Literature summary for 5.3.1.4 extracted from

Zhang, Y.W.; Jeya, M.; Lee, J.K.
Enhanced activity and stability of L-arabinose isomerase by immobilization on aminopropyl glass (2011), Appl. Microbiol. Biotechnol., 89, 1435-1442.

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Bacillus licheniformis

General Stability

General Stability	Organism
immobilization of Bacillus licheniformis L-arabinose isomerase on aminopropyl glass modified with glutaraldehyde (4 mg protein g per support) enhances the enzyme activity. The immobilized BLAI enzyme achieves 145% of the activity of the free enzyme, and the catalytic efficiency (kcat/Km) is improved 1.47fold after immobilization compared to the free enzyme. Immobilized enzyme on aminopropyl glass has about 30% higher activity than that on Eupergit C and 95% higher activity than that on agarose	Bacillus licheniformis

Organism

immobilization of Bacillus licheniformis L-arabinose isomerase on aminopropyl glass modified with glutaraldehyde (4 mg protein g per support) enhances the enzyme activity. The immobilized BLAI enzyme achieves 145% of the activity of the free enzyme, and the catalytic efficiency (kcat/Km) is improved 1.47fold after immobilization compared to the free enzyme. Immobilized enzyme on aminopropyl glass has about 30% higher activity than that on Eupergit C and 95% higher activity than that on agarose

Bacillus licheniformis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
352	-	L-arabinose	immobilized enzyme, in 50 mM phosphate buffer (pH 7.5),1 mM MnCl2, at 50°C	Bacillus licheniformis
369	-	L-arabinose	free enzyme, in 50 mM phosphate buffer (pH 7.5),1 mM MnCl2, at 50°C	Bacillus licheniformis

Organism

Organism	UniProt	Comment	Textmining
Bacillus licheniformis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-NTA column chromatography	Bacillus licheniformis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-arabinose	-	Bacillus licheniformis	L-ribulose	-	r

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
50	-	free enzyme	Bacillus licheniformis
70	-	immobilized enzyme	Bacillus licheniformis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
50	-	the half life of the free enzyme is 2 h and the half life of the aminopropyl glass-immobilized enzyme is 275 h at 50°C	Bacillus licheniformis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	8	immobilized enzyme	Bacillus licheniformis
7.5	-	free enzyme	Bacillus licheniformis