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Biomedical subjects

C Suresh

Publications and source records attributed to C Suresh.

10 recordsLinked to original sources

Bacteriology of diabetic foot lesions.

Infection plays a pivotal role in enhancing a diabetic foot at risk toward amputation. Effective antibiotic therapy against the offending pathogens is an important component of treatment of diabetic foot infections. Recognition of the pathogen is always difficult as the representative deep tissue sample for culture is surrounded by ulcer surface harbouring colonies of organisms frequently labelled as skin commensals. The emergent of resistant strains represents a compounding problem standing against efforts to prevent amputation. This study was undertaken to identify the pathogens associated with diabetic foot infection in terms of their frequency and sensitivity against certain commonly used antibiotics. Forty-four consecutive patients with open diabetic foot infections had wound swab taken for culture and sensitivity testing. Cultures positive were observed in 89% of the cases with Staphylococcus aureus, Klebsiella pneumoniae, Pseudomonas aeroginosa encountered in 20%, 14% and 14% of cases respectively. Mixed growths were isolated in 6% of cultures. All Staphylcoccus aureus isolates were resistant to Penicillin but 80% were sensitive to Erythromycin and Co-trimoxazole. Klebsiella pneumoniae isolates were sensitive to Methicillin and Gentamycin in 80% and 60% of cases respectively, and resistant to Ampicillin and Ceftazidime in 83% and 50% respectively. All Pseudomonas aeroginosa isolates were sensitive to Amikacin and Ciprofloxacin but 50% were resistant to Gentamycin. There was no single antibiotic possessing good coverage for all common organisms isolated from diabetic foot lesions. Staphylococcus aureus remains the predominant cause of diabetic foot infections followed by Klebsiela pneumonia and Pseudomonas aeroginosa. Most infections are monomicrobial. The emergence of multiresistant organisms is a worrying feature in diabetic foot infections.

Diabetic Foot↗

Evidence that the glucoamylases and alpha-amylase secreted by Aspergillus niger are proteolytically processed products of a precursor enzyme.

A 125-kDa starch hydrolysing enzyme of Aspergillus niger characterised by its ability to dextrinise and saccharify starch [Suresh et al. (1999) Appl. Microbiol. Biotechnol. 51, 673-675] was also found to possess activity towards raw starch. Segregation of these activities in the 71-kDa glucoamylase and a 53-kDa alpha-amylase-like enzyme supported by antibody cross-reactivity studies and the isolation of mutants based on assay screens for the secretion of particular enzyme forms revealed the 125-kDa starch hydrolysing enzyme as their precursor. N-terminal sequence analysis further revealed that the 71-kDa glucoamylase was the N-terminal product of the precursor enzyme. Immunological cross reactivity of the 53-kDa amylase with antibodies raised against the precursor enzyme but not with the 71- and 61-kDa glucoamylase antibodies suggested that this enzyme activity is represented by the C-terminal fragment of the precursor. The N-terminal sequence of the 53-kDa protein showed similarity to the reported Taka amylase of Aspergillus oryzae. Antibody cross-reactivity to a 10-kDa non-enzymic peptide and a 61-kDa glucoamylase described these proteins as products of the 71-kDa glucoamylase. Identification of only the precursor starch hydrolysing enzyme in the protein extracts of fungal protoplasts suggested proteolytic processing in the cellular periplasmic space as the cause for the secretion of multiple forms of amylases by A. niger.

Amino Acid Sequence↗

Separation and direct detection of raw and gelatinized starch hydrolyzing activities of glucoamylase on isoelectric focusing gels.

A procedure to detect raw and gelatinized starch activities of glucoamylase on isoelectric focusing (IEF) gels by using 2, 3, 5-triphenyltetrazolium chloride is described. The reagent reacts with the reducing group of glucose released by glucoamylase from the substrate starch. Using the reaction, production of glucoamylase by Aspergillus niger was detected on 10% IEF gels within a pH range of 2.5-9.5. Since the method can detect raw and gelatinized starch activities of glucomylase associated with 1 microg protein, it will be useful for enzyme engineering studies that involve screening of various mutations.

Aspergillus niger↗

Characterisation of a starch-hydrolysing enzyme of Aspergillus niger.

A UV-induced mutant strain of Aspergillus niger (CFTRI-1105-U9) overproduced a starch-hydrolysing enzyme with properties characteristically different from the known amylases of the fungus. The purified enzyme of 4.0 pI had an apparent molecular mass of 125 kDa and it dextrinised starch and then saccharified the dextrins. Patterns of the enzyme activity on starch, resulting in glucose at 60 degrees C and glucose, maltose and maltodextrins at 70 degrees C as primary products, suggested significant applications for the enzyme in starch-processing industries.

Aspergillus niger↗

An enzyme-linked immunosorbent assay for the estimation of fungal biomass during solid-state fermentation.

An enzyme-linked immunosorbent assay for sensitive, specific and quantitative estimation of fungal biomass during solid-state fermentation is described. Using this method, differential growth rates and colonization of the substrate can be studied. The assay has potential application for the efficient monitoring of solid-state fermentation involving specific fungus, for which available methods are not adequate.

Antibodies, Fungal↗

Clinical evaluation of gold foil as an apical sealing material for replantation.

Intentional replantation of mandibular molars was performed in forty patients. Different materials were used for sealing the apex. Healing was assessed by measuring biting force at 2-month intervals for up to 6 months. Gold foil was found to be the best material for apical sealing when improvement in biting force was used as the criterion.

Adolescent↗