Exploring an L-arabinose isomerase from cryophile bacteria Arthrobacter psychrolactophilus B7 for D-tagatose production

被引:13
作者
Nirwantono, Rudi [1 ,2 ,3 ]
Laksmi, Fina Amreta [1 ]
Nuryana, Isa [1 ]
Firdausa, Salsabila [1 ]
Herawan, David [1 ]
Giyandini, Ranistia [1 ]
Hidayat, Alam Ahmad [4 ]
机构
[1] Natl Res & Innovat Agcy BRIN, Res Ctr Appl Microbiol, Jl Raya Bogor,Km 46, Bogor 16911, Indonesia
[2] Univ Queensland, Sch Chem & Mol Biosci, Chem Bld,68 Cooper Rd, Brisbane, Qld 4072, Australia
[3] Bina Nusantara Univ, Fac Food Technol, Dept Biotechnol, Anggrek Jl Kebon Jeruk Raya 27, W Jakarta 11530, Indonesia
[4] Bina Nusantara Univ, Sch Comp Sci, Math Dept, Anggrek Jl Kebon Jeruk Raya 27, W Jakarta 11530, Indonesia
关键词
L -Arabinose isomerase; D; -Tagatose; Arthrobacter psychrolactophilus; D-GALACTOSE; CLONING; PURIFICATION; BIOCONVERSION; CONVERSION;
D O I
10.1016/j.ijbiomac.2023.127781
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A novel l-arabinose isomerase (L-AI) from Arthrobacter psychrolactophilus (Ap L-AI) was successfully cloned and characterized. The enzyme catalyzes the isomerization of d-galactose into a rare sugar d-tagatose. The recombinant Ap L-AI had an approximate molecular weight of about 258 kDa, suggesting it was an aggregate of five 58 kDa monomers and became the first record as a homo-pentamer L-AI. The catalytic efficiency (k(cat)/Km) and Km for d-galactose were 0.32 mM(-1) min(-1) and 51.43 mM, respectively, while for l-arabinose, were 0.64 mM(-1) min(-1) and 23.41 mM, respectively. It had the highest activity at pH 7.0-7.5 and 60 degrees C in the presence of 0.250 mM Mn2+. Ap L-AI was discovered to be an outstanding thermostable enzyme that only lost its half-life value at 60 degrees C for >1000 min. These findings suggest that l-arabinose isomerase from Arthrobacter psychrolactophilus is a promising candidate for d-tagatose mass-production due to its industrially competitive temperature.
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页数:10
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