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Partial Characterization of ?-Galactosidic Activity from the Antarctic Bacterial Isolate, Paenibacillus sp. LX-20 as a Potential Feed Enzyme Source.


ABSTRACT: An Antarctic bacterial isolate displaying extracellular ?-galactosidic activity was named Paenibacillus sp. LX-20 based on 16S rRNA gene sequence analysis. Optimal activity for the LX-20 ?-galactosidase occurred at pH 6.0-6.5 and 45°C. The enzyme immobilized on the smart polymer Eudragit L-100 retained 70% of its original activity after incubation for 30 min at 50°C, while the free enzyme retained 58% of activity. The enzyme had relatively high specificity for ?-D-galactosides such as p-nitrophenyl-?-galactopyranoside, melibiose, raffinose and stachyose, and was resistant to some proteases such as trypsin, pancreatin and pronase. Enzyme activity was almost completely inhibited by Ag(+), Hg(2+), Cu(2+), and sodium dodecyl sulfate, but activity was not affected by ?-mercaptoethanol or EDTA. LX-20 ?-galactosidase may be potentially useful as an additive for soybean processing in the feed industry.

SUBMITTER: Park I 

PROVIDER: S-EPMC4093098 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature

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Partial Characterization of α-Galactosidic Activity from the Antarctic Bacterial Isolate, Paenibacillus sp. LX-20 as a Potential Feed Enzyme Source.

Park Inkyung I   Lee Jaekoo J   Cho Jaiesoon J  

Asian-Australasian journal of animal sciences 20120601 6


An Antarctic bacterial isolate displaying extracellular α-galactosidic activity was named Paenibacillus sp. LX-20 based on 16S rRNA gene sequence analysis. Optimal activity for the LX-20 α-galactosidase occurred at pH 6.0-6.5 and 45°C. The enzyme immobilized on the smart polymer Eudragit L-100 retained 70% of its original activity after incubation for 30 min at 50°C, while the free enzyme retained 58% of activity. The enzyme had relatively high specificity for α-D-galactosides such as p-nitrophe  ...[more]

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