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PubMed1992

L-sorbose does not cause hemolysis in dog erythrocytes with inherited high Na, K-ATPase activity.

1. The hemolytic effect of L-sorbose on canine erythrocytes characterized by inherited high Na, K-ATPase activity and a high potassium concentration (HK RBCs) was compared with that on normal canine erythrocytes (LK RBCs). 2. Dogs having HK RBCs (HK dogs) revealed no clinical and hematological changes after administration of L-sorbose, whereas normal dogs (LK dogs) developed severe hemolytic anemia associated with hemoglobinuria and marked decreases of erythrocyte ATP concentrations. 3. In vitro, L-sorbose induced hemolysis in LK RBCs along with the depression of both ATP and lactate formation in these cells, but not in HK RBCs. The inhibition of glycolysis by L-sorbose in LK RBCs, however, was not observed when glucose-6-phosphate was used as a substrate instead of glucose. 4. These results suggest that the disparity of susceptibility to sorbose-induced hemolysis may be due to the difference in erythrocyte metabolism between HK and LK RBCs, especially the high activity of hexokinase in HK cells, which was 2-fold greater than that in LK RBCs.

Adenosine Triphosphate↗
PubMed1993

Dietary sorbose prevents and improves hyperglycemia in genetically diabetic mice.

The effect of dietary sorbose on the prevention (Experiment 1) and amelioration (Experiment 2) of diabetes was investigated in the genetically diabetic mouse [C57BL/KsJ (db/db)] for 6 wk. When sucrose (200 g/kg diet) in a control diet was replaced by sorbose, the blood glucose concentration was dramatically lower, but the serum insulin concentrations did not differ. When mice were fed the diets before the onset of diabetic symptoms, glucose excretion in urine was prevented in the mice fed the sorbose diet, but mice fed the control diet excreted glucose in the urine, and the concentration increased with age. When dietary treatment began after the development of diabetic symptoms, dietary sorbose greatly reduced the incidence of hyperglycemia and lowered urinary glucose excretion, compared with mice fed the sucrose-containing diet. These results suggest that dietary sorbose might be useful in patients with, or at risk of developing, noninsulin-dependent diabetes, both before and after exhibiting the syndrome.

Animals↗
PubMed2002

Cross-talk between the L-sorbose and D-sorbitol (D-glucitol) metabolic pathways in Lactobacillus casei.

A gene encoding sorbitol-6-phosphate dehydrogenase (SorF) belonging to the sorbose operon (sorFABCDG) has been characterized in Lactobacillus casei. Inactivation of this gene revealed the presence of another sorbitol-6-phosphate dehydrogenase that was induced by D-sorbitol (D-glucitol). The gene encoding this activity (gutF) has also been isolated, sequenced and disrupted. The sorbitol-6-phosphate dehydrogenase genes (sorF, gutF) were required for growth on L-sorbose and D-sorbitol, respectively. Biochemical and transcriptional analyses of the wild-type and mutant strains demonstrated that L-sorbose and D-sorbitol induced sorF and the gene encoding the sorbose operon activator (sorR), while the expression of gutF was only activated by D-sorbitol. Furthermore, these studies indirectly suggested that a common metabolite of the L-sorbose and D-sorbitol metabolic pathways (probably D-sorbitol 6-phosphate) would act as the effector of SorR. The same effector would also be the inducer of gutF, although the two pathways seem to be subject to distinct regulatory mechanisms.

Bacterial Proteins↗
PubMed1979

Metabolism of L-sorbose in the rat and the effect of the intestinal microflora on its utilization both in the rat and in the human.

L-[U-14C]-sorbose was administered orally as single doses to 5 normal rats. The recovery of radioactivity was 5.3% in the urine, 46% in the faeces exclusively as L-sorbose 16% as carbon dioxide. Caloric utilization was approximately 25%. A second group of 3 rats that had previously received L-sorbose in their diet showed 14C recoveries of 8.9% in the urine, 6.6% in the faeces and 59% as carbon dioxide. The time course of expired carbon dioxide suggests that a portion of L-sorbose was rapidly absorbed and partially metabolized while the principal pathway involved fermentation by the intestinal microflora to volatile fatty acids which were subsequently absorbed and metabolized. The total caloric utilization of L-sorbose was estimated to be 70%. It was observed that a human intestinal microflora also required an adaptation period in order to ferment this sugar. The efficiency of the fermentation was estimated to be 70%.

Administration, Oral↗
PubMed1994

Influence of dietary sorbose on diabetes in nonobese diabetic mice.

The effect of dietary sorbose on diabetes after the incidence of the syndrome in the nonobese diabetic mouse was investigated in the animals from 8 to 14 weeks of age. When sucrose (200 g/kg diet) in a control diet was replaced by sorbose, the body weight and the blood glucose concentration were significantly reduced, but the serum insulin concentration was unchanged. The urinary glucose concentration was the same for both sucrose and sorbose diets. It is suggested that after the incidence of diabetes, dietary sorbose could not improve urinary excretion of glucose, even though sorbose could reduce the blood glucose concentration.

Animals↗
PubMed2002

Productivity improvement in l-sorbose biosynthesis by fedbatch cultivation of Gluconobacter oxydans.

The effect of increased (100, 200 and 300 gl(-1)) initial sorbitol concentrations (S0) was investigated in the sorbitol to sorbose bioconversion process. Batch cultivations with a S0 of 100, 200 and 300 gl(-1) were completed at 10, 14 and 24 h with a corresponding overall sorbose productivity of 10.1, 14.3 and 12.4 gl(-1) h(-1) respectively. The decrease in sorbose productivity at S0=300 gl(-1) was attributed to the inhibition by sorbitol of culture growth and product formation. In order to eliminate substrate inhibition, two identical fed-batch cultivations were performed in which a highly concentrated (500 gl(-1)) sorbitol solution was added at a constant feed rate (0.2 l h(-1)) in the exponential phase of growth. The Fed-batch culture initiated with S0=225 gl(-1) exhibited an enhanced accumulation of sorbose (336.2 gl(-1)) but with a processing time of 24 h, and a productivity of 14.0 gl(-1) h(-1). While, the fed-batch culture initiated with S0=100 gl(-1) accumulated 279.7 gl(-1) of sorbose with an increase in productivity of 17.6 gl(-1) h(-1) in 16 h.

Journal Article↗
PubMed2001

L-Sorbose induces cellulase gene transcription in the cellulolytic fungus Trichoderma reesei.

L-Sorbose has previously been assumed to stimulate cellulase formation in an indirect manner, different from that of sophorose in Trichoderma reesei. Through Northern blot analysis however, L-sorbose was found to regulate coordinately six cellulase genes (including eg13, whose behavior has not been studied so far) at transcriptional level, as is the case with sophorose in T. reesei strains PC-3-7 and QM9414. Dot blot analysis showed that the proportions of each cellulase mRNA to cbh1 mRNA, the largest amount of mRNA transcribed in T. reesei, did not change when L-sorbose or sophorose was used as an inducer in the PC-3-7 and QM9414 strains. cbh2 and egl1 mRNAs were about 45-60% and 20-30% of the cbh1 transcript, whereas small amounts of mRNA, 1-2% of cbh1, were observed on other endoglucanase genes. Furthermore, the PC-3-7 strain showed an enhanced level of cellulase gene transcription, about two- and four- to six-fold higher than that of the QM9414 strain with sophorose and L-sorbose, respectively.

Cellulase↗
PubMed1975

Lipid-protein interactions at the erythrocyte membrane. Different influence of glucose and sorbose on membrane lipid transition.

When observed over a temperature range, erythrocyte membrane lipids undergo a transition at 18-20 degrees C (Zimmer, G. and Schirmer, H. (1974) biochim. Biophys. Acta 345, 314-320). This observation has prompted an investigation of the effects that substrate binding has on the transition of the red cell membrane. Glucose and sorbose were compared, since transport kinetics of these sugars still pose unresolved questions. In membranes, preloaded with glucose, the break at the transition temperature was intensified, while it was abolished or reversed in membranes preloaded with sorbose. These results were corroborated using different solubilization procedures (sonication, sodium dodecyl sulfate treatment) of the membranes, and also different techniques (viscosimetry, 90 degrees light scattering, 1-anilino-naphthalene-8-sulfonate fluorescence). In extracted membrane lipids, viscosimetry indicated a break at transition temperature after preloading with either glucose or sorbose. Disc electrophoresis revealed a different binding pattern of the two sugars. It is suggested, that the amplification of the discontinuity in red cell membranes by glucose and the abolition or reversal of the break by sorbose are mediated by membrane protein- and/or membrane lipid-protein interaction.

Blood Proteins↗
PubMed1999

Interactions of sodium pentobarbital with D-glucose and L-sorbose transport in human red cells.

Pentobarbital acts as a mixed inhibitor of net D-glucose exit, as monitored photometrically from human red cells. At 30 degrees C the Ki of pentobarbital for inhibition of Vmax of zero-trans net glucose exit is 2.16+/-0.14 mM; the affinity of the external site of the transporter for D-glucose is also reduced to 50% of control by 1. 66+/-0.06 mM pentobarbital. Pentobarbital reduces the temperature coefficient of D-glucose binding to the external site. Pentobarbital (4 mM) reduces the enthalpy of D-glucose interaction from 49.3+/-9.6 to 16.24+/-5.50 kJ/mol (P<0.05). Pentobarbital (8 mM) increases the activation energy of glucose exit from control 54.7+/-2.5 kJ/mol to 114+/-13 kJ/mol (P<0.01). Pentobarbital reduces the rate of L-sorbose exit from human red cells, in the temperature range 45 degrees C-30 degrees C (P<0.001). On cooling from 45 degrees C to 30 degrees C, in the presence of pentobarbital (4 mM), the Ki (sorbose, glucose) decreases from 30.6+/-7.8 mM to 14+/-1.9 mM; whereas in control cells, Ki (sorbose, glucose) increases from 6.8+/-1.3 mM at 45 degrees C to 23.4+/-4.5 mM at 30 degrees C (P<0.002). Thus, the glucose inhibition of sorbose exit is changed from an endothermic process (enthalpy change=+60.6+/-14.7 kJ/mol) to an exothermic process (enthalpy change=-43+/-6.2 7 kJ/mol) by pentobarbital (4 mM) (P<0.005). These findings indicate that pentobarbital acts by preventing glucose-induced conformational changes in glucose transporters by binding to 'non-catalytic' sites in the transporter.

Binding Sites↗
PubMed1990

Cloning and physical mapping of the sor genes for L-sorbose transport and metabolism from Klebsiella pneumoniae.

The sor genes of Klebsiella pneumoniae KAY2026, which enable the bacterium to metabolize the ketose L-sorbose, have been cloned on an 8.3kb DNA fragment into the multicopy plasmid, pACYC184. The genes were mapped by restriction analysis, by deletion mapping and by insertion mutagenesis with Tn1725. The corresponding gene products were identified by the maxicell technique. The structural genes sorD, sorA and sorE code for a D-glucitol-6-P dehydrogenase (27 kilodalton (kD)), an Enzymell (EllSor) activity specific for L-sorbose and an L-sorbose-1-P reductase (45kD). Besides these genes for known functions, three additional genes were discovered: sorC, coding for a transcriptional 40kD regulatory protein, and sorF and sorB, coding for two proteins of 14kD and 19kD, respectively, involved in transport. The genes form an operon (gene order sorCpCDFBAE) and are inducible by L-sorbose.

Biological Transport↗
PubMed1991

Sorbose fermentation in relation to acquisition and maintenance of enterotoxin plasmids in Escherichia coli.

Previous studies have shown that the majority of enterotoxigenic Escherichia coli (ETEC) strains isolated from humans failed to ferment sorbose. In an attempt to demonstrate if this phenomenon was due to enterotoxin (Ent) plasmid instability in sorbose fermenting strains, recipient E. coli strains were used in conjugation experiments with three donor Ent plasmids. No difference in the ability to uptake the Ent plasmid was shown between sorbose fermenting and non-fermenting recipient strains. In addition, no difference was seen in the stability of the Ent plasmids in recipient strains of each biotype. These results suggest that in-vivo selection may play a role in the predominant isolation of non-sorbose fermenting ETEC strains.

Drug Resistance, Microbial↗
PubMed1976

[Sorbose in Salmonella diagnosis (author's transl)].

From 1525 Salmonella strains checked for fermentation of sorbose the majority failed to attack this sugar or split it with distinct delay. None of these cultures showed production of acid from sorbose prior to the third day of incubation. In contrast, sorbose was attacked within 24 hours by 74 out of 100 Ballerup-Bethesda strains. As an easy and reliable basis test combination for performing a minimal biochemical Salmonella diagnosis a series consisting of Kligler's medium and media containing urea, lysine, lactose, sucrose, sorbose, and salicin is suggested.

Salmonella↗
PubMed1988

The effect of sorbose on NAD(P)ase production by Aspergillus nidulans.

1. NAD(P)ase activity was stimulated when 1% sorbose was present in the culture medium of A. nidulans, and this effect was partially reversed by 1% glucose. 2. The level of extracellular NAD(P)ase was more affected by sorbose in the culture medium than the intracellular enzyme and no morphological changes were obtained. 3. The sorbose effect on NAD(P)ase activity appears to be specific since two other exoenzymes tested (beta-glucosidase and alkaline protease) show normal secretion patterns. 4. These findings suggest that the sorbose effect on NAD(P)ase production may be the consequence of metabolic disorders not necessarily linked with the morphological changes induced by the ketohexose.

Aspergillus nidulans↗
PubMed1999

Production of D-iditol from D-sorbose by Rhodotolura rubra RY10 isolated from miso paste.

The yeast strain RY10 that can convert D-sorbose to D-iditol was isolated from miso paste and identified as Rhodotolura rubra. The cells grown on D-fructose were found to have relatively high conversion potential. Addition of ethanol to the reaction mixture significantly accelerated the conversion rate of D-sorbose to D-iditol. During the conversion reaction, ethanol was added to the reaction mixture at 48 h intervals to maintain the concentration of ethanol at 1.0%. The final conversion ratios were 82.7%, 95.0%, 93.7%, and 78.0% using washed cells when the concentration D-sorbose were 1.0%, 2.0%, 3.0% and 5.0%, respectively. The product produced from D-sorbose was identified as D-iditol by high performance liquid chromatography analysis, infrared spectrum, optical rotation and melting point measurements.

Journal Article↗
PubMed1999

Screening for L-sorbose and L-sorbosone dehydrogenase producing microbes for 2-keto-L-gulonic acid production.

Acetic acid bacteria incompletely oxidize L-sorbose to 2-keto-L-gulonic acid (2KLG) by L-sorbose- and L-sorbosone dehydrogenases. In order to isolate novel microorganisms with these enzyme activities, a new screening method has been studied with a presumption that microorganisms reuse their metabolic products when principal carbon sources are exhausted. When various keto-aldonic acid-producing microorganisms were tested for the ability to grow in minimal media containing such products as 2,5-diketo-gluconic acid, 2-keto-D-gluconic acid, 5-keto-D-gluconic acid or 2-keto-L-gulonic acid, they grew with these keto-aldonic acids as the sole carbon source. By enriching the isolates collected from screening samples for their growth in minimal medium containing 2KLG as the sole carbon source, as much as 50% of selected strains showed L-sorbose- and L-sorbosone dehydrogenase activities. In spite of the presence of these enzymes, no significant amount of 2KLG was detected in the culture broth, possibly due to 2KLG reductase activity, indicating that the direct screening for 2KLG producer microorganisms would be less successful. These results suggest that the screening strategy using 2KLG as a carbon source is a useful method for the selective screening of microorganisms with L-sorbose- and L-sorbosone dehydrogenases, and that a similar strategy may be applied to other cases.

Journal Article↗
PubMed1992

Cloning of the Escherichia coli sor genes for L-sorbose transport and metabolism and physical mapping of the genes near metH and iclR.

The sor genes for L-sorbose (Sor) degradation of Escherichia coli EC3132, a wild-type strain, have been cloned on a 10.8-kbp fragment together with parts of the metH gene. The genes were mapped by restriction analysis, by deletion mapping, and by insertion mutagenesis with Tn1725. Seven sor genes with their corresponding gene products have been identified. They form an operon (gene order sorCpCDFBAME) inducible by L-sorbose, and their products have the following functions: SorC (36 kDa), regulatory protein with repressor-activator functions; SorD (29 kDa), D-glucitol-6-phosphate dehydrogenase; SorF and SorB (14 and 19 kDa, respectively), and SorA and SorM (27 and 29 kDa, respectively), two soluble and two membrane-bound proteins, respectively, of an L-sorbose phosphotransferase transport system; SorE (45 kDa), sorbose-1-phosphate reductase. The sor operon from E. coli EC3132 thus is identical to the operon from Klebsiella pneumoniae KAY2026. On the basis of restriction mapping followed by Southern hybridization experiments, the sor genes were mapped at 91.2 min on the chromosome, 3.3 kbp downstream of the metH-iclR gene cluster, and shown to be transcribed in a counterclockwise direction. The chromosomal map of the Sor+ strain EC3132 differs from that of the Sor- strain K-12 in approximately 8.6 kbp.

Biodegradation, Environmental↗
PubMed1976

Conversion of L-sorbose to L-sorbosone by immobilized cells of Gluconobacter melanogenus IFO 3293.

Gluconobacter melanogenus IFO 3293 cells capable of converting L-sorbose to L-sorbosone were immobilized in polyacrylamide gel. The preferred polymer composition for high activity and stability was determined to contain a total monomer concentration of 7.2% and 16.6% crosslinking agent. No significant differences in optimal conditions for conversion, e.g., pH and temperature, were found in comparison with free cell suspensions. However, in the absence of L-sorbose, the thermal stability of immobilized cells was lower. After the initial loss, the conversion activity of immobilized cells increased, possibly due to lysis, and this increase was related to the polymerization conditions and the incubation temperature for the L-sorbose conversion. The enzymatic activity and stability of the immobilized cells also depended on the physical form of the gel and the aeration levels. Addition of electron acceptors or addition of L-sorbosone to the medium reduced, while addition of neomycin, ampicillin, chloramphenicol, and tetracycline increased the stability of the enzymatic activity.

Electron Transport↗
PubMed1995

Molecular analysis of the phosphoenolpyruvate-dependent L-sorbose: phosphotransferase system from Klebsiella pneumoniae and of its multidomain structure.

We have cloned a 3.4 kb DNA fragment from the chromosome of Klebsiella pneumoniae that codes for a phosphoenolpyruvate-dependent L-sorbose: phosphotransferase system (PTS). The cloned fragment was sequenced and four open reading frames coding for 135 (sorF), 164 (sorB), 266 (sorA) and 274 (sorM) amino acids, respectively, were found. The corresponding proteins could be detected in a T7 overexpression system, which yielded molecular masses of about 14,000 for SorF, 19,000 for SorB, 25,000 for SorA and 27,000 for SorM. SorF and SorB have all the characteristics of soluble and intracellular proteins in accordance with their functions as EIIASor and EIIBSor domains of the L-sorbose PTS. SorA and SorM, by contrast, are strongly hydrophobic, membrane-bound proteins with two to five putative transmembrane helices that alternate with a series of hydrophilic loops. They correspond to domains EIICSor and EIIDSor. The four proteins of the L-sorbose PTS resemble closely (27%-60%) the four subunits of a D-fructose PTS (EIIALev, EIIBLev, EIICLev, and EIIDLev) from Bacillus subtilis and the three subunits of the D-mannose PTS (EIIA,BMan, EIICMan, and EIIDMan) from Escherichia coli K-12. The three systems constitute a new PTS family, and sequence comparisons revealed highly conserved structures for the membrane-bound proteins. A consensus sequence for the membrane proteins was used to postulate a model for their integration into the membrane.

Amino Acid Sequence↗