About

Eugene Alford, MD, FACS, is an Associate Professor in Clinical Otolaryngology at Houston Methodist. He is affiliated with Texas A&M University School of Engineering Medicine and can be contacted via drgene@tamu.edu. His professional role involves clinical practice and academic responsibilities within the field of otolaryngology, contributing to the medical education and healthcare services provided through Houston Methodist and Texas A&M University.

Research topics

• Food science
• Chemistry
• Chromatography
• Biochemistry
• Biology

Selected publications

• Heat Inactivation of the Alkaline Phosphatase in Human Milk and Colostrum

  Journal of Food Protection · 1993-03-01 · 4 citations

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• Rheological Properties of Heat‐induced Gels from Egg Albumen Subjected to Freeze‐thaw

  Journal of Food Science · 1991-05-01 · 3 citations

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  ABSTRACT A back‐extrusion device was used to measure gel strength, elasticity, and viscosity index of heat‐induced gels of albumen maintained at 80°C from 5 to 30 min. These rheological properties were the same in albumen refrigerated 24 hr at 3°C as those observed in gels from fresh albumen suspensions. Short term frozen storage (−10°C for 24 hr) significantly reduced each gel parameter compared with fresh (control) albumen gels. Incorporation of sucrose into fresh albumen protected rheological properties of the heat‐induced gels from deleterious effects of freezing the albumen suspensions. Addition of 5 or 10% NaCl to albumen reduced or eliminated the ability of albumen to form heat‐induced gels.

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• Heat Stability of the Bile Salt-Stimulated Lipase in Human Milk Fortified with Sodium Taurocholate

  Journal of Food Protection · 1988-04-01 · 1 citations

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• Effect of Succinylation on the Proteolysis of Food Proteins

  Journal of Food Science · 1984-03-01 · 4 citations

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  ABSTRACT Casein, bovine serum albumin and soy globulin were succinylated and used as substrates, in both forms, for initial velocity studies of proteolysis by α‐chymotrypsin and pepsin. Succinylation resulted in modification of at least 91% of the free amine groups of the proteins. Proteolysis was determined by fluorometrically monitoring the appearance of amine groups. Kinetic constants were estimated by the direct equation plot using FORTRAN programs. Succinylation enhanced the initial proteolysis of all substrates by either enzyme as evidenced by an increased maximum velocity and decreased Michaelis constant for the modified substrates. Modification of casein caused the most pronounced differences in rates of proteolysis, resulting in the largest change in kinetic constants for pepsin and the smallest change for α‐chymotrypsin.

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• Correlation of the Rheological Behavior of Egg Albumen to Temperature, pH, and NaCl Concentration

  Journal of Food Science · 1984-01-01 · 44 citations

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  Rheological parameters of viscosity, gel strength, and elasticity were determined on heat-set egg albumen gels over various treatment combinations ranging from 65-90°C, pH 6.4-9.6, and NaCl concentrations of 0.0-0.1M added NaCl. Maximum viscosity was measured at a treatment combination of 77.5°C, pH 8.00, and 0.1M NaCl. Elasticity and gel strength were highest in gels with a treatment combination of 85.2°C, pH 9.0, and 0.08M NaCl. Temperature had the greatest effect on all three rheological parameters. Gels heated above 80°C were of unusual character, exhibiting syneresis and shrinkage.

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• Rapid high-temperature treatment of human milk

  The Journal of Pediatrics · 1984-03-01 · 116 citations

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• Lipolytic Activity During Storage of Human Milk: Accumulation of Free Fatty Acids

  Journal of Food Protection · 1984-09-01 · 7 citations

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• Heat Inactivation of Bile Salt-Stimulated Lipase Activity in Human Milk and Colostrum

  Journal of Food Protection · 1983-06-01 · 2 citations

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• Lipolytic Activity During Storage of Human Milk: Stability of the Bile Salt-Stimulated Lipase

  Journal of Food Protection · 1983-11-01 · 4 citations

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• Changes in Heat‐Induced Rheological Properties During Cold Storage of Egg Albumen

  Journal of Food Science · 1982-11-01 · 16 citations

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  ABSTRACT Two groups of eggs were stored at 15°C for 0, 5 and 10 days. One group was stored, with the shell removed, in sterile Whirl‐Pak bags. A second group was stored as intact whole eggs. Viscosity index, apparent elasticity, and initial penetration force were determined for heat‐induced (80°C, 80 min) gels of the thick, thin and mixed albumens from each group. The rheological parameters increased with storage time, with the greater increase exhibited by the gels of the albumens that were stored as shell eggs. Solution pH was a major factor controlling these rheological properties of heated egg albumen.

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Frequent coauthors

• C.W. Dill

  University of Wisconsin–Madison

  33 shared

• Ronald Richter

  Rutgers, The State University of New Jersey

  22 shared

• Cutberto Garza

  21 shared

• R. L. Edwards

  Harper Adams University

  10 shared

• C. Vanderzant

  8 shared

• C.T. Chen

  8 shared

• M.O. Hanna

  Texas A&M University

  8 shared

• N. Shewakramani

  Texas A&M University

  8 shared