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Biomedical subjects

R L Shogren

Publications and source records attributed to R L Shogren.

6 recordsLinked to original sources

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↗

Light-scattering studies of fractionated ovine submaxillary mucins.

Static and dynamic light-scattering studies of solutions of ovine submaxillary mucin (OSM) glycoproteins, fractionated by exclusion chromatography on Sephacryl S-1000, are reported. These experiments yielded information regarding the structure and conformation of the glycoprotein chain, in the form of weight-average molecular weights, Mw, z-average radius of gyration, Rg,z, and z-average of the inverse hydrodynamic radius, (Rh-1)z. The values of (Rh-1)z are found to correlate very well with the S-1000 elution volume characteristics for four OSM fractions of different molecular weights. The structural parameters for these OSM fractions are, within experimental error, similar to those deduced for porcine submaxillary mucins (PSM) in earlier studies. The results suggest that, like PSM, the glycoprotein structure of OSM consists of linear chains constructed by covalently linking two or more elementary subunits together via disulfide bonds. In addition, the rigidity of the protein core of OSM is substantially greater than that observed for non-glycosylated-polypeptide random coils. Because (Rh-1)z, and hence, elution volume depends only on the molecular weight of the mucin protein core, the Mw calibration obtained for OSM should be applicable to the chromatography of other mucin glycoproteins.

Animals↗

The thermal depolymerization of porcine submaxillary mucin.

The time dependence of the molecular weight, radius of gyration, and hydrodynamic size distribution for porcine submaxillary mucin (PSM) in solution have been studied using static and dynamic light scattering. The weight average molecular weight (Mw) of PSM in 6 M guanidine HCl, pH 7, is initially 3 X 10(6) and decreases with time in three phases: rapidly from 3-2 X 10(6), less rapidly from 2-0.9 X 10(6), and slowly below 0.9 X 10(6). The rates of decrease are much greater at pH 2. The energy of activation associated with each phase is 20 kcal/mol, which is similar to that reported for peptide bond cleavage at an aspartic acid residue. Addition of mercaptoethanol to PSM in 6 M guanidine HCl leads to a rapid decrease in Mw to 0.9 X 10(6), followed by a very slow further decrease. These results suggest that native PSM consists of subunits (Mw = 0.9 X 10(6] that are linked by disulfide bonds to form dimers (Mw = 2 X 10(6] and then higher aggregates. This cross-linking appears to occur at unglycosylated regions of the protein core, which are believed to be richer in aspartic acid than the rest of the molecule.

Animals↗

Light-scattering studies of chick limb bud proteoglycan aggregate.

Static and dynamic light-scattering methods have been used to investigate the structure of chick limb bud chondrocyte proteoglycan aggregate in 0.4 M guanidinium chloride. Zimm plot data for proteoglycan aggregate yield a molecular weight of 45 +/- 8 X 10(6) which compares well with a value of approximately 43 X 10(6) obtained by combination of the diffusion and sedimentation data via the Svedberg equation. The molecular weight of the proteoglycan subunit was determined previously to be 1.4 +/- 0.3 X 10(6), which indicates that the average proteoglycan aggregate molecule contains 32 associated subunits. This is in good agreement with electron microscopy which suggests an average of approximately 25.5 subunits/aggregate; it can be concluded that the aggregates visualized by electron microscopy are also present in solution. These data are also compatible with the ratio of the hydrodynamic volumes of proteoglycan aggregate and subunit. The formation of the aggregate structure has little effect on the solvent-binding capacity of the components: both proteoglycan aggregate and subunit have expanded coil conformations that include approximately 99% solvent.

Animals↗

Solvent-free process to esterify polysaccharides.

A novel process for the preparation of acetates of polysaccharides is described herein. The process involves the acetylation of polysaccharides with acetic anhydride in the presence of iodine as a catalyst. No solvent is required to bring about the acetylation. The method is simple, rapid, and characterized by a high conversion ratio. Conversion of cellulose and starch into their corresponding acetate derivatives has been demonstrated.

Acetic Acid↗