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NAM AND AHN Conclusion In this study, Hafnia alvei KNOUC302, a strain that produces lactose hydrolyzing enzyme at low temperature, was isolated from the samples of raw milk collected from dairy farms of Kyung-gi province in Korea. The results obtained in this study show that Hafnia alvei KNOUC302 grew optimally at 20 ºC and pH=7.0-7.2. The gene (KNOUC302 β- gal) consists of 918 bp encoding the protein of 306 amino acids and 34,806 Da of deduced Mw. In the search for cold-adapted β-galactosidase, we conclude that the β-D-galactosidase from Hafnia alvei KNOUC302 is a cold-active enzyme, and that the enzyme could have advantageous applications in the food industry, the treatment of chilled dairy products while avoiding flavor tainting and the risk of microbial contamination. References Fig. 3: DNA sequence of Hafnia alvei KNOUC302 β- galactosidase gene (KNOUC302β-gal) and deduced amino acid sequence. *The fragment from pRSET vector came from pRSET C, cloning vector. Bondarenko VM, Afanas’eva SM, Vasiurenko ZP (1982). Heterogeneity of the fatty acid composition of bacteria in the genera Klebsiella, Enterobacter, Hafnia and Serratia. Zurnal mikrobiologii I immunobiologii., 12 : 54-60. Brenner DJ, Farmer JJ (2005). Family I. Enterobacteriaceae. In: Bergey’s Manual of Systematic Bacteriology, Vol. 2, D.J. Brenner, N.R. Krieg, J.T. Staley(Eds.), Williams & Wilkins, Baltimore pp. 587-607. Coombs JM, Brenchley JE (1999). Biochemical and phylogenetic analyses of a cold-active β-galactosidase from the lactic acid bacterium Carnobacterium piscicola BA, Appl. Environ. Microbiol., 65 : 5443-5450. Farmer JJ, Brenner DJ (2005). Genus XXII. Obesumbacterium. In: Bergey’s Manual of Systematic Bacteriology, Vol. 2, D.J. Brenner, N.R Krieg, J.T. Staley (Eds.), Williams &Wilkins, Baltimore pp. 710-713. Feller G, Narinx E, Arpigny JL, Aittaleb M, Baise E, Genicot S, Gerday C (1996). Enzymes from psychrophilic organisms. FEMS Microbiol. Rev., 18: 189-202. Ghatak A, Guha AK, Ray L (2010). β-D-Galactosidase from Enterobacter cloacae: production and some physicochemical properties. Appl. Biochem. Biotechnol., 165 : 1678-1688. Gerday C, Aittaleb M, Bentahir M, Chessa JP, Claverie P, Collins T, D’Amico SM, Dumont J, Garsoux G, Georlette D, Hoyoux AT, Lonhienne T, Meuwiw, MA, Feller G (2000). Cold-adapted enzymes from fundamentals to biotechnology. Trends in Biotechnol., 18 : 103-107. Gutshall KR, Trimbur DE, Kasmir JJ, Brenchley JE (1995). Analysis of a novel gene and β-galactosidase isoenzyme from a psychrophilic Arthrobacter isolate. J. Bacteriol., 177 : 1981-1988. Hildebrandt P, Wanarska M, Kur J (2009). A new coldadapted β-D-galactosidase from the Antarctic Arthrobacter 107 J. Anim. Prod. Adv., 2012, 2(2):
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Page 7: Residual activity(%) Relative activ

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