ , in the presence of which only 10% activity was retained. Conclusions: The 35 kDa chitinase from Microbispora sp. V2 has an acidic pH optimum and a high temperature optimum. It is fairly stable and active, and degrades chitin efficiently, although the growth of the culture and enzyme production is slow. Significance and Impact of the Study: This report is the first detailed study of a chitinase from Microbispora sp. V2, isolated from hot springs. The chitinase from Microbispora sp. V2 may have potential applications in the recycling of chitinous wastes, particularly due to its thermophilic and acidophilic character. Studies at molecular level may provide further insight on the chitinolytic system of Microbispora spp. with respect to the number and types of chitinases and their regulation.