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[106] l-Arabinose isomerase

1966
Publisher Summary This chapter discusses the determination of L-arabinose isomerase. L-arabinose isomerase activity is assayed spectrophotometrically at 30° using a standard spectrophotometer equipped with an absorbancy converter, automatic cuvette positioner, and recorder.
K. Yamanaka, W.A. Wood
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Heterologous expression and characterization of Bacillus coagulans l-arabinose isomerase

World Journal of Microbiology and Biotechnology, 2012
Bacillus coagulans has been of great commercial interest over the past decade owing to its strong ability of producing optical pure L: -lactic acid from both hexose and pentose sugars including L: -arabinose with high yield, titer and productivity under thermophilic conditions.
Xingding, Zhou, Jin Chuan, Wu
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Crystallization and properties of l-arabinose isomerase from Lactobacillus gayonii

Biochimica et Biophysica Acta (BBA) - Enzymology, 1969
1. 1. l-Arabinose isomerase (l-arabinose ketol-isomerase, EC 5.3.1.4) was isolated in the crystalline state in 20% yield from the extracts of l-arabinose-grown cells of Lactobacillus gayonii. The molecular weight of the crystalline enzyme was estimated as 271 000 with the method of the sucrose density gradient centrifugation. 2. 2.
T, Nakamatu, K, Yamanaka
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Bacterial L-Arabinose Isomerases: Industrial Application for D-Tagatose Production

Recent Patents on DNA & Gene Sequences, 2011
D-tagatose is a natural monosaccharide with a low caloric value and has an anti-hyperglycemiant effect. This hexose has potential applications both in pharmaceutical and agro-food industries. However, the use of D-tagatose remains limited by its production cost.
Boudebbouze, Samira   +2 more
openaire   +4 more sources

Induction and repression of L-arabinose isomerase in Lactobacillus plantarum

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
Abstract The enzyme L -arabinose isomerase ( L -arabinose ketol-isomerase, EC 5.3.1.4) could be induced with the substrate L -arabinose in Lactobacillus plantarum in enriched medium only. There was a lag of a about 30 min before the synthesis of the enzyme could be detected. The enzyme level reached the maximum limit after 3 h. Catabolites like D -
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Bioconversion of D‐galactose into D‐tagatose by expression of L‐arabinose isomerase

Biotechnology and Applied Biochemistry, 2000
D‐Tagatose is a potential bulking agent in food as a non‐calorific sweetener. To produce D‐tagatose from cheaper resources, plasmids harbouring the L‐arabinose isomerase gene (araA) fromEscherichia coli,Bacillus subtilisandSalmonella typhimuriumwere constructed because L‐arabinose isomerase was suggested previously as an enzyme that mediates the ...
H J, Roh, P, Kim, Y C, Park, J H, Choi
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Mechanism of Ultraviolet Light Induced Catabolite Repression of L-arabinose Isomerase

International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine, 1982
(1982). Mechanism of Ultraviolet Light Induced Catabolite Repression of L-arabinose Isomerase. International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine: Vol. 42, No. 6, pp. 685-691.
D, Bhatnagar, A K, Bhattacharya
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Cloning and characterization of a novel l-arabinose isomerase from Bacillus licheniformis

Applied Microbiology and Biotechnology, 2008
Based on analysis of the genome sequence of Bacillus licheniformis ATCC 14580, an isomerase-encoding gene (araA) was proposed as an L-arabinose isomerase (L-AI). The identified araA gene was cloned from B. licheniformis and overexpressed in Escherichia coli.
Ponnandy, Prabhu   +5 more
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L-Arabinose isomerase and its use for biotechnological production of rare sugars

Applied Microbiology and Biotechnology, 2014
L-Arabinose isomerase (AI), a key enzyme in the microbial pentose phosphate pathway, has been regarded as an important biological catalyst in rare sugar production. This enzyme could isomerize L-arabinose into L-ribulose, as well as D-galactose into D-tagatose.
Zheng, Xu   +4 more
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Enhanced activity and stability of l-arabinose isomerase by immobilization on aminopropyl glass

Applied Microbiology and Biotechnology, 2010
Immobilization of Bacillus licheniformis L: -arabinose isomerase (BLAI) on aminopropyl glass modified with glutaraldehyde (4 mg protein g support⁻¹) was found to enhance the enzyme activity. The immobilization yield of BLAI was proportional to the quantity of amino groups on the surface of support.
Ye-Wang, Zhang   +2 more
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