PubMed Health⌕ Search

Biomedical subjects

S H Imam

Publications and source records attributed to S H Imam.

15 recordsLinked to original sources

Composite films based on biorelated agro-industrial waste and poly(vinyl alcohol). Preparation and mechanical properties characterization.

As a part of an ongoing project on the production of composite materials based on poly(vinyl alcohol) (PVA) and polymeric materials from renewable resources, the present paper reports on the incorporation of agricultural waste materials as organic fillers in a film matrix based on PVA as continuous phase. In this study lignocellulosic fibers byproducts, derived from sugar cane (SC) and apple (AP) and orange (OR) fruit juice extraction, were cast from PVA aqueous solutions. The effect of fiber type and composition on the relative properties of cast films was evaluated and compared. OR resulted to be suitable for blending in higher amounts by weight than SC and AP. Glycerol and urea were added as plasticizing agents and were observed to be effective in giving flexible films. Additionally, cornstarch was added to further increase the composition of polymers from renewable resources in cost-effective and ecoefficient composite film formulations. The prepared films resulted sensitive to moisture and water. To reduce water sensitivity, hexamethoxymethylmelamine (HMMM) was tested as a cross-linking agent for the present composite formulations. Cross-linked films exhibited significant improvement in water-resistance that can be taken as a tuneable structural feature for customized applications. The mechanical properties of the prepared composite films (elongation at break, tensile strength, Young modulus) were found to be dependent upon the nature and content of the filler and on environmental conditions.

Agriculture↗

Degradation of starch-poly(beta-hydroxybutyrate-co-beta-hydroxyvalerate) bioplastic in tropical coastal waters.

Extruded bioplastic was prepared from cornstarch or poly(beta-hydroxybutyrate-co-beta-hydroxyvalerate) (PHBV) or blends of cornstarch and PHBV. The blended formulations contained 30 or 50% starch in the presence or absence of polyethylene oxide (PEO), which enhances adherence of starch granules to PHBV. Degradation of these formulations was monitored for 1 year at four stations in coastal water southwest of Puerto Rico. Two stations were within a mangrove stand. The other two were offshore; one of these stations was on a shallow shoulder of a reef, and the other was at a location in deeper water. Microbial enumeration at the four stations revealed considerable flux in the populations over the course of the year. However, in general, the overall population densities were 1 order of magnitude less at the deeper-water station than at the other stations. Starch degraders were 10- to 50-fold more prevalent than PHBV degraders at all of the stations. Accordingly, degradation of the bioplastic, as determined by weight loss and deterioration of tensile properties, correlated with the amount of starch present (100% starch >50% starch > 30% starch > 100% PHBV). Incorporation of PEO into blends slightly retarded the rate of degradation. The rate of loss of starch from the 100% starch samples was about 2%/day, while the rate of loss of PHBV from the 100% PHBV samples was about 0.1%/day. Biphasic weight loss was observed for the starch-PHBV blends at all of the stations. A predictive mathematical model for loss of individual polymers from a 30% starch-70% PHBV formulation was developed and experimentally validated. The model showed that PHBV degradation was delayed 50 days until more than 80% of the starch was consumed and predicted that starch and PHBV in the blend had half-lives of 19 and 158 days, respectively. Consistent with the relatively low microbial populations, bioplastic degradation at the deeper-water station exhibited an initial lag period, after which degradation rates comparable to the degradation rates at the other stations were observed. Presumably, significant biodegradation occurred only after colonization of the plastic, a parameter that was dependent on the resident microbial populations. Therefore, it can be reasonably inferred that extended degradation lags would occur in open ocean water where microbes are sparse.

Biodegradation, Environmental↗

Binding of extracellular carboxymethylcellulase activity from the marine shipworm bacterium to insoluble cellulosic substrates.

The binding of extracellular endoglucanase, a carboxymethylcellulase (CMCase), produced by the marine shipworm bacterium to insoluble cellulose substrates was investigated. Up to 70% of CMCase activity bound to cellulosic substrates, and less than 10% bound to noncellulosic substrates. CMCase binding to cellulose was enhanced in basal salt medium or sodium phosphate buffer containing 0.5 M NaCl. Increased cellulose particle size correlated with decreased CMCase binding. Also, cellulose treated with either 5 N NaOH or commercial cellulase reduced the CMCase binding to these surfaces. Pretreatment of CMCase preparations with 0.01% sodium dodecyl sulfate, 5% beta-mercaptoethanol, and 5 mM EDTA or ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) had little effect on binding to cellulose. While pretreatment of CMCase with trypsin, chymotrypsin, and pronase had little effect on CMCase enzymatic activity, the ability to bind to cellulose was greatly diminished by these treatments.

Journal Article↗

Adhesion of Lactobacillus amylovorus to Insoluble and Derivatized Cornstarch Granules.

Approximately 70% of the cells in a suspension of the amylolytic bacterium Lactobacillus amylovorus bind to cornstarch granules within 30 min at 25 degrees C. More than 60% of the bound bacteria were removed by formaldehyde (2%) or glycine (1 M) at pH 2.0. More than 90% of the bound bacteria were removed by MgCl(2) (2 M; pH 7.0). Binding of L. amylovorus to cornstarch was inhibited in heat-killed cells and in cells that had been pretreated with glutaraldehyde, formaldehyde, sodium azide, trypsin, or 1% soluble potato starch. Bacterial binding to cornstarch appeared to correlate with both the concentration of cornstarch in the suspension and the amylose content in the granules. The ability of L. amylovorus to adhere to cornstarch granules was reduced for granules that had been extracted with HCl-ethanol, HCl-methanol, HCl-propanol, or HCl-butanol. Chemical derivatization of cornstarch resulted in a wide variety of adhesion responses by these bacteria. For example, 2-O-butyl starch (degree of substitution, 0.09) enhanced adhesion, whereas two palmitate starches (degree of substitution, 0.48 and 0.09) exhibited reduced adhesion activities. 2-O-(2-hydroxybutyl) starch and starch-poly(ethylene-co-acrylic acid) ester showed adhesion activities similar to those of the nonderivatized starch controls.

Journal Article↗

Adhesion of an Amylolytic Arthrobacter sp. to Starch-Containing Plastic Films.

Cells of the amylolytic bacterium KB-1 (thought to be an Arthrobacter sp.) adhered ( approximately 70%) to the surface of plastic films composed of starch-poly (methylacrylate) graft copolymer (starch-PMA), but did not adhere (<10%) to films composed of polymethylacrylate (PMA), polyethylene (PE), carboxymethyl cellulose, or a mixture of PE plus poly (ethylene-coacrylic acid) (EAA), starch plus PE, or starch plus PE and EAA. About 30% of the cells adhered to gelatinized insoluble starch. Dithiothreitol (5 mM), EDTA (5 mM), and soluble starch (1%, wt/vol) had little effect on the adhesion of KB-1 cells to starch-PMA films. However, glutaraldehyde-fixed cells, azide-treated cells, and heat-killed cells did not bind to starch-PMA plastic, suggesting that the observed adhesion required cell viability. Culture supernatant from 5-day-old KB-1 cultures contained a proteolytic enzyme that inhibited cell adhesion to starch-PMA plastics. Trypsin-treated KB-1 cells also lost their ability to bind to starch-PMA plastic. When washed free of trypsin and suspended in fresh medium, trypsin-treated bacteria were able to recover adhesion activity in the absence, but not in the presence, of the protein synthesis inhibitor chloramphenicol. These results suggested that adhesion of KB-1 to starch-PMA plastic may be mediated by a cell surface protein. Although KB-1 bacteria bound to starch-PMA plastic, they did not appear to degrade starch in these films. Evidence of starch degradation was observed for starch-PE-EAA plastics, where <10% of the bacteria was bound, suggesting that cell adhesion may not be a prerequisite for degradation of some starch-containing plastics.

Journal Article↗

Adhesive properties of a symbiotic bacterium from a wood-boring marine shipworm.

Adhesive properties of a cellulolytic, nitrogen-fixing bacterium isolated from a marine shipworm by Waterbury et al. (J. B. Waterbury, C. B. Calloway, and R. D. Turner, Science 221:1401-1403, 1983) are described. S-labeled cells of the shipworm bacterium bound preferentially to Whatman no. 1 cellulose filter paper, compared with its binding to other cellulose substrata or substrata lacking cellulose. The ability of the bacteria to bind to Whatman no. 1 filter paper was significantly reduced by glutaraldehyde or heat treatment of cells. Pretreatment of cells with azide, valinomycin, gramicidin-D, bis-hexafluoroacetylacetone (1799), or carbonyl cyanide-p-trifluoromethoxyphenylhydrazone inhibited adhesion activity. Cells pretreated with pronase or trypsin also exhibited reduced binding activity, but chymotrypsin and peptidase had no effect on adhesion activity. Cellodextrins and methyl cellulose 15 inhibited the adhesion of shipworm bacteria to filter paper, whereas glucose, cellobiose, and soluble carboxymethyl cellulose had no significant effect. The divalent cation chelators EDTA and EGTA [ethylene glycol-bis(beta-aminoethyl ether)-N,N,N'N'-tetraacetic acid] had little or no effect on adhesive properties of shipworm bacteria. Also, preabsorbing the substratum with extracellular endoglucanase isolated from the shipworm bacterium or 1% bovine serum albumin had no apparent effect on bacterial binding. Low concentrations (0.01%) of sodium dodecyl sulfate solubilized a fraction from whole cells, which appeared to be involved in cellular binding activity. After removal of sodium dodecyl sulfate, several proteins in this fraction associated with intact cells. These cells exhibited up to 50% enhanced binding to filter paper in comparison to cells which had not been exposed to the sodium dodecyl sulfate-solubilized fraction.

Journal Article↗

Activation of the cell wall degrading protease, lysin, during sexual signalling in Chlamydomonas: the enzyme is stored as an inactive, higher relative molecular mass precursor in the periplasm.

During the mating reaction in Chlamydomonas reinhardtii mating type plus and mating type minus gametes adhere to each other via adhesion molecules on their flagellar surfaces. This adhesive interaction induces a sexual signal leading to release of a cell wall degrading enzyme, lysin, that causes wall release and degradation. In this article, we describe the preparation of a polyclonal antibody against the 60,000-Mr lysin polypeptide excised from SDS-PAGE gels. After absorption of the IgG with cell walls to remove antibodies against a carbohydrate epitope common to several Chlamydomonas glycoproteins, the immune IgG reacted with the 60,000-Mr polypeptide, and a 47,000-Mr species that we show here was immunologically cross-reactive with the 60,000-Mr molecule. By use of several fractionation methods including ion exchange and molecular sieve chromatography, sucrose gradient centrifugation, and affinity chromatography, we showed that the 60,000-Mr antigen copurified with lysin activity, thereby demonstrating that the antibody was indeed directed against the enzyme. Immunoblot experiments on suspensions of nonmating and mating gametes showed that the 60,000-Mr antigen was missing in the nonmating gametes. Instead, they contained a 62,000-Mr antigen that was not present in suspensions of mating gametes that had undergone sexual signalling. Furthermore, nonmating gametes whose walls were removed with exogenously added lysin did not contain either form of the antigen. We also found that the 62,000-Mr form of the antigen, which could be released from gametes by freeze-thawing, did not have wall degrading activity. These results indicate that lysin in gametes is stored in the periplasm as a higher relative molecular mass, inactive precursor and also that sexual signalling induces conversion of this molecule to a lower relative molecular mass, active enzyme. This may be a novel example of processing of an extracellular protease induced by cell contact.

Antibody Specificity↗

The Chlamydomonas cell wall degrading enzyme, lysin, acts on two substrates within the framework of the wall.

The Chlamydomonas cell wall is a multilayered, extracellular matrix containing 20-25 proteins and glycoproteins, many of which are highly enriched in hydroxyproline. 80-90% of the wall protein is located in a crystalline portion of the wall that is soluble in sarkosyl-urea solutions as well as in chaotropic salts. Although the wall has no cellulose it contains a noncrystalline, highly insoluble framework portion that is responsible for the integrity and overall shape of the wall. In the present report we show that the framework of the wall is composed of two components that are acted upon by lysin, a wall degrading enzyme released by mating gametes. One, which makes up the major portion of the framework, is insoluble upon boiling in SDS-PAGE sample buffer. Lysin treatment of this portion leads to its physical degradation and the concomitant appearance of several SDS-dithiothreitol-soluble polypeptides ranging in relative molecular mass from greater than 400,000 to less than 60,000. The second component is the flagellar collar. This hollow cylinder composed of striated fibers aligned in parallel array serves as the tunnel in the wall through which the flagella protrude. Our evidence indicates that the primary collar polypeptide is a 225,000-Mr molecule that itself has at least two functional domains. One domain, contained in a 185,000-Mr fragment, permits the self-association of the molecules to form the main body of the collar. The second part of the molecule anchors the collar to the wall framework via sarkosyl-urea-insensitive, SDS-dithiothreitol-sensitive linkages.

Cell Wall↗

Degradation of the framework of the Chlamydomonas cell wall by proteases present in a commercially available alpha-amylase preparation.

A commercially available alpha-amylase derived from Bacillus licheniformis contained an enzymatic activity able to degrade the inner portion or framework of the cell wall of Chlamydomonas reinhardtii. Both the wall-degrading activity and the contaminating protease were destroyed by heating the alpha-amylase preparation at 90 degrees C for 30 min. Since the alpha-amylase activity was uneffected by heat treatment, we conclude that it was not the alpha-amylase but the contaminating protease in the preparation that was responsible for the cell wall-degrading activity.

Bacillus↗

The Chlamydomonas cell wall: characterization of the wall framework.

The cell wall of the biflagellate alga Chlamydomonas reinhardtii is a multilayered, extracellular matrix composed of carbohydrates and 20-25 polypeptides. To learn more about the forces responsible for the integrity of this cellulose-deficient cell wall, we have begun studies to identify and characterize the framework of the wall and to determine the effects of the cell wall-degrading enzyme, lysin, on framework structure and protein composition. In these studies we used walls released into the medium by mating gametes. When isolated shed walls are degraded by exogenously added lysin, no changes are detected in the charge or molecular weight of the 20-25 wall proteins and glycoproteins when analyzed on one- and two-dimensional polyacrylamide gels, which suggests that degradation of these shed walls is due either to cleavage of peptide bonds very near the ends of polypeptides or that degradation occurs via a mechanism other than proteolysis. Incubation of walls with Sarkosyl-urea solutions removes most of the proteins and yields thin structures that appear to be the frameworks of the walls. Analysis by polyacrylamide gel electrophoresis shows that the frameworks are highly enriched in a polypeptide of Mr 100,000. Treatment of frameworks with lysin leads to their degradation, which indicates that this part of the wall is a substrate for the enzyme. Although lysin converts the Mr 100,000 polypeptide from an insoluble to a soluble form, there is no detectable change in Mr of the framework protein. Solubilization in the absence of lysin requires treatment with SDS and dithiothreitol at 100 degrees C. These results suggest that the Chlamydomonas cell wall is composed of two separate domains: one containing approximately 20 proteins held together by noncovalent interactions and a second domain, containing only a few proteins, which constitutes the framework of the wall. The result that shed walls can be solubilized by boiling in SDS-dithiothreitol indicates that disulfide linkages are critical for wall integrity. Using an alternative method for isolating walls from mechanically disrupted gametes, we have also shown that a wall-shaped portion of these unshed walls is insoluble under the same conditions in which shed walls are soluble. One interpretation of these results is that wall release during mating and the wall degradation that follows may involve distinct biochemical events.

Carbohydrates↗

Specificity of marine microbial surface interactions.

The macromolecular surface components involved in intraspecific cell surface interactions of the green microalga Chlorella vulgaris and closely associated bacteria were investigated. The specific surface attachment between this alga and its associated bacteria is mediated by lectin-like macromolecules associated with the surfaces of these cells. The binding activity of these surface polymers was inhibited by specific simple sugars; this suggests the involvement of specific receptor-ligand binding sites on the interactive surfaces. Epifluorescent microscopic evaluation of bacteria-alga interactions in the presence and absence of the macromolecules that mediate these interactions showed that the glycoproteins active in these processes were specific to the microbial sources from which they were obtained. The demonstration and definition of the specificity of these interactions in mixed microbial populations may play an important role in our understanding of the dynamics of marine microbial populations in the sea.

Adhesiveness↗

Increased inhibitory action against adenosine 5'-triphosphate in the isolated taenia of the guinea-pig caecum by substitution in the A-ring of 2-phenylisatogen.

1 The ability of a series of 17 isatogen derivatives to relax smooth muscle, inhibit adenosine 5'-diphosphate (ADP)-stimulated respiration in isolated mitochondria and to antagonize the inhibitory effects of adenosine 5'-triphosphate (ATP) on smooth muscle was measured. 2 Substitution in the 4- and 7-positions of the A-ring gave compounds that were strong inhibitors of mitochondrial ATP synthesis and potent, non-specific smooth muscle relaxants. The compounds also possessed ATP-receptor blocking activity. 3 Substitution in the 5- and 6-positions of the A-ring decreased both the relaxant effect on smooth muscle and inhibition of ATP synthesis, whilst enhancing ATP-receptor antagonism. 4 In a series of 6-substituted 2-phenylisatogens, 6-methoxy-2-phenylisatogen was the most effective ATP-receptor antagonist. This compound also showed the greatest separation of the desired pharmacological activity (ATP-receptor blockade) from the other two activities (smooth muscle relaxation and inhibition of mitochondrial ATP synthesis).

Adenosine Triphosphate↗

Starch graft poly(methyl acrylate) loose-fill foam: preparation, properties and degradation.

Starch graft poly(methyl acrylate) (S-g-PMA) was prepared by ceric ion initiation of methyl acrylate in an aqueous corn starch slurry (prime starch) which maximized the accessibility of the starch for graft polymerization. A new ceric ion reaction sequence was established as starch-initiator-methyl acrylate followed by addition of a small amount of ceric ion solution when the graft polymerization was almost complete to quench the reaction. As a result of this improved procedure, no unreacted methyl acrylate monomer remained, and thus, essentially no ungrafted poly(methyl acrylate) homopolymer was formed in the final grafted product. Quantities of the high purity S-g-PMA so prepared in pilot scale were converted to resin pellets and loose-fill foam by single screw and twin screw extrusion. The use of prime starch significantly improved the physical properties of the final loose-fill foam, in comparison to foam produced from regular dry corn starch. The S-g-PMA loose-fill foam had compressive strength and resiliency comparable to expanded polystyrene but higher bulk density. The S-g-PMA loose-fill foam also had better moisture and water resistance than other competitive starch-based materials. Studies indicated that the starch portion in S-g-PMA loose-fill foam biodegraded rapidly, whereas poly(methyl acrylate) remained relatively stable under natural environmental conditions.

Acrylic Resins↗