Lipoxygenase isozymes of peanut

Sanders, Timothy H.; Pattee, H. E.; Singleton, John

doi:10.1007/bf02532761

Cited by 43 publications

(30 citation statements)

References 13 publications

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“…These results are similar to that reported for French bean lipoxygenase (Kermasha and Metche, 1986). Cyanide ion was reported to inhibit partially purified lipoxygenase from peanut a t concentrations greater than 1 mM (Siddiqi and Tappel, 1957), while Sanders et al (1975) reported that cyanide ion concentration below 14 mM had little effect on the activity of a purified alkaline isozyme of peanut lipoxygenase but inhibited an acid isozyme lipoxygenase from the same seed. De Lumen et al (1978) demonstrated that 50% inhibition of green bean lipoxygenase was obtained a t 20 mM final cyanide concentration.…”

Section: Resultssupporting

confidence: 90%

Partial purification and characterization of lipoxygenase of canola seed (Brassica napus var. Westar)

Kermasha¹,

Alli²

1990

J. Agric. Food Chem.

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Lipoxygenase was extracted from canola seeds (Brassica napus var. Westar) and partially purified by precipitation with solid ammonium sulfate at 20-50 % of saturation. Further purification of the enzyme was performed by conventional ion-exchange chromatography on DEAE-cellulose. The partially purified enzyme demonstrated the presence of a major and two minor protein fractions which were also found in a commercial soybean lipoxygenase (Sigma Chemical Co.); however, the lipoxygenase activity profile indicates the presence of a single enzymatic active fraction in both canola seed extract and commercial soybean lipoxygenase. The pH for optimum activity was 7.5. The apparent K , value calculated from the best straight line was 2.0 X M. The effect of cyanide on the enzyme activity was investigated. The partially purified lipoxygenase from canola seed showed higher specificity for linoleic acid used as substrate as compared to linolenic acid. The activity of the canola lipoxygenase extract was considerably greater with linoleic acid as substrate when compared with linoleic acid esters; the observed order of activity was as follows: linoleic acid > monolinolein > dilinolein > trilinolein. However, the enzyme showed higher specificity for the canola lipid extract than for linoleic acid and its esters. A chromogenic reaction on polyacrylamide disc gel electrophoresis demonstrated that the enzyme activity in the canola lipoxygenase is associated with the major band.

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Section: Resultssupporting

confidence: 90%

Partial purification and characterization of lipoxygenase of canola seed (Brassica napus var. Westar)

Kermasha¹,

Alli²

1990

J. Agric. Food Chem.

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“…In the production of fatty acid hydroperoxides, the addition of an oxygen molecule to a polyunsaturated fatty acid is catalyzed by lipoxygenase enzymes. In peanuts, lipoxygenases are reported to be involved in the response to Aspergillus colonization (Burow et al., ; Sanders, Pattee, & Singleton, ). Lineoleic acid is one of the main fatty acids present in peanut lipids.…”

Section: Resultsmentioning

confidence: 99%

“…Heme was identified as having the second highest fold change and was significantly different between the market types ( P < 0.05). Peanut peroxidase, a heme peroxidase, is a classical extracellular plant peroxidase (Sanders et al., ). Extracellular plant peroxidases have been implicated in cell wall metabolism as well as in wound defense and plant hormone metabolism (Burow et al., ; Schuller, Ban, van Huystee, McPherson, & Poulos, ).…”

Section: Resultsmentioning

confidence: 99%

Metabolite Profiles of Raw Peanut Seeds Reveal Differences between Market‐Types

Klevorn

Dean

Johanningsmeier

2019

Journal of Food Science

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Peanuts (Arachis hypogaea L.) are prized for their flavor and popular worldwide as food or as food ingredients. The raw peanut seed contains the precursor compounds to roasted peanut flavor and has the potential to be manipulated through traditional breeding methods. However, little is known about the metabolome of the raw seeds. Comprehensive metabolite profiles of both raw runner and Virginia‐type peanuts were determined. Using a system incorporating several methodologies including (RP)/UPLC‐MS/MS and HILIC/UPLC‐MS/MS, along with quantitation of fatty acids, free amino acids, and tocopherols, 365 metabolites were identified and of these, 52 were significantly different between market types (P < 0.05). Higher levels of gamma‐glutamylalanine, oxylipins, purine metabolites, and alpha‐ketoglutarate derived members of the glutamate family of amino acids defined the Virginia‐type, while runner‐type peanuts were differentiated by their ethylmalonate and eicosenoate content. This study presents a comprehensive analysis of the raw peanut seed, providing knowledge of the range of small molecules present in peanuts. The new information presented here will enable future research for peanut quality improvement. Practical Application Peanuts are widely used as snack foods and as food ingredients. Knowledge of the secondary metabolite compounds in raw peanuts is needed to determine their importance in peanut flavor and nutritional quality. This report used a nontargeted analytical approach for the identification of these types of compounds in peanuts for the first time. These data were supplemented with quantitative analysis of free amino acids and tocopherols and discussed as potential flavor precursors and health promoting compounds.

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“…Samples were kept cold throughout the extraction process except when centrifuged. Enzymatic activity of the extract was measured polarigraphically in a reaction vessel fitted with a Clark oxygen electrode (Sanders et al, 1975). Lipoxygenase activity was determined by adding 200 μΕ of the aqueous enzyme extract to 1.5 mL of 82.50 linoleic acid and 0.8% Tween 20 in pH 6.4, 0.1 Μ phosphate buffer and aerated 0.2 mL phosphate buffer in a 1.7-μΕ reaction vessel.…”

Section: Methodsmentioning

confidence: 99%

Effect of Blanching on Peanut Shelf-Life1

Sanders

Adelsberg²,

Hendrix

et al. 1999

Peanut Science

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Blanching, seed coat removal, is often a processing step in peanut manufacturing but the general peanut industry consensus is that shelf-life reduction occurs as a result of the process. In order to examine the effects of blanching on shelf-life, runner-type peanuts were blanched using total heating time and final temperature in a 3 X 3 factorial experiment. In each of nine treat ments, heating began at 32 C and increased incremen tally through six heating zones over a total time of30,45, : The use of trade names in this publication does not imply endorsement by the U.S. Corresponding author.or 60 min to a final temperature of either 76.7, 87.8, or 98.9 C. Blanched peanuts from each treatment and nonblanched control samples were stored at 26 ± 1C and ambient RH and were sampled over a 28-wk period. Peroxide value (PV) and oxidative stability index (OSI) of blanched and nonblanched peanuts were similar indi cating no meaningful shelf-life differences. Descriptive sensory analysis of peanuts roasted when taken from storage indicated no significant differences in intensity of painty and cardboardy descriptors between blanched and nonblanched peanuts. Mean separations of at tributes, including roast peanutty, for which significant differences were noted revealed only a weak, inconsis tent relationship between descriptor intensities and final blanching temperature.

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Lipoxygenase isozymes of peanut

Cited by 43 publications

References 13 publications

Partial purification and characterization of lipoxygenase of canola seed (Brassica napus var. Westar)

Partial purification and characterization of lipoxygenase of canola seed (Brassica napus var. Westar)

Metabolite Profiles of Raw Peanut Seeds Reveal Differences between Market‐Types

Effect of Blanching on Peanut Shelf-Life1

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