Results of data gathered at a smoking cessation counselling stand in the Dublin Dental University Hospital on Mouth Cancer Awareness Day 2012.

INTRODUCTION: The addictive aspect of smoking is well acknowledged. Research has shown that interventions by healthcare professionals have been shown to be effective and that smokers will benefit from smoking cessation counselling before, during and after their quit attempts. Dental hygienists, as part of the healthcare team, are well positioned to provide this counselling. MATERIAL AND METHODS: A questionnaire was completed by patients, staff, students and members of the public, during Mouth Cancer Awareness Day 2012 in the Dublin Dental University Hospital to assess the prevalence of smoking as well as the history of smoking and quit attempts by current and former smokers. RESULTS: The prevalence of smoking was lower than the national average. A total of 18.3% of those surveyed were smokers, 25% were former smokers, and 68% of the smokers had their first cigarette within 30 minutes of waking, indicating high dependence. DISCUSSION AND CONCLUSIONS: The majority of the smokers (79%) had attempted to quit. Stress was the most common reason for lapsing. The most common reasons for smoking cessation were health issues. The public is well disposed to receive information regarding smoking and the methods available to quit by healthcare professionals on health awareness days such as Mouth Cancer Awareness Day.

Congenital sialidosis.

Congenital sialidosis is a rare disease resulting from the absence of neurominidase and presenting with hydrops fetalis, hepatosplenomegaly, dysmorphic features, vacuolated lymphocytes and extensive vacuolation of the connective tissue. Elevated levels of sialooligosaccharides in the urine is characteristic. We describe a newborn baby with congenital sialidosis and discuss the difficulties in reaching the diagnosis.

Kinetic investigation of penicillin G acylase from a mutant strain of Escherichia coli ATCC 11105 immobilized on oxirane-acrylic beads.

Highly purified penicillin G acylase from a mutant derivative of Escherichia coli ATCC 11105 was immobilized on oxirane-acrylic beads by covalent binding via oxirane groups. The highest specific activity, (322 U g-1 dry matrix at 40 degrees C and at pH 8.0) was obtained by using an enzyme solution having 13.8 U mg-1 specific activity and 72.73 mg total protein. The efficiency of immobilization was 95.8%. Kinetic parameters of immobilized penicillin G acylase were determined at the same pH and temperature by a preparation having 8.1 mg bound protein. The Km value and substrate inhibition constant of the enzyme were found to be 11.36 mmol dm-3 and 680 mmol dm-3 penicillin G respectively. Phenylacetic acid and 6-aminopenicillanic acid were estimated as the competitive and non-competitive inhibitors of the enzyme and their inhibition constants were found to be 90 mmol dm-3 phenylacetic acid and 76.1 mmol dm-3 for 6-aminopenicillanic acid. The activation energy of the hydrolytic reaction was calculated to be 7.75 kcal mol-1. The immobilized enzyme showed highest activity at pH 8.0 and at 55 degrees C. The enzyme was stable when incubated at 4 degrees C for one day at a pH range of 5.0 to 9.0. Thermal stability (over 30 min) was observed up to 40 degrees C but decreased at higher temperatures and was almost absent at 60 degrees C. A 95% conversion rate was observed at 28 degrees C and at 40 degrees C with 60 and 30 min operation times respectively. Operational stability of the enzyme was improved further with dithiothreitol treatment. Activity loss was around 5% following 20 cycles of repeated use of the enzyme at 40 degrees C. No significant loss of activity was observed at 28 degrees C when the enzyme was used for 20 cycles. 6-Aminopenicillanic acid in the reaction mixture was observed to be stable during conversion reactions which were carried out at both temperatures.