Abstract：
:L-arabinose isomerase (L-AI) (EC 5. 3. 1. 4. L-AI) that mediates the isomerization of D-galactose to D-tagatose was isolated from Lactobacillus brevis (MF 465792), and was further purified and characterized. Pure enzyme with molecular weight of 60.1 kDa was successfully obtained after the purification using Native-PAGE gel extraction method, which was a monomer in solution. The L-AI was found to be stable at 45-75 °C, and at pH 7.0-9.0. Its optimum temperature and pH was determined as 65 °C and 7.0, respectively. Besides, we found that Ca2+, Cu2+, and Ba2+ ions inhibited the enzyme activity, whereas the enzyme activity was significantly enhanced in the presence of Mg2+, Mn2+, or Co2+ ions. The optimum concentration of Mn2+ and Co2+ was determined to be 1 mM. Furthermore, we characterized the kinetic parameters for L-AI and determined the Km (129 mM) and the Vmax (0.045 mM min- 1) values. Notably, L. brevisL-AI exhibited a high bioconversion yield of 43% from D-galactose to D-tagatose under the optimal condition, and appeared to be a more efficient catalyst compared with other L-AIs from various organisms.
journal_name
Bioprocess Biosyst Engjournal_title
Bioprocess and biosystems engineeringauthors
Du M,Zhao D,Cheng S,Sun D,Chen M,Gao Z,Zhang Cdoi
10.1007/s00449-018-2018-9subject
Has Abstractpub_date
2019-01-01 00:00:00pages
107-116issue
1eissn
1615-7591issn
1615-7605pii
10.1007/s00449-018-2018-9journal_volume
42pub_type
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