Jaiesoon Cho

Degradation of Phytate Pentamagnesium Salt by Bacillus sp. T4 Phytase as a Potential Eco-friendly Feed Additive

A bacterial isolate derived from soil samples near a cattle farm was found to display extracellular phytase activity. Based on 16S rRNA sequence analysis, the strain was named Bacillus sp. T4. The optimum temperature for the phytase activity toward magnesium phytate (Mg-InsP6) was 40°C without 5 mM Ca2+ and 50°C with 5 mM Ca2+. T4 phytase had a characteristic bi-hump two pH optima of 6.0 to 6.5 and 7.4 for Mg-InsP6. The enzyme showed higher specificity for Mg-InsP6 than sodium phytate (Na-InsP6). Its activity was fairly inhibited by EDTA, Cu2+, Mn2+, Co2+, Ba2+ and Zn2+. T4 phytase may have great potential for use as an eco-friendly feed additive to enhance the nutritive quality of phytate and reduce phosphorus pollution.

Immobilization of the Antarctic Bacillus sp. LX-1 α-Galactosidase on Eudragit L-100 for the Production of a Functional Feed Additive

Partially purified α-galactosidase from Bacillus sp. LX-1 was non-covalently immobilized on a reversibly soluble-insoluble polymer, Eudragit L-100, and an immobilization efficiency of 0.93 was obtained. The optimum pH of the free and immobilized enzyme was 6.5 to 7.0 and 7.0, respectively, while there was no change in optimum temperature between the free and immobilized α-galactosidase. The immobilized α-galactosidase was reutilized six times without significant loss in activity. The immobilized enzyme showed good storage stability at 37°C, retaining about 50% of its initial activity even after 18 d at this temperature, while the free enzyme was completely inactivated. The immobilization of α-galactosidase from Bacillus sp. LX-1 on Eudragit L-100 may be a promising strategy for removal of α-galacto-oligosaccharides such as raffinose and stachyose from soybean meal and other legume in feed industry.

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

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-nitrophenyl-α-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+, Hg2+, Cu2+, and sodium dodecyl sulfate, but activity was not affected by β-mercaptoethanol or EDTA. LX-20 α-galactosidase may be potentially useful as an additive for soybean processing in the feed industry.

Extracellular lipase of the antarctic bacterial isolate, Pseudomonas sp. INK1 as a potential tool for improving the flavor quality of dairy products

An antarctic bacterial isolate displayed extracellular lipolytic activity. Based on the 16S rRNA sequence analysis, the strain was named Pseudomonas sp. INK1. The INK1 lipase was secreted into the production medium during transition to the stationary phase. The enzyme reached the apparent maximal activity at pH 8 to 9, with optimal activity at 50°C. The enzyme was active against a wide range of fatty acid esters of p-nitrophenyl, showing the highest activity towards p-nitrophenyl caprylate. It could also release caprylic acid from a natural substrate cream. The enzyme activity was strongly inhibited by Zn 2+ and Mn 2+ , and slightly enhanced by EDTA. INK1 lipase may be a potentially useful