Abstract
Kluyveromyces marxianus NRRL Y-1196 yielded the highest lactase activity when cultivated in shake flasks for 24 h in sauerkraut brine with 0.2% lactose as an inducer. The enzyme was purified 4-fold and had a specific activity of 28 units/mg protein. The Km value was 3.94 mM. The pH and temperature optima of the enzyme were 7.0 and 50°C, respectively. It was stable between pH 6.0 to 7.6, but lost its activity at 60°C.
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References
Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Anal. Biochem. 72:248–254.
Goncalves, J.A. and Castillo, F.J. 1982. Partial purification and characterization of b-galactosidase fromKluyveromyces fragilis.J. Dairy Sci. 65:2088–2094.
Hang, Y.D., Splittstoesser, D.F. and Landschoot, R.L. 1972. Sauerkraut waste: a favorable medium for cultivating yeast.Appl.Microbiol. 24:1007–1008.
Hewitt, G.M. and Grootwassink, J.W.D. 1984. Simultaneous production of inulinase and lactase in batch and continuous cultures ofKluyveromyces fragilis.Enzyme Microb. Technol. 6:263–270.
Joshi, M.S., Gowda, L.R. and Bhat, S.G. 1987. Permeabilization of yeast cells (Kluyveromyces fragilis) to lactose by cetyltrimethylammonium bromide.Biotechnol. Lett. 9:549–554.
Mahoney, R.R., Nickerson, T.A., and Whitaker, J.R. 1975. Secretion of strain, growth conditions, and extraction procedures for optimum production of lactase fromKluyveromyces fragilis.J. Dairy Sci. 58:1620–1629.
Mahoney, R.R. and Whitaker, J.R. 1977. Stability and enzymatic properties of b-galactiosidase fromKluyveromyces fragilis.J. Food Biochem. 1:327–350.
Uwajima, T., Yagi, H., and Terada, O. 1972. Purification, crystalization and some properties of b-galactosidase fromSaccharomyces fragilis.Agr. Biol. Chem., 36:570–577.
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Ku, M.A., Hang, Y.D. Production of yeast lactase from sauerkraut brine. Biotechnol Lett 14, 925–928 (1992). https://doi.org/10.1007/BF01020630
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DOI: https://doi.org/10.1007/BF01020630