cinnamate/potato

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Partial purification and characterization of UDPG:t-cinnamate glucosyltransferase in the root of sweet potato, Ipomoea batatas Lam.

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Previously, we isolated t-cinnamoyl-D-glucose as a possible intermediate in chlorogenic acid biosynthesis from sweet potato root. The enzyme which catalyzes the formation of t-cinnamoyl-D-glucose has been purified 539-fold from sweet potato root (Ipomoea batatas Lam.) and characterized. It required

Studies on the induction of cinnamic acid 4-hydroxylase in potato tuber.

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The change in activity of cinnamic acid 4-hydroxylase (CA4H) in potato parenchyma tissue exposed to various conditions has been examined. Maximum induction of CA4H activity was obtained at 18 hr of incubation. Though CA4H induction can occur in dark, over 100% increase in enzyme activity was

The Plant Pathogenic Bacterium Streptomyces scabies Degrades the Aromatic Components of Potato Periderm via the β-Ketoadipate Pathway.

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The outer potato periderm layer consists of dead suberized cells. Suberin, a protective biopolymer, is made of a polyaliphatic portion covalently linked to polyaromatic moieties. Evidence accumulates that Streptomyces scabies, the main causal agent of potato common scab, can degrade the

Nitrogen recycling during phenylpropanoid metabolism in sweet potato tubers.

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In the first step of the phenylpropanoid metabolic pathway, L-phenylalanine (L-Phe) is deaminated to form E-cinnamate, in a conversion catalyzed by phenylalanine ammonia-lyase (PAL; EC 4.3.1.5). The metabolic fate of the ammonium ion (NH4+) produced in this reaction was investigated in sweet potato

Chlorogenic Acid Biosynthesis Appears Linked with Suberin Production in Potato Tuber (Solanum tuberosum).

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Potato (Solanum tuberosum L.) is a good source of dietary antioxidants. Chlorogenic acid (CGA) and caffeic acid (CA) are the most abundant phenolic acid antioxidants in potato and are formed by the phenylpropanoid pathway. A number of CGA biosynthetic routes that involve hydroxycinnamoyl-CoA quinate

Molecular cloning and functional analysis of the ortho-hydroxylases of p-coumaroyl coenzyme A/feruloyl coenzyme A involved in formation of umbelliferone and scopoletin in sweet potato, Ipomoea batatas (L.) Lam.

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Ortho-hydroxylation of cinnamates is a key step in coumarin biosynthesis in plants. Ortho-hydroxylated cinnamates undergo trans/cis isomerization of the side-chain and then lactonization to form coumarins. Sweet potato [Ipomoea batatas (L.) Lam.] accumulates umbelliferone and scopoletin after biotic

Formation of p-coumaric acid and o-coumaric acid from L-phenylalanine by microsomal membrane fractions from potato: Evidence of membrane-bound enzyme complexes.

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The enzymes described here are the membrane-bound L-phenylalanine ammonia-lyase and cinnamate hydroxylase. Microsomes prepared from tubers of Solanum tuberosum L. are capable of converting L-phenylalanine into both o- and p-coumaric acid. Three microsomal fractions obtained by density gradient

Pre-heating and polyphenol oxidase inhibition impact on extraction of purple sweet potato anthocyanins.

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Purple sweet potatoes (PSP) have been used as a natural food colorant with high acylated anthocyanins concentrations. Commercially extracting pigments from PSP can be challenging due to firm texture and high polyphenol oxidase (PPO) content. These studies evaluated hot water immersions (30, 50, 70,

Phenylalanine ammonia-lyase: enzymic conversion of 3-(1,4-cyclohexadienyl)-L-alanine to trans-3-(1,4-cyclohexadienyl)acrylic acid.

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The phenylalanine analogue 3-(1,4-cyclohexadienyl)-L-alanine is converted to the hitherto unknown cinnamate analogue trans-3-(1,4-cyclohexadienyl)acrylic acid by L-phenylalanine ammonia-lyase (EC 4.3.1.5) from maize, potato, or Rhodotorula glutinis. The structure assigned to the product is confirmed

l-Phenylalanine Ammonia-Lyase (Maize): Evidence for a Common Catalytic Site for l-Phenylalanine and l-Tyrosine.

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l-Phenylalanine ammonia-lyase (E.C. 4.3.1.5) from maize is active with l-tyrosine and l-phenylalanine and exhibits atypical Michaelis-Menten kinetics with both substrates. With phenylalanine as a substrate, the pH optimum is 8.7 and with tyrosine, 7.7. The estimated Km at high substrate

Hybridization of the natural antibiotic, cinnamic acid, with layered double hydroxides (LDH) as green pesticide.

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OBJECTIVE Heavy application of highly toxic synthetic pesticides has been committed to protect crops against insects and diseases, which have brought about serious environmental problems. Thus, an inevitable and fundamental issue has been how to protect crops without harmful effects on nature. As a

Toxicity of allyl esters in insect cell lines and in Spodoptera littoralis larvae.

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We investigated the effects of five allyl esters, two aromatic (allyl cinnamate and allyl 2-furoate) and three aliphatic (allyl hexanoate, allyl heptanoate, and allyl octanoate) in established insect cell lines derived from different species and tissues. We studied embryonic cells of the fruit fly

Status of bioactive compounds in foods, with focus on fruits and vegetables.

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Components of cereals, legumes, pulses, proteins, sea food, milk, carbohydrates and lipids are being evaluated for their influence on human health, as biofunctional compounds. However, references dealing with fruits and vegetables exceed any other food group and accordingly their focus. Fruits and

Biosynthesis of salicylic acid in plants.

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Salicylic acid (SA) is an important signal molecule in plants. Two pathways of SA biosynthesis have been proposed in plants. Biochemical studies using isotope feeding have suggested that plants synthesize SA from cinnamate produced by the activity of phenylalanine ammonia lyase (PAL). Silencing of

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