PubMed Health⌕ Search

Biomedical subjects

R A Lawrie

Publications and source records attributed to R A Lawrie.

14 recordsLinked to original sources

Risk characterisation and management of sewage sludge on agricultural land--implications for the environment and the food-chain.

The disposal of sewage wastes may cause severe environmental problems as was graphically demonstrated with pollution on Sydney's ocean beaches in recent years. Sewage sludges contain valuable plant nutrients and organic matter which can improve the fertility and structure of the soil. However, human parasites, pathogenic micro-organisms and chemicals capable of causing soil contamination, phytotoxicity and residues in animal products may also be present. Although sewage sludge is frequently spread on agricultural land overseas, it is not common in Australia and most states do not have specific regulations to minimise risk and promote good practice. A sludge-to-land program began in the Sydney region in 1990. It follows guidelines written by NSW Agriculture to encourage beneficial agricultural use of sludge by adoption of environmentally sustainable practices. This article describes the major risks to the food-chain and the environment, which may be associated with applying sewage sludge to agricultural land. It summarises how the risks are managed, and where further research data are required.

Animals↗

Protein quality and iron availability of intermediate moisture beef stored at 38 degrees C.

The longissimus dorsi of a bull and steer were cut into cubes 1.5 cm3 and processed to a water activity (aw) 0.85 by canning in a solution of 9.5 p. 100 sodium chloride, 0.5 p. 100 potassium sorbate and a pre-determined amount of glycerol and water for sixteen hours with continuous tumbling on an end over shaker. After partial drying the intermediate moisture (i.m.) meat pieces were stored at 38 degrees C for periods up to 24 weeks and then freeze-dried before milling and incorporation into test diets fed to rats. Protein quality of fresh cooked beef and i.m. meat stored at 38 degrees C was measured in terms of net protein utilisation (NPU). There was no significant difference in NPU between cooked beef and freshly processed i.m. beef. There were no changes in NPU of i.m. meat from bull up to 9 weeks of storage. After 3 weeks of storage of the meat from the steer however, the NPU fell to 53.0, a level characteristic of cereal protein. This fall in NPU was associated with a decrease in the levels of all essential amino acids (in the protein hydrolysate). Valine and threonine being first and second limiting amino acids. Further storage of i.m. beef after 3 weeks produced a slower rate of decrease in NPU, the value at 24 weeks being 32.1 (61 p. 100 fall). Available lysine decreased by only 15 p. 100 after twenty-four weeks, this measurement under-estimating the fall in protein quality. The decrease in solubility of the meat in SDS/beta-mercaptoethanol on storage was of similar magnitude to that of NPU. Iron availability of i.m. meat, measured by haemoglobin regeneration in rats, showed improved iron availability compared to freshly cooked beef, even though marked changes had occurred in the meat heamatin complexes.

Animals↗

Electrophoretic differentiaion f myofibrillar proteins in the pig.

1. Starch-gel electrophoretograms of myosin and tropomyosin preparations in 8m-urea, from longissimus dorsi and psoas muscles of the pig, were characterized by laser densitometry. 2. The typical pattern for freshly prepared myosin from both muscles was similar, there being five electrophoretically distinct components. 3. The number of electrophoretically distinct components in both muscles increased after freeze-drying, but the effect of freeze-drying was more marked in longissimus dorsi. 4. Extraction with 8m-urea containing 2% beta-mercaptoethanol decreased the number of major electrophoretically distinct components of the fresh myosin of both muscles to four. 5. Although there was also some simplification of the patterns after freeze-drying the greater susceptibility of the myosin from longissimus dorsi was still evident. 6. The typical pattern for freshly prepared tropomyosin in 8m-urea differed in the two muscles: in each case it was more complex than that of the corresponding myosins. 7. The pattern of tropomyosin from neither longissimus dorsi nor psoas was altered significantly after freeze-drying. 8. Electrophoretograms of pig longissimus dorsi tropomyosin in 8m-urea differed from those of longissimus dorsi tropomyosin from sheep, ox and rabbit. 9. Extraction of the tropomyosins in 8m-urea and 2% beta-mercaptoethanol simplified the electrophoretic pattern to two major components with samples from pig, sheep and ox, and to one major component with samples from rabbit. 10. It was concluded that classification of skeletal muscles as ;red' or ;white' is insufficient to account for the degree of functional specialization which the electrophoretograms suggest.

Animals↗