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Coenzyme regeneration catalyzed by NADH oxidase from Lactococcus lactis (CROSBI ID 204987)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Sudar, Martina ; Findrik, Zvjezdana ; Vuković Domanovac, Marija ; Vasić-Rački, Đurđa Coenzyme regeneration catalyzed by NADH oxidase from Lactococcus lactis // Biochemical engineering journal, 88 (2014), 12-18. doi: 10.1016/j.bej.2014.04.001

Podaci o odgovornosti

Sudar, Martina ; Findrik, Zvjezdana ; Vuković Domanovac, Marija ; Vasić-Rački, Đurđa

engleski

Coenzyme regeneration catalyzed by NADH oxidase from Lactococcus lactis

Lactococcus lactis was aerobically grown in a bioreactor to produce NADH oxidase, an enzyme used for NAD+ regeneration. The enzyme was isolated and purified from the cells that were harvested at the end of exponential phase of growth. The influence of temperature, pH and oxygen on enzyme activity was investigated. The enzyme was kinetically characterized at different pH values and in different buffers. It was found that Michaelis constants for oxygen are very low (the highest was 4.5 µmol dm-3 at pH 8.0). NADH oxidase was tested as a regenerating enzyme in a model system of L- methionine oxidation catalyzed by L-phenylalanine dehydrogenase from Rhodococcus sp. When NADH oxidase from L. lactis was used for NAD+ regeneration, 100% L- methionine conversion was achieved, while without regeneration of NAD+ it was estimated to be about 28%. The operational stability of NADH oxidase was followed and it was found that enzyme activity decay occurs. The operational stability decay rate constant, kd, was estimated to be 8.0 • 10- 5 min-1.

Lactococcus lactis ; NADH oxidase ; coenzyme NAD+ regeneration

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Podaci o izdanju

88

2014.

12-18

objavljeno

1369-703X

10.1016/j.bej.2014.04.001

Povezanost rada

Biotehnologija, Kemijsko inženjerstvo

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