ABSTRACT
Bioprocesses were developed to enhance the value of proteins from deoiled corn germ. Proteins were hydrolyzed with trypsin, thermolysin, GC 106, or Flavourzyme to generate the bioactive peptide sequences. At an enzyme to substrate ratio of 1:100, protein hydrolysis of wet-milled germ was greatest using thermolysin followed by trypsin, GC 106, and Flavourzyme. For the dry-milled corn germ, protein hydrolysis was greatest for GC 106 and least for Flavourzyme. Electrophoretic patterns indicated that the hydrolysis conditions used were adequate for generating low molecular weight peptides for both germs. Unhydrolyzed dry- and wet-milled corn germ did not appear to contain angiotensin I converting enzyme (ACE)-inhibitory peptides. After hydrolysis with trypsin, thermolysin, and GC 106 but not Flavourzyme, ACE inhibition was observed. ACE inhibition was greatest for the GC 106 hydrolysate for both wet- and dry-milled corn germ. Denaturing the protein with urea before hydrolysis, in general, increased the amount of ACE-inhibitory peptides found in the hydrolysate. Membrane fractionations of both the wet- and dry-milled hydrolysates indicated that most of the ACE-inhibitory peptides were in the <1 kDa fraction. Examination of the control total protein extracts (before treatment with proteases) from wet- and dry-milled germ revealed that neither had ACE-inhibitory properties. However, when both total corn germ control protein extracts were fractionated, the <1 kDa fraction of wet-milled corn germ proteins exhibited ACE inhibition, whereas the comparable low molecular weight fraction from dry-milled corn germ did not.
Subject(s)
Angiotensin-Converting Enzyme Inhibitors/isolation & purification , Peptide Fragments/isolation & purification , Plant Proteins/isolation & purification , Seeds/chemistry , Zea mays/chemistry , Food Handling/methods , Hydrolysis , Peptide Fragments/chemistry , Peptide Fragments/metabolism , Peptide Hydrolases/metabolism , Plant Proteins/chemistry , Plant Proteins/metabolismABSTRACT
To identify high-valued coproducts from commercially processed corn germ, it was necessary to determine the effect of processing conditions on corn germ proteins. We found that significantly less protein was extracted from commercial wet-milled as compared to dry-milled corn germ using Tris, sodium dodecyl sulfate (SDS) buffer containing 14 mM 2-mercaptoethanol at 100 degrees C for 10 min. SDS-polyacrylamide gel electrophoresis (PAGE) revealed a number of proteins with molecular masses ranging from approximately 10 to 66 kDa for the dry-milled corn germ as compared to only a few significant protein bands centered around 23 kDa in the wet-milled corn germ. The protein content of the wet- and dry-milled corn germ was approximately the same; however, nonprotein nitrogen values were significantly greater for the wet-milled than for the dry-milled germ. The distribution of fractionated germ protein freshly excised from the embryo of yellow dent corn kernels was more similar to that of dry-milled than wet-milled corn. SDS-PAGE of laboratory preparations of wet-milled corn germ more closely resembled commercial dry- than wet-milled corn germ, which could be attributed to limited microbial growth during steeping in the laboratory preparations.
Subject(s)
Agriculture/methods , Plant Proteins/analysis , Seeds/chemistry , Zea mays/chemistry , Electrophoresis, Polyacrylamide Gel , Food Handling/methods , Nitrogen/analysisABSTRACT
Adhesive properties on glass of commercial zein and an inexpensive zein-lipid mixture isolated from dry-milled corn were investigated. A method was developed for uniformly preparing bonded glass panels and measuring the amount of pull required to separate the panels. The adhesive strength of commercial zein to glass was greater at 29% than at 52% relative humidity (RH). Bonded samples prepared from zein isolates were less sensitive to changes in RH. Bonds using commercial zein formulations containing plasticizer reached a maximum strength at 10% poly(ethylene glycol) regardless of RH. Formulations that required the least amount of ethanol (35-42%) were obtained by adjusting its pH to 3 or 10 with a volatile acid or base. These formulations completely bonded to the glass panels at low sample concentrations as estimated by 100% cohesive failure and exhibited lower Young's Modulus values than most of the other bonding materials tested. Samples bonded with a polyvinyl acetate emulsion adhesive were not as strong as the zein-bonded samples and were sensitive to changes in RH.
Subject(s)
Glass , Zea mays/chemistry , Zein/chemistry , Adhesiveness , Ethanol , Hydrogen-Ion ConcentrationABSTRACT
Dry-milled yellow corn and freshly ground food and nonfood grade yellow and white hybrid corn kernels were pretreated in a solution of lactic acid and sodium metabisulfite followed by extraction with 70% ethanol. Zein was precipitated from the extract by reducing the ethanol content of the extract to 40%. Lipid associated with the zein isolates was between 15 and 20% and contained mostly endogenous free fatty acids. The effect of the endogenous free fatty acids on zein isolate films, with and without free fatty acids, was determined by measuring various film properties. Stress-strain measurements indicated 40-200% greater elongation for zein films containing endogenous free fatty acids. Films prepared from zein isolated from preground corn stored for approximately 4 months (27 degrees C, 17% relative humidity) had approximately 3 times greater elongation values than zein films prepared from freshly ground corn.
