CEPCEB Members

Jerome S. Schultz Distinguished Professor Department of Chemical/Environmental Engineering University of California Riverside, CA 92521 Phone: (951) 827-2111 Fax: (951) 827-5696 Areas of Expertise Biosensors Artificial Membranes Biomaterials Pharmacokinetics
Background Selected Publications (Bibliography page)

Background

Professor Schultz received his B.S. and M.S. degrees in chemical engineering from Columbia University. He was awarded the Ph.D. degree in biochemistry by the University of Wisconsin and was subsequently employed for six years by Lederle Laboratories. While at Lederle, he was a group leader in the Research Division developing new antibiotics, enzymes, and steroids. He then joined the University of Michigan's Department of Chemical Engineering where, in addition to his professorial responsibilities, he led research in applied microbiology, biomaterials, and membrane separations. Dr. Schultz served as chairman of the Department from 1977 until 1985, where he championed the concept of molecular engineering. He then took a two year leave-of-absence from Michigan to accept an assignment as Deputy Director of the Program for Engineering Research Centers at the National Science Foundation.

In 1987 Dr. Schultz joined the University of Pittsburgh as Director of the newly established Center for Biotechnology and Bioengineering. This interdisciplinary research Center has programs in bioprocessing, biosensors, bioartificial organs and gene therapy. In addition to promoting a vigorous research environment, Dr. Schultz has led the formation of an academic program in Bioengineering that has culminated in the formation of a new Department of Bioengineering in the School of Engineering that offers B.S., M.S. and Ph.D. degrees in Bioengineering. The units administrated by Dr. Schultz were recognized by major national awards from the Whitaker Foundation, Kresge Foundation, Keck Foundation, and a NIH Biotechnology Training Grant and are ranked in the top 20 bioengineering departments by US News and World Report . In 2004 Dr. Schultz accepted a new position at the University of California, Riverside as Distinguished Professor and Director of the Center for Bioengineering Research.

Professor Schultz enjoys a distinguished international reputation for his research initiatives in the areas of biosensors and synthetic membranes. His study of biosensors involves the utilization of biomolecules that have recognition functions - e.g., antibodies, membrane proteins, bioreceptors - to provide the selectivity capability of sensor probe devices. Professor Schultz has shown that these biological transducer molecules can be coupled with readout devices, such as fiber optics, to result in biosensors that provide unique characteristics to measure biomolecules i.e., sugars, drugs, toxic drugs in situ.

Professor Schultz has made several seminal contributions to the use of membranes in separation and purification. He proved the mechanism of selective separations in microporous membranes to be a function of hydrodynamic drag and partitioning of molecules. He also demonstrated and developed theories for carrier-mediated diffusion of gases through liquid membranes.

Dr. Schultz' achievements have been recognized by several organizations. He has held a Career Development Award from NIH, received the Bioengineering Award from the American Institute of Chemical Engineers, was a founding Fellow and President of the American Institute for Medical and Biological Engineering, was named as a Fellow of the American Association for the Advancement of Science, and is a member of the National Academy of Engineering. Dr. Schultz has served as chairman of the Biotechnology Division of the American Chemical Society and the Food, Pharmaceutical and Bioengineering Division of the American Institute of Chemical Engineers. He is the editor of Biotechnology Progress, published jointly by these two societies.

While at the University of Pittsburgh he was named to the rank of Distinguished Professor, one of about 20 faculty at the University that have this recognition. Also he was recently recognized by the Biochemical Technology Division of the American Chemical Society by being given the Marvin J. Johnson Award for year 2000. This award is designated for outstanding and innovative research contributions in the area of microbial and biochemical technology.

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Fig 1. Design of a GIP (glucose indicator protein) for sensing glucose based on FRET. (a) Diagram of the GIP structure showing how FRET between two GFPs can measure glucose concentration. The GBP adopts an "open" form in the presence of the glucose, which triggers a conformation change, causing two GFPs apart from the center of GBP leading to the change in FRET. The b represents one molecule of the glucose bound onto the binding cleft of the GBP. (b) Domain structure of the GIP. The boundary region of amino acid sequence between the fused proteins was determined empirically to ensure the stable and efficient expression of GIP in E. coli. GFPuv: green fluorescent protein with several mutations to enhance the excitation by UV light. YFP: yellow fluorescent protein. GBP: glucose-binding protein. FRET: fluorescence resonance energy transfer.

Fig. 2. Schematics illustrating the principles of the fluorescence affinity hollow fiber sensor. In the absence of glucose, fluorochromelabeled Concanavalin A is bound to fixed glucose residues inside porous beads (left hand). The beads are colored with dyes that prevent the excitation light from penetrating into them and inducing Con A to fluoresce, thus keeping the fluorescence emission at 520 nm. After diffusion of glucose through the hollow fiber membrane (molecular weight cutoff, 10 kDa), Con A is displaced from the beads and diffuses out of them, and hereby fluorochrome-labeled Con A becomes exposed to excitation light resulting in a strong increase in fluorescence (right hand).

Fig 3. Diagram of retroviral vectors for integration of CD34EGFP into the genome of CD34+ stem cells and progenitor cells. (a) RV_CD34EGFP encoding the CD34EGFP cell marker, in which EGFP was placed downstream of the CD34 promoter. The CD34 promoter drove cell-specific expression of EGFP in CD34+ stem cells and progenitor cells. (b) RV_CMVEGFP encoding a reporter, CMVEGFP, in which EGFP was constitutively expressed from the CMV promoter. Symbols: Neor, neomycin resistance gene; LTR, long terminal repeat sequence derived from a murine stem cell virus (PMCV); ã+, the extended retroviral packaging signal sequence; KCS, a Kozak consensus sequence.

 

Selected Publications (Bibliography page)

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