17 research outputs found
Processamento auditivo em crianças e adolescentes em situação de risco e vulnerabilidade
CONTEXT AND OBJECTIVE: Children and adolescents who live in situations of social vulnerability present a series of health problems. Nonetheless, affirmations that sensory and cognitive abnormalities are present are a matter of controversy. The aim of this study was to investigate aspects to auditory processing, through applying the brainstem auditory evoked potential (BAEP) and behavioral auditory processing tests to children living on the streets, and comparison with a control group. DESIGN AND SETTING: Cross-sectional study in the Laboratory of Auditory Processing, School of Medicine, Universidade de São Paulo. METHODS: The auditory processing tests were applied to a group of 27 individuals, subdivided into 11 children (7 to 10 years old) and 16 adolescents (11 to 16 years old), of both sexes, in situations of social vulnerability, compared with an age-matched control group of 10 children and 11 adolescents without complaints. The BAEP test was also applied to investigate the integrity of the auditory pathway. RESULTS: For both children and adolescents, there were significant differences between the study and control groups in most of the tests applied, with significantly worse performance in the study group, except in the pediatric speech intelligibility test. Only one child had an abnormal result in the BAEP test. CONCLUSIONS: The results showed that the study group (children and adolescents) presented poor performance in the behavioral auditory processing tests, despite their unaltered auditory brainstem pathways, as shown by their normal results in the BAEP test
Lipase production by marine fungus Aspergillus Awamori Nagazawa
The present study indicate the scope for the
utilization of the marine fungus Aspergillus awamori Nagazawa BTMFW 032 for
extracellular lipase production employing submerged fermentation. To the best of
our knowledge this is the first report on lipase production by a marine fungus
employing statistical modeling towards industrial production. The characterization
of purified lipase produced by A. awamori showed stability in organic solvents,
oxidizing agent and reducing agents, I,3-regiospecificity and hydrolytic activity.
These properties make this lipase an ideal candidate for biocatalysis in organic
media for the production of novel compounds such as biodiesel and sugar fatty
esters. 91.4 % reduction in oil and grease content in ayurvedic oil by the treatment
of A. awamori lipase indicates that there is a scope for this enzyme in the treatment
of oil effluents and bioremediation. There is ample scope for further research on
the biochemistry of the enzyme, structure elucidation and enzyme engineering
towards a wide range of further applications, besides enriching scientific
knowledge on marine enzymes.Department of Biotechnology,
Cochin University of Science and Technolog
Cone Snail Glutaminyl Cyclase Sequences from Transcriptomic Analysis and Mass Spectrometric Characterization of Two Pyroglutamyl Conotoxins
The post-translational modification of N-terminal glutamine (Q) to a pyroglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Four complete QC sequences from the species C. araneosus, C. frigidus, C. litteratus, and C. monile and two partial sequences from C. amadis and C. miles have been obtained by analysis of transcriptomic data. Comparisons with mammalian enzyme sequences establish a high level of identity and complete conservation of functional active site residues, including a cluster of hydrogen-bonded acidic side chains. Mass spectrometric analysis of crude venom samples coupled to conotoxin precursor protein sequences obtained from transcriptomic data establishes the presence of pyroglutamyl conotoxins in the venom of C. frigidus and C. amadis. The C. frigidus peptide belongs to the M superfamily, with cysteine framework III, whereas the C. amadis peptide belongs to the divergent superfamily with cysteine framework VI/VII. Additionally, gamma carboxylation of glutamic acid and hydroxylation of proline are observed in the C. frigidus peptide. Mass spectral data are available via ProteomeXchange with identifier PXD009006
Marine Bacteria As Source Of Pigment For Application As Dye In Textile Industry
The textile industry is one amongst the rapidly growing industries world wide, which utilizes enormous
amounts of synthetic dyes. Consequently, the effluent from these textile industries poses serious threat to the
environment which is often very difficult to treat and dispose. This has become a very grave problem in environment
conservation and hence natural pigments have drawn the attention of industry as safe alternative. In this context,
in the present study an attempt was made to bioprospect marine bacteria towards isolation of a suitable and ideal
pigment that could be used as a natural dye. A marine Serratia sp. BTWJ8 was recognized to synthesize enormous
amounts of a prodigiosin-like pigment. The pigment was isolated and characterized for various properties. The
pigment was evaluated for application as a dye in the textile industry. Results of the studies indicated that this
pigment could be used as a natural dye for imparting red-yellow colour to various grades of textile materials. The
colour was observed to be stable after wash performance studiesCochin University of Science and TechnologyProc. Internatl. Conf. Biodiv. Conserv. & Mgt., 2008 : 743 - 4
Contryphan Genes and Mature Peptides in the Venom of Nine Cone Snail Species by Transcriptomic and Mass Spectrometric Analysis
The occurrence of contryphans, a class of single disulfide-bond-containing peptides, is demonstrated by the analysis of the venom of nine species of cone snails. Ten full gene sequences and two partial gene sequences coding for contryphan precursor proteins have been identified by next-generation sequencing and compared with available sequences. The occurrence of mature peptides in isolated venom has been demonstrated by LC-ESI-MS/MS analysis. De novo sequencing of reduced, alkylated contryphans from C. frigidus and C. araneosus provides evidence of sequence variation and post-translational modification, notably gamma carboxylation of glutamic acid. The characterization of Fr965 (C. frigidus) provides a rare example of a sequence lacking Pro at position 5 in the disulfide loop. The widespread occurrence of contryphan genes and mature peptides in the venom of contyr genes and mature peptidesin the venom of diverse cone snails is suggestive of their potential biological significance
Cone Snail Glutaminyl Cyclase Sequences from Transcriptomic Analysis and Mass Spectrometric Characterization of Two Pyroglutamyl Conotoxins
The
post-translational modification of N-terminal glutamine (Q)
to a pyroglutamyl (Z) residue is observed in the conotoxins produced
by marine cone snails. This conversion requires the action of the
enzyme glutaminyl cyclase (QC). Four complete QC sequences from the
species <i>C. araneosus</i>, <i>C. frigidus, C. litteratus</i>, and <i>C. monile</i> and two partial sequences from <i>C. amadis</i> and <i>C. miles</i> have been obtained
by analysis of transcriptomic data. Comparisons with mammalian enzyme
sequences establish a high level of identity and complete conservation
of functional active site residues, including a cluster of hydrogen-bonded
acidic side chains. Mass spectrometric analysis of crude venom samples
coupled to conotoxin precursor protein sequences obtained from transcriptomic
data establishes the presence of pyroglutamyl conotoxins in the venom
of <i>C. frigidus</i> and <i>C. amadis</i>. The <i>C. frigidus</i> peptide belongs to the M superfamily, with cysteine
framework III, whereas the <i>C. amadis</i> peptide belongs
to the divergent superfamily with cysteine framework VI/VII. Additionally,
gamma carboxylation of glutamic acid and hydroxylation of proline
are observed in the <i>C. frigidus</i> peptide. Mass spectral
data are available via ProteomeXchange with identifier PXD009006
Production, purification and partial characterization of a novel protease from marine Engyodontium album BTMFS10 under solid state fermentation
Engyodontium album isolated from marine sediment produced protease, which was active at pH 11. Process parameters influencing the
production of alkaline protease by marine E. album was optimized. Particle size of <425 mm, 60% initial moisture content and incubation at 25 8C
for 120 h were optimal for protease production under solid state fermentation (SSF) using wheat bran. The organism has two optimal pH (5 and 10)
for maximal enzyme production. Sucrose as carbon source, ammonium hydrogen carbonate as additional inorganic nitrogen source and amino acid
leucine enhanced enzyme production during SSF. The protease was purified and partially characterized. A 16-fold purified enzyme was obtained
after ammonium sulphate precipitation and ion-exchange chromatography. Molecular weight of the purified enzyme protein was recorded
approximately 38 kDa by SDS-PAGE. The enzyme showed maximum activity at pH 11 and 60 8C. Activity at high temperature and high alkaline
pH suggests suitability of the enzyme for its application in detergent industryCochin University of Science and TechnologyProcess Biochemistry 41 (2006) 956–96
Protease inhibitor from Moringa oleifera leaves: Isolation, purification, and characterization
Protease inhibitors have great demand in medicine and biotechnology. We report here the purification
and characterization of a protease inhibitor isolated from mature leaf extract of Moringa oleifera that
showed maximum inhibitor activity. The protease inhibitor was purified to 41.4-fold by Sephadex G75
and its molecular mass was calculated as 23,600 Da. Inhibitory activity was confirmed by dot-blot and
reverse zymogram analyses. Glycine, glutamic acid, alanine, proline and aspartic acid were found as the
major amino acids of the inhibitor protein. Maximal activity was recorded at pH 7 and at 40 ◦C. The
inhibitor was stable over pH 5–10; and at 50 ◦C for 2 h. Thermostability was promoted by CaCl2, BSA
and sucrose. Addition of Zn2+ and Mg2+, SDS, dithiothreitol and -mercaptoethanol enhanced inhibitory
activity, while DMSO and H2O2 affected inhibitory activity. Modification of amino acids at the catalytic
site by PMSF and DEPC led to an enhancement in the inhibitory activity. Stoichiometry of trypsin–protease
inhibitor interaction was 1:1.5 and 0.6 nM of inhibitor effected 50% inhibition. The low Ki value (1.5 nM)
obtained indicated scope for utilization of M. oliefera protease inhibitor against serine proteasesCochin University of Science and TechnologyProcess Biochemistry 46 (2011) 2291–230
Propyl Gallate Synthesis Using Acidophilic Tannase and Simultaneous Production of Tannase and Gallic Acid by Marine Aspergillus awamori BTMFW032
Marine Aspergillus awamori BTMFW032, recently reported by us, produce
acidophilic tannase as extracellular enzyme. Here, we report the application of this
enzyme for synthesis of propyl gallate by direct transesterification of tannic acid and in
tea cream solubilisation besides the simultaneous production of gallic acid along with
tannase under submerged fermentation by this fungus. This acidophilic tannase enabled
synthesis of propyl gallate by direct transesterification of tannic acid using propanol as
organic reaction media under low water conditions. The identity of the product was
confirmed with thin layer chromatography and Fourier transform infrared spectroscopy.
It was noted that 699 U/ml of enzyme could give 60% solubilisation of tea cream within
1 h. Enzyme production medium was optimized adopting Box–Behnken design for
simultaneous synthesis of tannase and gallic acid. Process variables including tannic acid,
sodium chloride, ferrous sulphate, dipotassium hydrogen phosphate, incubation period
and agitation were recognized as the critical factors that influenced tannase and gallic acid
production. The model obtained predicted 4,824.61 U/ml of tannase and 136.206 μg/ml gallic
acid after 48 h of incubation, whereas optimized medium supported 5,085 U/ml tannase and
372.6 μg/ml of gallic acid production after 36 and 84 h of incubation, respectively, with a
15-fold increase in both enzyme and gallic acid production. Results indicated scope for
utilization of this acidophilic tannase for transesterification of tannic acid into propyl gallate, tea
cream solubilisation and simultaneous production of gallic acid along with tannaseCochin University of Science and TechnologyAppl Biochem Biotechnol (2011) 164:612–628
DOI 10.1007/s12010-011-9162-
Lipase from marine Aspergillus awamori BTMFW032: Production, partial purification and application in oil effluent treatment
Marine fungus BTMFW032, isolated from seawater and identified as Aspergillus awamori, was observed to
produce an extracellular lipase, which could reduce 92% fat and oil content in the effluent laden with oil.
In this study, medium for lipase production under submerged fermentation was optimized statistically
employing response surface method toward maximal enzyme production. Medium with soyabean meal-
0.77% (w/v); (NH4)2SO4-0.1 M; KH2PO4-0.05 M; rice bran oil-2% (v/v); CaCl2-0.05 M; PEG 6000-0.05% (w/v);
NaCl-1% (w/v); inoculum-1% (v/v); pH 3.0; incubation temperature 35 8C and incubation period-five days
were identified as optimal conditions for maximal lipase production. The time course experiment under
optimized condition, after statistical modeling, indicated that enzyme production commenced after
36 hours of incubation and reached a maximum after 96 hours (495.0 U/ml), whereas maximal specific
activity of enzyme was recorded at 108 hours (1164.63 U/mg protein). After optimization an overall 4.6-
fold increase in lipase production was achieved. Partial purification by (NH4)2SO4 precipitation and ion
exchange chromatography resulted in 33.7% final yield. The lipase was noted to have a molecular mass
of 90 kDa and optimal activity at pH 7 and 40 8C. Results indicated the scope for potential application of
this marine fungal lipase in bioremediation.Cochin University of Science & TechnologyNew Biotechnology Volume 28, Number 6 October 201