The effect of αα‐lactalbumin and ββ‐lactoglobulin hydrolysates on the metabolic activity of Escherichia coli JM103

• Autores: T. Rokka, M. Karp, A. Pihlanto-Leppälä, P. Marnila, L. Hubert, H. J. T. Korhonen
• Localización: Journal of applied microbiology, ISSN 1364-5072, Vol. 87, Nº 4, 1999, págs. 540-545
• Idioma: inglés
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• Resumen

  • Bovine milk proteins α‐lactalbumin (α‐la) and β‐lactoglobulin (β‐lg) were hydrolysed with seven different proteolytic enzymes, and the effect of various hydrolysates on a genetically modified luminous Escherichia coli JM103 was tested in vitro with a bioluminescence assay for bacterial growth and metabolism. Undigested proteins did not inhibit the activity of tested E. coli JM103 at a concentration as high as 0·1 g ml−1. At the same concentrations, α‐la hydrolysed with pepsin or trypsin and β‐lg hydrolysed with alcalase, pepsin or trypsin, showed a lower metabolic activity during the first 8 h of growth. The activity of E. coli JM103 in the presence of 25 mg ml−1α‐la or β‐lg hydrolysed with pepsin and trypsin was only 21% of the control after incubation for 6 h. The preliminary results indicated that ultrafiltration through 10 kDa and 1 kDa molecular mass cut‐off membranes may be used to enrich bacteriostatic properties.