A study of commercial β-galactosidase stability under simulated in vitro gastric conditions
Laen...
Failid
Kuupäev
2018
Kättesaadav alates
Autorid
Žolnere, K.
Ciproviča, I.
Ķirse, A.
Cinkmanis, I.
Ajakirja pealkiri
Ajakirja ISSN
Köite pealkiri
Kirjastaja
Abstrakt
β-Galactosidase
activity in milk may be affected by several factors, such as
temperature, pH, milk composition, and metal ions. It is important to note that digestive proteases
and gastrointestinal pH can affect enzyme activity during transit through the gastrointestinal
tract.
For the investigation of commercial β
-
galactosidase stability in human and animal gastric tracts,
human gastrointestinal tract (GIT) models were employed, enabling prediction of enzyme activity
under
in vivo
conditions. The aim of this study was to
analyse and compare commercial β
-
galactosidase stability under simulated
in vitro
gastric conditions. Commercial enzymes
(Ha
Lactase 5200 produced by
Kluyveromyces lactis
and NOLA™Fit5500 produced by
Bifidobacterium bifidum
expressed in
Bacillus lichenifo
rmis
, Chr. Hansen, Hørsholm, Denmark;
GODO
-
YNL2 produced by
Kluyveromyces lactis
, Danisco, Copenhagen, Denmark) were used
for this study. Commercial enzymes were added to GIT models at 1 and 5
mL
L
–
1
. The enzyme
activity was assessed as the percentage of l
actose hydrolysis by the enzymes from
Kluyveromyces
lactis
and
Bacillus licheniformis
using HPLC after digestion. β
-
Galactosidase extracted from
yeast (
Kluyveromyces lactis
) and bacteria (
Bacillus licheniformis
) was found to be effective as a
strategy for
improving lactose tolerance.
Kirjeldus
Article
Märksõnad
β-galactosidase, simulated gastric conditions, lactose hydrolysis, articles