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Full-Text Articles in Food Science

Plasmin In Milk: Activity Measurement, Effect Of Environmental Factors, And Correlation With Milk Coagulation, Eric D. Bastian May 1989

Plasmin In Milk: Activity Measurement, Effect Of Environmental Factors, And Correlation With Milk Coagulation, Eric D. Bastian

All Graduate Theses and Dissertations, Spring 1920 to Summer 2023

Bovine plasmin activity was measured on H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide by following absorbance changes at 405 nm. Steady-state kinetic parameters Vmax, Km, KI, and KI' were estimated. Bovine plasmin is competitively inhibited by casein and has a Kcat of .0158 ΔA405/min/nM, Km of .107 mM substrate, and KI of .86 mg/ml casein. Bovine plasmin can be measured directly in bovine milk without interference from casein.

A total of 380 milk samples from nineteen Holstein (one herd) and nineteen Jersey (one herd) cows was collected monthly during one lactation period. Samples …


Influence Of Processing Parameters On Nutrient Recovery During Ultrafiltration Of Milk And Meltability Of Pasteurized Process Cheese Food Made From The Retentate, Susan Kay Fortier Collinge May 1989

Influence Of Processing Parameters On Nutrient Recovery During Ultrafiltration Of Milk And Meltability Of Pasteurized Process Cheese Food Made From The Retentate, Susan Kay Fortier Collinge

All Graduate Theses and Dissertations, Spring 1920 to Summer 2023

Three batches of milk were ultrafiltered to 60, 65, or 70% volume reduction before diafiltration. Starting diafiltration at 70% volume reduction took less time and water without affecting nutrient recovery.

Whole milk was heated to 60, 72, and 82°C for 16 s. Milk representing each heat treatment was divided into three batches, one unacidified (pH 6.6), the others acidified to pH 6.2 and 5.8. The milk was ultrafiltered, diafiltered, and concentrated to 5x (80% volume reduction). Retentate was inoculated with .5% lactic culture and incubated at 28°C to pH 5.1. Each lot of fermented retentate was evaporated under 76 kPa …


Effect Of Heating To 200 C On Casein Micelles In Milk: A Metal Shadowing And Negative Staining Electron Microscope Study, V. R. Harwalkar, Paula Allan-Wojtas, Miloslav Kalab Jan 1989

Effect Of Heating To 200 C On Casein Micelles In Milk: A Metal Shadowing And Negative Staining Electron Microscope Study, V. R. Harwalkar, Paula Allan-Wojtas, Miloslav Kalab

Food Structure

Milk was heated to 200 C for 3 min in sealed inverted-Y-shaped glass vials and reacted with a glutaraldehyde solution at that temperature. Electron microscopy of the metal-shadowed and negatively stained samples revealed that casein micelles in the milk did not disintegrate extensively at the high-temperature used but, rather, became enlarged. Some of them were found to be either clustered or distorted.


Composition And Some Properties Of Spray-Dried Retentates Obtained By The Ultrafiltration Of Milk, Miloslav Kalab, Marijana Caric, Mansour Zaher, V. R. Harwalkar Jan 1989

Composition And Some Properties Of Spray-Dried Retentates Obtained By The Ultrafiltration Of Milk, Miloslav Kalab, Marijana Caric, Mansour Zaher, V. R. Harwalkar

Food Structure

Retentates containing 20, 27, and 34% total solids, obtained on commercial scale by the ultrafiltration of milk were spray-dried on laboratory scale using centrifugal atomization and single stage drying with the inlet air temperature of 220 C and the outlet air temperature of 90 C.

The protein content in the powders was 31% to 35% compared to 24.8% protein in the control whole-milk powder. Lactose contents were markedly lower in the retentate powders (-10.6%) than in the milk powder (40.4%). Storage of the powders at 37 C resulted in a marked increase in the 5-hydroxmethylfural contents with doubling of this …