Assessment of hydrolysis of cheese whey and use of hydrolysate for bioproduction of carotenoids by Sporidiobolus salmonicolor CBS 2636

BACKGROUND: The increasing industrial demand for carotenoids has led to growing interest in their bioproduction. The need to reduce production costs has encouraged the use of low‐cost agroindustrial substrates. In this context, this work studied the pretreatment of Mozzarella cheese whey and the use of the pretreated whey as fermentation medium for the bioproduction of carotenoids by Sporidiobolus salmonicolor CBS 2636. RESULTS: Bioproduction was carried out in an orbital shaker using a 10 mL L^?1 inoculum, incubation at 25 °C and a stirring rate of 180 rpm for 120 h in a non‐illuminated environment. The carotenoids were recovered using liquid N₂ combined with dimethyl sulfoxide for cell rupture and an acetone/methanol mixture (7:3 v/v) for extraction. The maximum concentration of total carotenoids obtained was 590.4 µg L^?1 in a medium with 900 g L^?1 cheese whey hydrolysate and 4 g L^?1 K₂HPO₄ at 180 rpm, 25 °C and pH 4. CONCLUSION: The use of enzyme‐hydrolysed cheese whey was more effective in carotenoid bioproduction by S. salmonicolor CBS 2636 than the use of acid‐hydrolysed cheese whey. The concentration of total carotenoids obtained with the enzymatic hydrolysate was six times higher than that obtained with the acid hydrolysate. Copyright © 2009 Society of Chemical Industry     

Comparison of technetium-99m-sestamibi scintimammography with contrast-enhanced MRI for diagnosis of breast lesions

A carboxylesterase [2,3,4,6-tetra-O-acetyl-1-[(N-acetyl-N-phenylamino)oxy]-1-deoxy-beta-D-g lucopyranoside (GPA) O-deacetylase] from a culture product of Aspergillus oryzae (Taka diastase) was purified 8500-fold with a yield of 3%. The molecular mass of the purified enzyme was shown to be 35 +/- 1 kDa by SDS/PAGE. The enzyme shows a selective O-deacetylation activity of GPA to give the fully O-deacetylated glucoside. Among the substrates tested, the enzyme did not hydrolyze benzoyl and phenylacetyl esters and acetamides. In the hydrolysis of p-nitrophenyl esters, the acyl preference is acetyl > propionyl > butyryl, judging from the Vmax/Km values. A good correlation between log(Vmax/Km) and the Taft's Es constant of the alkyl group of the acyl moiety was obtained. The optimum pH was around 7.3 at 37 degrees C, and the enzyme was inhibited by mercuric chloride, p-chloromercuribenzoate and diisopropyl fluorophosphate. This enzyme should be useful for the selective removal of acetyl groups that serve to protect hydroxyl groups during carbohydrate synthesis.     

D2-dopamine-receptor occupancy during treatment with haloperidol decanoate

The experience of development of a protocol for the nutritional management of postoperative surgical patients is described. The protocol was developed with the involvement of all the professionals working in the ward (nurses, anesthetists, dieticians and surgeons). It contained indications on how and when re-start feeding for non complicated surgical patients. Specific indications for diabetic, hypertensive and nephropatic patients were devised. The protocol was readily adopted and successfully implemented, indicating that the strategy of sharing and discussing problems involving all the professionals leads to a better chance of success.     

Iodine-123-iodobenzamide binding in parkinsonism: reduction by dopamine agonists but not L-Dopa

The aim of the present study was to investigate the effect of treatment with L-Dopa or a dopamine agonist, or both, on specific striatal 123I-iodobenzamide (IBZM) binding using an intraindividual longitudinal design. METHOD: We prospectively studied the effect of dopaminomimetic treatment on specific [123I]IBZM binding measured by SPECT in 29 patients with a clinical diagnosis of Parkinson's disease, none of whom had previously received dopaminomimetic drugs. The patients had been selected on the basis of normal subsequent specific [123I]IBZM binding, semiquantitatively calculated as the basal ganglia/frontal cortex ratio, and a positive response to the dopamine agonist apomorphine before initiation of dopaminomimetic therapy. A second 123I-IBZM SPECT investigation was performed after 3-6 mo of treatment with L-Dopa or a dopamine agonist, or both. RESULTS: Specific [123I]IBZM binding was unchanged in 10 patients treated with L-Dopa alone. However, after treatment with a dopamine agonist there was a significant decline in specific [123I]IBZM binding (p < 0.05). After treatment with a combination of L-Dopa and a dopamine agonist, specific [123I]IBZM binding was reduced without reaching a level of significance (p = 0.08). CONCLUSION: Short-term treatment with a dopamine agonist but not with L-Dopa reduces specific [123I]IBZM binding. Therefore, before performing an [123I]IBZM SPECT scan in patients previously treated with dopaminomimetic drugs, dopamine agonists should be discontinued.