ABSTRACT
Zein isolation by aqueous ethanol extraction from dry-milled corn produces a mixture of zeins, covalently linked polymers (dimers, tetramers, etc.) and higher-molecular-weight aggregates, some of which were not soluble in aqueous alcohol. The insoluble particles were identified as protein aggregates which form when the extraction solution is heated, particularly under alkaline conditions. The insoluble protein aggregates were not present in zein isolated by the same method from corn gluten meal. Zeins extracted from corn gluten meal and dry-milled corn were fractionated (by differential solubility) to identify differences in their polypeptide compositions. Using polyacrylamide gel electrophoresis, beta- and gamma-zeins were detected in dry-milled corn, but only trace amounts of beta-zein were found in corn gluten meal. Treatment of dry-milled corn with 0.55% lactic acid and 0.2% sulfur dioxide at 50 degrees C for 6 h before ethanol extraction resulted in a 50% increase in zein isolate yield with high solubility (98%). This pre-extraction treatment cleaved disulfide linkages of the beta- and gamma-zeins and significantly reduced insoluble aggregates in zein isolates.
Subject(s)
Disulfides/chemistry , Zea mays/chemistry , Zein/analysis , Electrophoresis, Polyacrylamide Gel , Food Handling/methods , Plant Structures/chemistry , Solubility , Zein/isolation & purificationABSTRACT
An inexpensive zein-lipid mixture was isolated from yellow dent, dry-milled corn. Grease permeation through zein isolate applied to brown Kraft paper was found to be independent of loading levels at zein isolate levels above 30 mg/16 in.(2). The data shows that water vapor transmission rates depended on the amount of coating applied. Triacylglycerols were the most abundant lipid in milled corn but were absent in the zein isolate (perhaps due to hydrolysis by lipases). Zein from the paper was hydrolyzed enzymatically and the hydrolysis monitored by SDS-capillary electrophoresis. At an E:S ratio of 1:100 no further increase in the hydrolysate peak occurred after 10 and 30 min for alpha-chymotrypsin and pancreatin 8 x; however, zein and lipid were still present 1 h after hydrolysis by pancreatin 1 x.
