Perspectives of biotechnological production of l-ribose and its purification

Hu, Chao Chin; Li, Liangzhi; Zheng, Yayue; Rui, Lilian; Hu, Cuiying

doi:10.1007/s00253-011-3552-4

Cited by 34 publications

(10 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…T. thermophilus produces a series of enzymes of biotechnological interest, including glucose isomerase, xylose isomerase, proteases, beta-glucosidase, L-asparaginase, phosphatases (at least four), pyrophosphatase and several DNA and RNA processing enzymes [ 40 ]. More recently other promising enzymes from T. thermop hilus have been reported such as NADH-oxidases [ 44 ], mannose-6-P-isomerase [ 45 , 46 ] and superoxide dismutases [ 47 ], amongst others.…”

Section: Thermus Thermophilus ( T Thmentioning

confidence: 99%

Thermus thermophilus as a Source of Thermostable Lipolytic Enzymes

2015

View full text Add to dashboard Cite

Lipolytic enzymes, esterases (EC 3.1.1.1) and lipases (EC 3.1.1.3), catalyze the hydrolysis of ester bonds between alcohols and carboxylic acids, and its formation in organic media. At present, they represent about 20% of commercialized enzymes for industrial use. Lipolytic enzymes from thermophilic microorganisms are preferred for industrial use to their mesophilic counterparts, mainly due to higher thermostability and resistance to several denaturing agents. However, the production at an industrial scale from the native organisms is technically complicated and expensive. The thermophilic bacterium Thermus thermophilus (T. thermophilus) has high levels of lipolytic activity, and its whole genome has been sequenced. One esterase from the T. thermophilus strain HB27 has been widely characterized, both in its native form and in recombinant forms, being expressed in mesophilic microorganisms. Other putative lipases/esterases annotated in the T. thermophilus genome have been explored and will also be reviewed in this paper.

show abstract

Section: Thermus Thermophilus ( T Thmentioning

confidence: 99%

Thermus thermophilus as a Source of Thermostable Lipolytic Enzymes

2015

View full text Add to dashboard Cite

show abstract

“…They have recently attracted the attention of many researchers by the possibility of their use as low-calorie carbohydrate sweeteners and bulking agents. There have been some detailed reviews on physiological function and biological production of some rare sugars, such as D-tagatose (Oh 2007), D-allose (Lim and Oh 2011), xylitol (Granstrom et al 2007), and L-ribose (Hu et al 2011). …”

Section: Introductionmentioning

confidence: 99%

Recent advances on applications and biotechnological production of d-psicose

Zhang

Yan

et al. 2012

Appl Microbiol Biotechnol

136

109

View full text Add to dashboard Cite

D-Psicose is a hexoketose monosaccharide sweetener, which is a C-3 epimer of D-fructose and is rarely found in nature. It has 70 % relative sweetness but 0.3 % energy of sucrose, and is suggested as an ideal sucrose substitute for food products. It shows important physiological functions, such as blood glucose suppressive effect, reactive oxygen species scavenging activity, and neuroprotective effect. It also improves the gelling behavior and produces good flavor during food process. This article presents a review of recent studies on the properties, physiological functions, and food application of D-psicose. In addition, the biochemical properties of D-tagatose 3-epimerase family enzymes and the D-psicose-producing enzyme are compared, and the biotechnological production of D-psicose from D-fructose is reviewed.

show abstract

“…The latter is the precursor of d-xylulose-5-phosphate, an intermediate in the pentose phosphate pathway (Lee et al, 1986). Strikingly, l-ribulose is useful in manufacturing l-ribose, a pharmaceutical raw material that is useful for the production of l-form sugar-based antiviral drugs, including those for the treatment of Hepatitis B virus (HBV), Hepatitis C virus (HCV), Human immunodeficiency virus (HIV) and Human cytomegalovirus (HCMV) (Okano, 2009;Hu et al, 2011). Moreover, AI was also found to be active in isomerizing d-galactose to d-tagatose (Cheetham & Wootton, 1993).…”

Section: Introductionmentioning

confidence: 99%

Protein purification, crystallization and preliminary X-ray diffraction analysis ofL-arabinose isomerase fromLactobacillus fermentumCGMCC2921

Liang

et al. 2015

Acta Cryst Sect F

View full text Add to dashboard Cite

L-Arabinose isomerase (AI) catalyzes the isomerization of L-arabinose to L-ribulose, as well as that of D-galactose to D-tagatose. A thermophilic AI derived from Lactobacillus fermentum CGMCC2921 (LFAI) was overexpressed in Escherichia coli BL21 (DE3). This enzyme was purified to over 95% purity by nickel affinity, Mono-Q ion-exchange and size-exclusion chromatography. The LFAI protein was crystallized from either 0.1 M bis-tris pH 6.5, 23% PEG 3350, 0.3 M NaCl (form 1 crystals) or 0.1 M bis-tris pH 6.0, 25% PEG monomethyl ether 5000 (form 2 crystals). Diffraction data from form 1 LFAI crystals were collected to 2.80 Å resolution using synchrotron radiation. The form 1 crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a=85.11, b=184.57, c=186.26 Å, α=β=γ=90°. The asymmetric unit contained six LFAI subunits, corresponding to a calculated Matthews coefficient of 2.29 Å3 Da(-1) and a solvent content of 46.22%.

show abstract

Perspectives of biotechnological production of l-ribose and its purification

Cited by 34 publications

References 35 publications

Thermus thermophilus as a Source of Thermostable Lipolytic Enzymes

Thermus thermophilus as a Source of Thermostable Lipolytic Enzymes

Recent advances on applications and biotechnological production of d-psicose

Protein purification, crystallization and preliminary X-ray diffraction analysis ofL-arabinose isomerase fromLactobacillus fermentumCGMCC2921

Contact Info

Product

Resources

About