I would first like to express my profound thanks to the Association, and to Dr. Kasarda and the Osborne Committee, for choosing me to receive this incredible honor. I am truly humbled and can't help but think that this must be some sort of mistake - like the elephant flautist at the piano asking himself "What am I doing here?!"

But here I am. Most of my predecessors have offered profound and interesting lectures and observations. With me, that’s probably unlikely. But perhaps I can at least offer a few perspectives about research in cereal chemistry gained during 33 years of research on the proteins of wheat and corn.

<SLIDE 2> The title of my lecture originates from a 1998 article in Trends in Plant Science (Wessler et al 1998), entitled "Standing on the shoulders of giants." It refers to the sense of history at a recent maize meeting, and to the debt that today’s scientists owe to those of the past. This is equally true for all of us, since our accomplishments have built on those of many others, including those with whom we have worked closely. <SLIDE 3> Here, for example, is a list - with apologies to any who have been omitted - of many of those I worked with over the years. Included are excellent supervisors, such as Osborne medalist Dr. Joseph Wall, who provided a model and a research environment that encouraged success. Also present are many colleagues from within our organization; great technical support staff; scientists from around the world who came to our laboratory to work; and colleagues from many other locations.

In this lecture I will try to do three things. First, I’d like to offer a few observations on the life and work of Thomas Burr Osborne, undoubtedly the greatest cereal chemist ever. His life and accomplishments should serve as a model for all of us - and it is highly appropriate that we should remember and appreciate what he did. Secondly, I’ll mention a few research areas I was involved in at Peoria, usually because of being in the right place at the right time, with the right people. And finally, I’ll offer a few personal observations about the importance of research.

<SLIDE 4> I’m not a farmer (a man outstanding in his field!), like my Dad, who first got me involved in agriculture. But perhaps I can tell you a bit about my involvement in cereal chemistry, since I believe that one responsibility of those long active in a field must be to provide a link to the past, and a sense of continuity. This may be more important than ever today. First, new cereal chemists are met with a voluminous body of knowledge. More has happened in our lifetimes than in all preceding years, and it’s nearly impossible to really know and understand all that’s been done, and to keep up with new advances. This sometimes leads to an unfortunate tendency to ignore early contributions. But we can learn a great deal from past studies - they remind us of how we got here, and can show us how to proceed.

<SLIDE 5> The importance of cereal grains, and especially their proteins, has long been recognized. There is much evidence that ancient farmers were very interested in wheat. <SLIDE 6> A little later the first cereal chemist (obviously a baker) recognized, while pondering the adhesive properties of a dough, that many of wheat's unique properties were due to its proteins.

Eventually chemists learned to write, and began to publish their observations. <SLIDE 7> One of the earliest papers about wheat proteins was presented in 1728 by an Italian scientist, Beccari, and published in 1745 (see Bailey and Beccari 1941). This paper notes the unique importance of wheat in foods, and describes the separation of gluten and starch from flour. It shows gluten and starch to have very different chemical and physical properties, and notes the cohesive nature of dough. <SLIDE 8> And it clearly notes the importance of fundamental research on grain and flour - "a study worthy of a scientist".

<SLIDE 9> Relatively little more seems to have been done during the next 150 years, until the appearance of the most remarkable chemist, Thomas Burr Osborne. It is most appropriate, in this lecture commemorating the award named after him, to briefly review his life and incredible accomplishments (Vickery 1931, 1956), which may well serve as a model for others to follow.

Thomas Burr Osborne was born in New Haven, CT, in 1859, and was educated in New Haven. He was an inventive genius, with a natural aptitude for original thinking and experimentation in many aspects of science. He wanted to prove things for their own sake and to establish facts to his own satisfaction, not to blindly accept traditional knowledge.

Osborne attended Yale University. While there, he was interested in all aspects of natural history. One of his most interesting activities was extramural. He became aware of a problem in flour milling. The existing method for purifying middlings was unsatisfactory. Osborne reasoned that differences in electrical properties of particles in ground wheat might be a basis for separation. He therefore devised a machine in which flour passed under electrostatically charged rubber rolls; lighter bran particles flew up and adhered to these rolls. Patents were granted, and this purifier was used successfully for several years.

Osborne graduated from Yale in 1881, and continued graduate studies there, first in medicine, and then in chemistry, receiving his Ph.D. in 1885. In 1886 he joined the Connecticut Agricultural Experiment Station as an analytical chemist. He was hired by the distinguished chemist and station director, Dr. Samuel Johnson. Osborne's early studies were of gums and carbohydrates - but in 1887 Johnson suggested that Osborne investigate the proteins of plant seeds, a topic that had received little attention. Osborne pursued this topic for the next nearly 40 years.

At this time, few chemists were interested in studying vegetable proteins. Protein research seemed hopeless. Proteins were difficult to work with; there were no satisfactory methods of separation and purification; and days of time-consuming labor often yielded few definite results. Fundamental protein research was also perceived as of little use to farmers.

It had been generally believed that there were only a few types of proteins. Osborne's work clearly showed this to be untrue. In 1889 he began to isolate and characterize seed proteins - first, from oats, and eventually from 32 different plants. He took great pains to isolate pure proteins as they occur in the seed. At this time, the accepted criteria of protein purity were analyses for carbon, hydrogen, nitrogen, and sulfur. Osborne recognized that this was hopelessly inadequate. He developed and refined methods of protein composition analysis - including analysis of the amino acids arising upon hydrolysis - and he added criteria of solubility and functionality to describe and differentiate proteins. This was a real turning-point in protein chemistry.

Every seed was found to contain two or more different proteins. Sometimes the same proteins occurred in different seeds - but Osborne's careful analyses - combined with collaborative biological studies - often showed different proteins in different species. Clearly, differences among proteins were greater than their similarities.

<SLIDE 10> It is amazing to realize the incredible amount of effort that went into these studies. For example, as described by Osborne's colleague Vickery (1956), 1100 gm of purified gliadin were hydrolyzed to determine glutamic acid and mono-amino acids, and much more was needed for other determinations. Such large quantities were necessary since each pure amino acid had to isolated and weighed. As Vickery noted, that Osborne and his few assistants accomplished so much in this new field is a matter for wonder.

Osborne's work clearly showed that most proteins could be characterized by amino acid analysis, coupled with a study of their physical properties. Variable recoveries of amino acids upon hydrolysis also led to the concept of correction factors. Furthermore, these studies laid the foundation for later nutrition investigations.

<SLIDE 11> In the decade of the 1900's, Osborne concentrated on some of the more complicated problems of protein chemistry, including the alcohol-soluble and alcohol-insoluble proteins of wheat. His results on wheat proteins came together in the famous 1907 monograph entitled "The Proteins of the Wheat Kernel" (Osborne 1907), which should be a fundamental source book for all cereal chemists. It reviews the history of the subject, and presents all results up to that time. It defines and characterizes gliadin and glutenin with stunning insight and accuracy. For example, their amino acid compositions are remarkably accurate, and clearly indicate their unique aspects.

<SLIDE 12> Osborne's publications are also remarkable for their completeness. As noted by Vickery (1931), "operations are so minutely and carefully outlined that it is possible to repeat Osborne's work to its last detail and secure preparations that correspond exactly to those he described."

Time will permit only the briefest mention of Osborne's later research. His studies of proteins led to extensive collaboration with Lafayette Mendel from 1909 through 1928. Together they published more than 100 papers on various aspects of nutrition. The existence of vitamins was clearly demonstrated, as was the essential nutritional role of proteins. They developed carefully controlled rat feeding studies which showed that proteins differ in nutritional value because of differences in contents of essential amino acids. Throughout his career, Osborne published more than 4000 pages in more than 250 papers and books in the fields of vegetable proteins, animal proteins, and nutrition. His publications are very well written - directly, without literary adornment - and facts are clearly presented.

<SLIDE 13> It's also revealing to see Osborne through the eyes of his colleagues. Vickery (1956) said that in the laboratory, Osborne was the leader who went about his work with singleness of purpose. He disciplined himself and required discipline of others . . . He could analyze problems acutely, uncover fallacies, and plan experiments that would lead to the correct result. No amount of labor was spared to arrive at the truth. He lived for his work and allowed nothing to interfere with it. Another colleague, C. B. Morrison (1928), noted that "Thomas Burr Osborne will always be remembered by those engaged in the research and technical activities of the cereal industries, as a pioneer whose innate genius and perseverance in an unpromising and difficult field have made possible our fundamental knowledge of the proteins of the cereal grains and their nutritive properties." Vickery (1931) noted that Osborne was perhaps fortunate in not becoming an administrator: "He was more fortunate than most men in that advancing years, distinctions and scientific recognition did not bring with them administrative responsibilities which deprived him of the opportunity to share in the daily work of the laboratory. His time was always freely available for discussion . . . Ever kindly and courteous . . .he has left a memory that will long be treasured by those who had the privilege of knowing him." And, as Vickery (1956) noted, "He was a great man and a great biochemist, and one has only to leaf through any volume of this journal to find the traces of his footsteps on many pages."

It's also revealing to consider the research climate in which Osborne operated. He received adequate financial support, even in the early years when results came slowly and their application was not clear. No interference or distraction was allowed to hinder the work. This is a striking example of the value in science of a policy of noninterference by those controlling research funds. Except for routine annual reports, Osborne was never asked for statements of progress nor for outlines of projects. The relationship was always one of mutual confidence and esteem (Vickery 1931).

Osborne received many honors, including an honorary degree from Yale in 1910 and election to the National Academy - but the honor he appreciated most was the first award of the Thomas Burr Osborne medal by the AACC in 1928, in recognition of his contributions to cereal chemistry (Vickery 1956). In his remarks upon accepting the medal, Osborne made several memorable observations (Osborne 1928). He clearly noted the value of research in cereal chemistry, even when there are no known immediate practical applications: ". . . I therefore hope that what I have said of my experience will inspire other workers to take up new lines of work with the confident expectation that whatever may be learned and definitely established in regard to the chemistry of cereals cannot fail, sooner or later, to be of use and to be worth all that it costs in time and money." He made a pointed comment about one way in which industry should support research: "Chemists have done much for the industries and it is now time that the industries should appreciate this and be generous in paying their debt." He emphasized that much then remained - as it does today - to be done: "In the field of cereal chemistry there are still many problems awaiting investigation. With modern facilities . . . and improved apparatus and available funds, it ought to be possible to learn much that will be useful and of broad application. We do not yet know, by any means, as much about the proteins of the cereals as we ought to know. This is particularly true of wheat gluten." Finally, Osborne noted the importance of the AACC in promoting research: "Your Association of Cereal Chemists is in a position to promote such investigations successfully. . . . It is no longer possible in such a field as yours for one man to work alone effectively. . . . To solve these problems requires the cooperation of many among you . . .".

Thomas Burr Osborne - truly a giant in cereal chemistry to whom we all owe a huge debt of gratitude, and from whose accomplishments there is much for us to learn.

<SLIDE 14> I'd now like to move ahead several decades - to the mid 1960s, when many scientists again began to examine and try to better understand cereal grains. In some ways, little more was then known about plant proteins beyond what Osborne had found. <SLIDE 15> It was a little like the three blind men feeling the elephant - one said it was a snake, and one a tree, and one a wall. Similarly, scientists debated the nature and importance of gliadin, glutenin, and other factors, trying to decide how each contributed to gluten and to its functional properties.

But there had been some pioneering advances in isolating and characterizing seed proteins. For example, scientists at many laboratories had developed better ways to extract proteins, extending Osborne's methods based on differences in solubility. More had been learned about the amino acid compositions of proteins, and about the importance of disulfide bonds. New analytical methods were also emerging. <SLIDE 16> For example, a technique known as moving boundary electrophoresis separated proteins by charge, showing further complexity of wheat proteins (Jones et al 1959). <SLIDE 17> And when electrophoresis was done in a starch gel, results were even better, and more heterogeneity was found (Woychik et al 1961, 1964). Studies using the ultracentrifuge also began to reveal sizes and relationships of proteins, and new chromatography techniques were developed that could separate proteins based on size or ionic nature.

This, then, was approximately, the status of cereal protein knowledge when I came to Peoria in 1966. My background was in enzymology - and I soon learned that much about enzymes didn't apply to cereal storage proteins. Enzymes were soluble, and could be separated by many methods. But grain proteins had unusual compositions and solubilities - many are soluble only in acids, organic solvents, or detergents. They are very heterogeneous, and often are large polymers. Many methods of protein chemistry simply didn't work. A few weeks in the library revealed how much we didn't know. For example, how could seed proteins best be isolated? Many fractions previously thought pure were now being shown to be mixtures. We didn't know if glutelins - such as wheat glutenin - were made up of prolamin subunits, such as gliadin. Finally, most analytical methods that were then available were pretty awful. <SLIDE 18> Here, for example, two eager young scientists try to separate wheat proteins by chromatography on a typical small (ca. 8 ft!) column. Single experiments like this took days or weeks; they were laborious, irreproducible, low resolution, and generally non-quantitative.

But the importance of cereal protein research was recognized. Cereals are the world's most important food and feed - and their proteins are especially important for nutrition. Protein compositions can serve as fingerprints to identify grains and predict quality. Knowledge of proteins can help breed better varieties. And, perhaps most importantly, cereal proteins have unique functional properties, such as the viscoelasticity of gluten that permits bread to be baked. <SLIDE 19>

<SLIDE 20> Thus, in 1966, I was privileged to join Joseph Wall, along with John Rothfus, Floyd Huebner, and other great colleagues, in research on cereal proteins. <SLIDE 21> We were challenged to clarify the mystical relationship between the structure and properties of wheat gluten. These studies continued at our laboratory for more than three decades. At the same time, many excellent researchers at other laboratories in the USDA and throughout the world made many important advances in this field. Excellent cooperation among them greatly assisted these efforts. The result of such studies has seldom been a product or a process, but rather a body of fundamental knowledge, as documented in many publications, that provides the basis for future progress. These studies have at least partially solved this most challenging and difficult problem of relating gluten's structure and properties - for wheat gluten is indeed nature's largest and most complex molecule (Wrigley 1996).

Let me briefly review, then, a few of the studies I've been involved in, and try to show how they, along with advances by many other investigators, have helped us better understand the proteins of cereal grains. <SLIDE 22> In some of my earliest research (Bietz and Rothfus 1970), we began to look at the structures of gliadin and glutenin. Proteins were digested with enzymes, and the resulting peptides analyzed by electrophoresis, chromatography, and amino acid analysis. These studies suggested that many gliadins were similar, but also showed unique differences among them, and between gliadin and glutenin.

In the early 1970s, several factors seemed to come together and add to our understanding of cereal proteins. <SLIDE 23> The key to this was a new method known as sodium dodecyl sulfate-polyacrylamide gel electrophoresis (or SDS electrophoresis). In this method, proteins bind to the detergent SDS, forming negatively-charged complexes. The speed of migration of these complexes in an electrical field then depends almost totally on protein size. Others had developed this method and applied it to different proteins - we found that it also worked well with cereal proteins (Bietz and Wall 1972). This was one of those rare "eureka moments" in science. SDS electrophoresis showed that gliadin and glutenin were very heterogeneous, and very different. It revealed the approximate molecular weights of proteins in each fraction. And it clearly showed, for the first time, glutenin's unique high MW subunits. <SLIDE 24> The composition of these high MW subunits differed among wheats. Payne, using improved methods, showed that this type of analysis can thus predict wheat's breadmaking potential (Payne et al 1981).

SDS electrophoresis led to other discoveries. <SLIDE 25> For example, we saw differences among glutenins prepared by different methods, showing that many glutenin preparations contained a gliadin impurity (Bietz and Wall 1975). This led to a precipitation procedure to purify glutenin. <SLIDE 26> We also found that glutenin's subunits - released after cleavage of disulfide bonds - were of two very different types (Bietz and Wall 1973). Some, soluble in ethanol, are similar to gliadin in size, but differ in number and location of cysteine residues, so they crosslink into glutenin polymers, rather than remain as monomers, like gliadin. In contrast, glutenin's high-MW subunits were insoluble in ethanol.

The contribution of these high-MW subunits to wheat's properties was increasingly recognized. Wheats with the right type and amount of these proteins, achieved through breeding, could have the best quality. We therefore became interested in how specific chromosomes affect the amount and type of glutenin. To study this, we were greatly helped by the late and great Dr. Ernie Sears. He grew and supplied us with large quantities of wheat aneuploid lines, having different chromosome compositions. By isolating their proteins, we were starting to learn a little about these lines - but then serendipity struck in the person of the famous Australian wheat geneticist, Dr. Ken Shepherd, who came to our laboratory to work for a few months. Ken, along with Dr. Colin Wrigley, had used other types of electrophoresis to characterize proteins of wheat aneuploids - and he wanted to extend these studies using SDS electrophoresis. For this, Dr. Sears supplied us with small amounts of all aneuploids of the variety Chinese Spring. During the next weeks, we developed a procedure to isolate glutenin from single kernels, and analyzed hundreds of samples by SDS electrophoresis (Bietz et al 1975). <SLIDE 27> In aneuploids involving wheat's group 1 chromosomes, we found major differences in high MW subunits. <SLIDE 28> This enabled us to locate the genes for these subunits on the long arms of group 1 chromosomes. In applications such as this, SDS electrophoresis has become very widely used in wheat research and for quality improvement.

<SLIDE 29> These studies made us increasingly curious about the actual structures of wheat proteins - that is, the order of their amino acids, which determines protein properties. We at first believed that the large number of wheat proteins, plus their large proline and glutamine contents, would interfere with sequence analysis. Nevertheless, we did obtain a protein sequencer, and began such studies. <SLIDE 30> To our surprise, we got reasonably good sequence information for whole gliadin, suggesting that many gliadins are similar (Bietz et al 1977). This was confirmed when we analyzed gliadins that Floyd Huebner had purified - their sequences were almost identical. <SLIDE 31> This helped us better understand wheat's evolution. An early ancestor mutated into several species. The gene for gliadin also became duplicated, and then changed slightly through mutations, giving rise to many slightly different proteins. Finally, three diploid wheat species joined to form hexaploid bread wheat. Don Kasarda and his colleagues at the USDA's Western Lab began similar studies of protein sequences about this same time, and went much farther with them (Kasarda et al 1984) - ultimately determining complete sequences of gliadins and many other wheat proteins. This has contributed greatly to efforts today to improve wheat through molecular biology.

<SLIDE 32> We also examined sequences of proteins of several other cereals (Bietz 1982). In each cereal, one predominant prolamin sequence was present, suggesting evolution similar to that in wheat, and confirming how cereal grains evolved. <SLIDE 33> One corn protein was especially interesting. Its many proline and histidine residues were arranged in a remarkable hexapeptide sequence that repeated again and again (Esen et al 1982). Repeating sequences like this have since been found in many cereal proteins, and contribute to their unique properties.

One interesting aspect of a career in science is the role of serendipity - finding interesting new things almost by accident. But such accidents usually depend upon an optimal situation, such as a long-term research program, with considerable freedom and flexibility. Let me give you an example.

<SLIDE 34> In our studies of protein sequences, we used many methods to analyze cleaved amino acids. The best method for this purpose was high-performance liquid chromatography, and we obtained an instrument for this purpose - here shown in a typically messy lab with another essential component of research success - Leigh Ann Cobb, who provided excellent technical support. Until about 1980, HPLC was used primarily to analyze small molecules - but suddenly others began to develop columns and methods that could separate proteins. Since we had an HPLC instrument, we obtained a protein column. <SLIDE 35> It separated proteins on the basis of size, like gel filtration chromatography, a method widely used to analyze wheat proteins. Size-exclusion HPLC turned out to be an excellent method of analysis (Bietz 1984). Separations - even of very small samples - were as good as or better than those of earlier methods. Size-exclusion HPLC showed that protein molecular weight distributions differed among wheats, suggesting a relationship to breadmaking quality. The method had many advantages. Separations were reproducible, and amounts of proteins could be precisely determined. Accurate molecular weights were revealed, even with very small samples. And most importantly, the method is fast and automatic - one instrument could analyze 50 to 100 samples per day, as compared to about one per day with earlier methods. Other researchers, including Jean-Claude Autran from France, Fin MacRitchie and Ian Batey from Australia, and their colleagues, have since significantly improved this method (Dachkevitch and Autran 1989, Batey et al 1991), and it is now used extensively. It has the potential to be the quickest and most generally applicable method to estimate wheat or flour quality through protein analysis. Thus, size-exclusion HPLC has become an important method to help us analyze and understand cereal proteins.

New methods such as this usually don't make older methods extinct - but they are frequently used in their place. But another "eureka moment" was to come. We eventually got a second pump for our HPLC equipment, permitting us to vary solvent composition during a separation. Another type of HPLC column also became available, known as "reversed-phase." It separated proteins based on differences in hydrophobicity of its surface amino acids. <SLIDE 36> We obtained one of these columns, and tested it with a crude gliadin sample. Eureka! The separation was better than any we had previously achieved (Bietz 1983).

<SLIDE 37> For the next several years, much effort went into development and optimization of reversed-phase HPLC. I would be remiss if I did not acknowledge the major contributions of two who contributed so much to these efforts - my long-time friend and colleague Floyd Huebner (on the right), and Thierry Burnouf, a French postdoctoral fellow with us during the early years of these studies.

<SLIDE 38> Some of our first studies attempted to optimize separations of gliadin - and indeed, very good results can be achieved (Bietz et al 1984a). < SLIDE 39> Similarly, reversed-phase HPLC gave good separations of glutenin's subunits - and its important high molecular weight subunits were well separated from low-MW subunits (Burnouf and Bietz 1984a). Reversed-phase HPLC had many advantages: it was reproducible, fast, sensitive, and quantifiable. But perhaps most importantly, it complements most other methods.

<SLIDE 40> Time will not permit a full review of how reversed-phase HPLC has developed and been used - but let me mention a few of its applications. One of its first uses was varietal identification (Bietz et al 1984b). Gliadin could be rapidly extracted and analyzed, giving "fingerprints" that differentiate most varieties. This can be especially important in breeding and marketing wheat. <SLIDE 41> For example, some varieties were shown to have more than one biotype - closely related, but genetically distinct, lines (Lookhart et al 1986). This can be important in selecting parents for breeding. <SLIDE 42> Similarly, reversed-phase HPLC is useful in genetic studies - we found, for example, which peaks contain proteins coded by the high MW glutenin subunit genes (Burnouf and Bietz 1985).

<SLIDE 43> The quantitative capabilities of reversed-phase HPLC also showed that environment can markedly influence the relative amounts of wheat proteins (Huebner and Bietz 1988). This helps explain how both environment and genetics influence the quality of any wheat.

<SLIDE 44> Indeed, predicting quality or end-use potential can be a major application for HPLC. For example, pasta quality of durum wheats could be rapidly predicted by analyzing small portions of single kernels; desirable types could be selected and grown, or undesirable types eliminated early during breeding (Burnouf and Bietz 1984b). Similarly, breadmaking quality of wheat can be predicted by HPLC (Huebner and Bietz 1994). We are still challenged to identify all such relationships, and to optimize their use.

<SLIDE 45> During these studies, the methods we used continued to evolve. First, we found that high temperature often gives much better separations (Bietz and Cobb 1985) - probably by disrupting hydrogen bonds. <SLIDE 46> We also found that very rapid analyses are possible - here, for example, wheats were identified in only a few minutes per sample. Still better and faster analyses are possible with newer columns (Huebner and Bietz 1995). These methods have great potential for routine use, since one instrument and operator could automatically analyze hundreds of samples per day. In many other studies, it has been shown that reversed-phase HPLC can analyze proteins of all other cereal grains, including corn, oats, barley, rye, rice, triticale, and sorghum (Kruger and Bietz 1994).

<SLIDE 47> HPLC gave us another major problem, however - how to interpret the large amount of data it produces. In each chromatogram, the location and size of every peak may be important. To analyze such data, we had to develop or use two important tools - computers and statistics. <SLIDE 48> When these studies began, there were no personal computers, nor any software to store, plot, or analyze data. But we had something - or I should say someone - even better. Our mainframe computer operator, Roy Butterfield, developed an incredible suite of programs to store, plot, compare, and analyze data. <SLIDE 49> We also eventually recognized the need for statistical analyses. In this we were greatly assisted by Terry Nelsen. In several studies with Terry and others, we showed the usefulness of multivariate and other statistical techniques for data analysis (Simpson et al 1989). <SLIDE 50> Here is one example. Many mutant genes can affect the composition and properties of corn. HPLC showed that, in many of these lines, protein compositions also change significantly (Paulis et al 1992). And interestingly, when two of these genes are present, their combined effect is much greater than the sum of their individual effects. We don't yet understand how this works - but it does show how quantitative HPLC, combined with statistical data analysis, can show important and exciting ways in which the composition, quality, and end-use of cereals might be improved by controlling the genes that express proteins.

Much more could be said about developments and accomplishments of many of our colleagues using HPLC - but time won't permit that. Many of these advances are summarized in the volume High-Performance Liquid Chromatography of Cereal and Legume Proteins, published in 1984 by the AACC, co-edited with Jim Kruger, another pioneer in the field of cereal protein HPLC (Kruger and Bietz 1984).

<SLIDE 51> Before I close, I'd like to briefly mention one other exciting research area that is proving to be another "eureka". Electrophoresis - usually in gels - has long been one of the best ways to fractionate and characterize cereal proteins. But most electrophoresis methods are difficult to use, and have many problems. <SLIDE 52> In the early 1990s, a new type of instrument became available that had the potential to solve these problems. It was known as capillary electrophoresis. Through the support of Dr. Don Koeltzow, then with FGIS, we obtained and began to evaluate such an instrument - here shown with another invaluable colleague, Liz Schmalzried. In capillary electrophoresis, separations take place in very narrow glass capillaries. They are rapid, sensitive, quantifiable, and reproducible - as well as automatic. <SLIDE 53> We found that capillary electrophoresis also gives very good separations of wheat proteins (Bietz and Schmalzried 1995). It has many advantages over earlier electrophoresis methods, and may prove to be as valuable as HPLC. Methods of capillary electrophoresis have since been extensively developed and improved by George Lookhart, Scott Bean, and their colleagues at Manhattan (Bean et al 1998) - I'll leave a full discussion of this technique to them.

In this presentation, I've tried to present a story that illustrates the value of fundamental scientific research. I believe that several factors are necessary for success in such an endeavor. First and foremost are the people - their importance and abilities must be recognized and appreciated. And there must be enough people, having complementary interests and abilities, to provide a "critical mass" that facilitates collaboration and progress. Second is the research environment. Research does not always require highly sophisticated and expensive equipment - but neither should scientists have to scrape by with much less than what is needed and optimal. Thus, financial support should - as it was for Osborne - be adequate - and administrative staff should provide the many necessary support services, freeing scientists to do what they do best. Finally, while some goals and a timetable are desirable, we must recognize that fundamental research, by its very nature, explores the unknown. We may know, more or less, where we want to go, but we're not always sure how or when we'll get there, and there can be many detours and diversions along the way. Thus, successful fundamental research demands a long-term commitment. We should also realize - and remind others - that scientific research is an incredibly good investment - for example, one economic analysis (Araji 1989) showed that every dollar spent on wheat research in the western United States yielded nearly $143 in benefits! And we must remember that the knowledge provided by fundamental research is the starting point for all future applications.

This, then, concludes the summary of my adventure in cereal chemistry - which is largely a story of the many great people I've been privileged to work with, and to whom most of the credit for my few "eureka experiences" must be given. <SLIDE 54> I've now entered a somewhat different stage of life, often characterized by a computer, a cat, a couch, a remote control, and perhaps an appropriate beverage within easy reach.

In closing, it would be impossible to improve upon the words of Thomas Burr Osborne (1928) as he accepted the first medal awarded by the AACC in his name: " . . . I again thank you for the honor you have done me and congratulate you on the opportunities that lie before you for important contributions to science and industry." Thank you very much!

References