title: Altered superoxide dismutase activity by carbohydrate utilization in a Lactococcus lactis strain.
abstract: Reactive oxygen species, such as superoxide, can damage cellular components, such as proteins, lipids, and DNA. Superoxide dismutase (SOD) enzymes catalyze the conversion of superoxide anions to hydrogen peroxide and dioxygen. SOD is present in most lactococcal bacteria, which are commonly used as starters for manufacturing fermented dairy products and may have health benefits when taken orally. We assessed the effects of carbohydrate use on SOD activity in lactococci. In Lactococcus lactis ssp. lactis G50, the SOD activity of cells grown on lactose and galactose was higher than that on glucose; in Lactococcus lactis ssp. cremoris H61, SOD activity was independent of the type of carbohydrate used. We also investigated the activity of NADH oxidase, which is related to the production of superoxide in strains G50 and H61. Activity was highest in G50 cells grown on lactose, lower on galactose, and lowest on glucose, whereas activity in H61 cells did not differ with the carbohydrate source used. The SOD and NADH oxidase activities of strain G50 in three carbohydrates were linked. Strain G50 fermented lactose and galactose to lactate, acetate, formate, and ethanol (mixed-acid fermentation) and fermented glucose to mainly lactate (homolactic fermentation). Strain H61 fermented glucose, lactose, and galactose to mainly lactate (homolactic fermentation). In strain G50, when growth efficiency was reduced by adding a metabolic inhibitor to the growth medium, SOD activity was higher than in the control; however, the metabolism was homofermentative. Aerobic conditions, but not glucose-limited conditions, increased SOD activity, and mixed-acid fermentation occurred. We conclude that the effect of carbohydrate on SOD activity in lactococci is strain dependent and that the activity of commercial lactococci can be enhanced through carbohydrate selection for mixed-acid fermentation or by changing the energy distribution, thus enhancing the value of the starter and the resulting dairy products.
authors.affiliation: NARO Institute of Livestock and Grassland Science, Ikenodai 2, Tsukuba, Ibaraki 305-0901, Japan. anne@affrc.go.jp.
authors.forename: H
authors.initials: H
authors.lastname: Kimoto-Nira
authors.affiliation: NARO Institute of Livestock and Grassland Science, Ikenodai 2, Tsukuba, Ibaraki 305-0901, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Moriya
authors.affiliation: NARO Institute of Livestock and Grassland Science, Ikenodai 2, Tsukuba, Ibaraki 305-0901, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Ohmori
authors.affiliation: NARO Institute of Livestock and Grassland Science, Ikenodai 2, Tsukuba, Ibaraki 305-0901, Japan.
authors.forename: C
authors.initials: C
authors.lastname: Suzuki
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D003470:Culture Media / Q000378:metabolism; D005285:Fermentation; D005690:Galactose / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism*; D013294:Lactococcus lactis / Q000201:enzymology* / Q000378:metabolism; D007785:Lactose / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D013482:Superoxide Dismutase / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D003470:Culture Media; D009097:Multienzyme Complexes; D013482:Superoxide Dismutase; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases; D005947:Glucose; D007785:Lactose; D005690:Galactose