Phytate × Calcium/Zinc Molar Ratios: Are They Predictive of Zinc Bioavailability?

The utility of the phytate/zinc and phytate × calcium/zinc molar ratios for predicting zinc bioavailability from processed soybean foods was investigated. Weight gain and bone zinc accumulation in rats fed various soy protein products were plotted against the calculated molar ratios. The phytate × calcium/zinc ratio was a better predictor of zinc bioavailability in similarly processed products than was the phytate/ zinc ratio. However, in some cases the phytate × calcium/zinc ratio was not effective since some processing procedures apparently altered binding of phytic acid to minerals and other food components.     

Whey Protein Coating Effect on The Oxygen Uptake of Dry Roasted Peanuts

A procedure was developed to coat peanuts with aqueous whey protein isolate (WPI) solutions based on increasing coating-solution viscosity. Oxygen uptake of WPI-coated nuts and uncoated nuts were compared. WPI coatings delayed oxygen uptake of dry roasted peanuts at intermediate (53%) and low (21%) storage relative humidity. They had similar results at 29°C and 37°C. The effects of coating thickness and storage relative humidity indicate that the mechanism of protection of the coatings was through their oxygen barrier properties.     

Effect of Sodium Nitrite Concentration, Sodium Erythorbate and Storage Time on the Quality of Franks Manufactured from Mechanically Deboned Turkey

The effects of sodium nitrite (0-156 ppm), sodium erythorbate (0 or 550 ppm) and storage time (up to 10 wk at 4°C) were measured on the chemical and sensory properties of turkey franks formulated largely from mechanically deboned turkey (MDT), Residual nitrite in the finished product was proportional to that incorporated at time of formulation and was reduced by using small initial amounts in combination with the maximum allowable erythorbate (550 ppm). Acceptable cured color in turkey franks was achieved with the incorporation of 50 ppm of nitrite. Erythorbate effectively increased cured color development and stability, particularly with smaller amounts of nitrite. Rancidity development in turkey franks was not of major significance. Even so, the presence of erythorbate imposed further control of oxidative changes in lipids. Maximum cured flavor development occurred with 50–100 ppm nitrite.     

Emulsifying Properties of Food Proteins: Development of a Standardized Emulsification Method

A recirculating valve-homogenizer was used to compare the emulsifying properties of bovine serum albumin and milk proteins. The energy input per unit volume was directly obtained from the mean maximum valve head pressure per stroke. The mean maximum velocity of the emulsion in the valve head was 83m sec^?1 during a valve opening time of 150 × 10 ^?3 sec reflecting a large velocity gradient per stroke of 4.2 × 10^?6 m³ The method detected changes in the emulsifying activity of proteins resulting from chemical modification, and from process or environmental factors, e.g., ionic strength. The valve-head pressure profile was used to compare the fluidity of the emulsions at different levels of energy input per unit volume (E) and an apparent viscosity index (AVI) has been proposed.     

IDENTIFICATION OF PROCYANIDIN A2 AS POLYPHENOL OXIDASE SUBSTRATE IN PERICARP TISSUES OF LITCHI FRUIT

Postharvest browning of litchi fruit results in short shelf life and reduced commercial value. Experiments were conducted to separate, purify and identify polyphenol oxidase (PPO ) substrates that cause litchi fruit to brown. PPO and its substrate were extracted from the pericarp tissues of litchi fruit. The litchi PPO substrate was purified using polyamide column, silica gel column and Sephadex LH‐20 column chromatography. The browning substrate was selected by a 0.5% FeCl₃ solution and then identified using a partially purified litchi PPO. Analyses of ultraviolet spectrometry, nuclear magnetic resonance and electrospray ionization mass spectrometry indicated that the PPO substrate was procyanidin A2. The substrate can be oxidized to ο‐quinones by litchi PPO and then form brown‐colored by‐products, resulting in pericarp browning of harvested litchi fruit.     

PURIFICATION AND PARTIAL CHARACTERIZATION OF TWO α-AMYLASE INHIBITORS FROM BLACK BEAN (Phaseolus vulgaris)1

Two α-amylase inhibitors from black bean (Phaseolus vulgaris) were purified to homogencity using ammonium sulfate fractionation, DEAE-Sephadex chromatography, phenyl-Sepharose hydrophobic interaction chromatography and gel filtration with Sephadex G-100. The inhibitors were designated I–1 and I–2 based on their order of elution from the phenyl-Sepharose column. Both inhibitors are mannose containing glycoproteins, composed of subunits; active against porcine pancreatic, human salivary, and insect α-amylases and inactive against bacterial, mold, and plant α-amylases. The inhibitors I-1 and I–2 have molecular weights of 49,000 and 47,000 and isoelectric points 4.93 and 4.86, respectively. Both inhibitors have similar amino acid compositions and are rich in aspartic acid, serine, glutamic acid, valine, and threonine and are low in sulfur containing amino acids. I–2 is more resistant to heat denaturation than I-1.     

PARTIAL CHARACTERIZATION OF TRYPSIN-CHYMOTRYPSIN INHIBITORS FROM BEAN (PHASEOLUS VULGARIS L., VAR. ROSINHA G2): CHEMICAL AND PHYSICAL PROPERTIES

The three trypsin inhibitors A, B and C previously isolated from Brazilian pink bean (Phaseolus vulgaris L. var. Rosinha G2) had molecular weights of 18,200 to 18,500 by sodium dodecyl sulfate polyacrylamide gel electrophoresis, 20,000 by gel filtration on Sephadex G-100 and 20,400 by sucrose density gradient ultracentrifugation with a Stokes molecular radius of 20 Å, a frictional coefficient of 1.14, a diffusion coefficient of 10.7 × 10^?7 cm²s^?1, a partial specific volume of 0.69 cm³g^?1 and a molar absorptivity of 5.5 × 10³ M^?1 cm^?1 at 280 nm. All three inhibitors bound two moles of trypsin and one mole of chymotrypsin. The K_i values for trypsin were: A, 8.5 × 10^?10 M; B, 1.8 × 10^?10 M and C, 6.8 × 10^?10 M while for chymotrypsin they were: A, 4.4 × 10^?7 M; B, 2.8 × 10^?8 M and C, 3.0 × 10^?8 M. Reductive methylation caused loss of inhibitor activity of all three inhibitors against trypsin without significantly affecting inhibitor activity against chymotrypsin (with exception of inhibitor B), indicating that the inhibitors have lysine in binding site for trypsin. Partial reduction of the disulfide bonds caused loss of inhibitor activity against both trypsin and chymotrypsin with some regain of inhibitor activity following dialysis. Cyanogen bromide cleaved all three inhibitors into two fragments with significant retention of inhibitor activity. Cyanogen bromide-treated inhibitor B had nearly twice the original inhibitor activity against trypsin with no loss of inhibitor activity against chymotrypsin.