1983
DOI: 10.1007/bf02787446
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Increased oilseed protein solubility after peroxide exposure

Abstract: Oilseed proteins of peanut (arachin), pumpkin (cucurbitin) and soy (ll-S glycinin) were exposed to 30% H:O 2. Solubilities of arachin, cucurbitin, and glycinin increased 8.5-fold, 40-fold, and ca. 200-fold, respectively, in aqueous (arachin and cucurbitin) or acidic (glycinin) media. Implications for utilization of oilseed proteins following exposure-to H~ 02 are discussed.

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Cited by 4 publications
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“…In our earlier studies (8,9), cucurbitin was exposed to H202 for 2 h and then dialyzed against catalase for peroxide removal. Dialysis, however, produced additional time of actual contact to peroxide while it was being depleted by irreversible destructive diffusion.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…In our earlier studies (8,9), cucurbitin was exposed to H202 for 2 h and then dialyzed against catalase for peroxide removal. Dialysis, however, produced additional time of actual contact to peroxide while it was being depleted by irreversible destructive diffusion.…”
Section: Resultsmentioning
confidence: 99%
“…Their solubilities in water increase, however, after chemical modifications such as acylation, mild oxidation and partial hydrolysis {3-5). Regarding oxidatively induced solubilization, cucurbitin, which is the principal seed storage protein of Cucurbitaceae (cucurbits such as gourds, melons, pumpkins) as well as a physicochemically typical oilseed globulin {6,7}, becomes soluble in salt~free and peroxide~free water after being exposed to H202 (8,9). However, the length of exposure required to render cucurhitin wate~soluble has not been determine~ In this communication we describe changes in the solubility of cucurbitin after several different periods of exposure to H202.…”
mentioning
confidence: 95%