Research Background

Soybeans are the most economical source of protein for human foods and the animal industry. Soybean seeds contain 35 to 55% of protein on a dry weight basis and an important source of edible vegetable oil throughout the world. However, the protein fraction has nutritional deficiencies, such as a low level of sulfur bearing amino acids, and antinutritional components, such as the Kunitz trypsin inhibitor and the human allergen P34. Modification of these components could make soybean a more valuable protein source. Genetic approaches have been used to eliminate the Kunitz trypsin inhibitor, reduce the expression of P34, and introduce numerous other transgenes into soybeans. However, there is essentially no literature regarding collateral or unintended effects of these transgenic modifications. Unlike traditional breeding, recombinant DNA technology permits the transfer of genetic material from unrelated species, and this is precisely why a safety assessment is necessary. Safety assessment of transgenic crops provides assurances that toxic or allergenic compounds are not transferred along with the desired trait when new DNA is introduced into an organism. At present, safety assessments of transgenic crops using proteomics tools are limited. Therefore, my research program will focus on developing and evaluating various proteomics tools, which have the potential for risk assessment of transgenic soybean and other genetically modified Crops.

Primary Research Goals

  Study the natural variation of seed proteins in a wide range of soybean using proteomics.

  Apply proteomics tools to study the homogeneity of collateral effects associated with the Roundup Ready gene in a number of different genetic backgrounds.

  Apply proteomics tools to study the predictability of collateral effects resulting from the different introductions of the same transgene.

  Identify and characterize highly expressed genes in Roundup Ready soybean seeds during seed development using DNA microarrays.

Process for the production of monoterpenes using bacterium containing recombinant DNA. 1997. US patent # 5 688 673.

Method for production of monoterpene derivatives of limonene. 1998. US patent # 5 763 237.

Method for degradation of pinenes by bacillus pallidus. 1996. US patent # 6 156 533.

Savithiry, S., D. Gage, W. Fu, and P. Oriel. 1998. Degradation of pinene by Bacillus palladus BR425. Biodegradation. 9, 337-341.

Savithiry, S., T. K. Cheong, and P. Oriel. 1997. Production of a-terpineol from E. coli cells expressing thermostable limonene hydratase. Appl. Biochem. Biotechnol. 61, 213-220.

Oriel, P. and Savithiry, S. 1995. Harnessing the power of microbes. Focus. 21-22.

Savithiry, S. and K. Kumar. 1994. mRNA levels of Ca²⁺ independent forms of protein kinase C in post-ischemic gerbil brain by Northern blot analysis. Molecular and Chemical Neuropathology. 21, 1-11.

Ries, S., S. Savithiry, V. Wert and I. Widders. 1994.Cations signals rapidly elicited in several different plant species by pinching the leaves. J.Expt.Bot. 451, 3679-371

Ries, S., S. Savithiry, V. Wert and I. Widders. 1993.Rapid induction of ion pulses in tomato, maize and cucumber plants following a foliar application L (+) adenosine. Plant Physiol. 101, 49-55.

Savithiry, S., B. Madhukar, and K. Kumar. 1993. Northern analysis and in-situ hybridization for expression of protein kinase C isozymes in gerbil brain using oligodeoxyribonucleotide probes. Neuroscience Communication. 13, 125-132.

Kumar, K. and S. Savithiry. 1993. Comparison of a-tubulin mRNA and heat shock protein mRNA in gerbil brain following 10 min of ischemia. Molecular Brain research. 120: 130-136.

Kumar, K., S. Savithiry, and B. Madhukar. 1992. Expression of protein kinase C in post-ischemic brain, an in situ hybridization study. Metabolic Brain Disease 7, 93-100.

Savithiry, S., and S. Ries. 1992. Mode of action of 9-B-L(+) adenosine on malate dehydrogenase within second of treatment to the foliage in rice. Plant Physiol. (Life Science Advance) 11, 217-223.

Savithiry, S., V. Wert., S. Ries. 1991. Influence of 9-B-L(+) adenosine on malate dehydrogenase (MDH) activity in rice. Physiol. Plant. 84, 460-466.

Savithiry, S. and S. Gnanamanickam, 1987. Bacterization of peanut with Pseudomonas fluorescens for biological control of Rhyzoctonia solani and for enhanced yield. Plant and Soil. 102, 11-15.