CHARACTERIZATION OF LIGNIN-CARBOHYDRATE COMPLEXES OF ITALIAN RYEGRASS AND ALFALFA

1990 ◽  
Vol 70 (1) ◽  
pp. 193-201 ◽  
Author(s):  
TSUNEO KONDO ◽  
KAZUHIKO MIZUNO ◽  
TADASHI KATO ◽  
TADAKAZU HIROI
Keyword(s):  
Enzymatic Hydrolysis ◽  
Ferulic Acid ◽  
Enzymatic Degradation ◽  
Produced Water ◽  
Lolium Multiflorum ◽  
Complex Structure ◽  
Italian Ryegrass ◽  
Syringyl Lignin ◽  
Insoluble Material ◽  
Ferulic Acids

Lignin-carbohydrate complexes (LCC) were isolated from Italian ryegrass (Lolium multiflorum Lam.) and alfalfa (Medicago sativa L.) stems and their chemical and physical properties, and enzymatic degradation examined. The LCCs, soluble in water, were composed of guaiacyl-syringyl lignin and hemicellulosic carbohydrate mostly consisting of xylose, glucose and arabinose. Enzymatic hydrolysis of the LCCs produced water-insoluble materials which were markedly rich in lignin. In both plant species, the carbohydrate of the insoluble material had a high proportion of arabinose. The insoluble material of Italian ryegrass contained two to three times more xylose and arabinose than that of alfalfa. The Italian ryegrass LCC released significant amounts of p-coumaric and ferulic acids by alkaline and acid hydrolysis, but the alfalfa LCC did not, indicating a more complex structure of the cell wall matrix of Italian ryegrass. The ferulic acid in ryegrass lignin may be responsible for restricting enzymatic degradation of hemicellulose in ryegrass more than occurs in legumes.Key words: Lignin-carbohydrate complex, enzymatic hydrolysis, hemicellulose, ferulic acid, Italian ryegrass, alfalfa

CELL WALL-BOUND p-COUMARIC AND FERULIC ACIDS IN ITALIAN RYEGRASS

1990 ◽  
Vol 70 (2) ◽  
pp. 495-499 ◽  
Author(s):  
TSUNEO KONDO ◽  
KAZUHIKO MIZUNO ◽  
TADASHI KATO
Keyword(s):  
Cell Wall ◽  
Ferulic Acid ◽  
Lolium Multiflorum ◽  
Italian Ryegrass ◽  
Coumaric Acid ◽  
Stages Of Growth ◽  
Cell Wall Polymers ◽  
Cross Links ◽  
Ferulic Acids ◽  
Acid Esters

Cell wall-bound p-coumaric and ferulic acids were determined for stems of Italian ryegrass (Lolium multiflorum Lam.) sampled at different stages of growth. The greater part of the detected p-coumaric acid was linked to cell wall polymers through ester linkages. No definite relationship was found between the accumulation of p-coumaric acid esters and plant maturation. Some part of the detected ferulic acid was simultaneously esterified and etherified to cell wall polymers. Such ester- and ether-linked ferulic acid augmented with increasing maturity, suggesting that the number of ferulic acid cross-links in the cell wall matrices of ryegrass increases with plant maturation.Key words: p-coumaric acid, ferulic acid, Italian ryegrass, cell wall, phenolic acids

Inhibitory effects of Italian ryegrass (Lolium multiflorum Lam.) seedlings of rice (Oryza sativa L.)

2018 ◽  
Vol 44 (2) ◽  
pp. 219-232 ◽  
Author(s):  
S.J Jang ◽  
K.R. Kim ◽  
Y.B. Yun ◽  
S.S. Kim ◽  
Y.I Kuk
Keyword(s):  
Oryza Sativa ◽  
Oryza Sativa L ◽  
Lolium Multiflorum ◽  
Italian Ryegrass ◽  
Inhibitory Effects

Quantitative trait loci analysis of nitrate-nitrogen content in Italian ryegrass (Lolium multiflorum Lam.)

Euphytica ◽  
2021 ◽  
Vol 217 (1) ◽  
Author(s):  
Wenqing Tan ◽  
Di Zhang ◽  
Nana Yuyama ◽  
Jun Chen ◽  
Shinichi Sugita ◽  
...  
Keyword(s):  
Quantitative Trait Loci ◽  
Nitrogen Content ◽  
Quantitative Trait ◽  
Nitrate Nitrogen ◽  
Lolium Multiflorum ◽  
Italian Ryegrass ◽  
Trait Loci

scholarly journals Highly-Efficient Release of Ferulic Acid from Agro-Industrial By-Products via Enzymatic Hydrolysis with Cellulose-Degrading Enzymes: Part I–The Superiority of Hydrolytic Enzymes Versus Conventional Hydrolysis

Foods ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 782
Author(s):  
Karina Juhnevica-Radenkova ◽  
Jorens Kviesis ◽  
Diego A. Moreno ◽  
Dalija Seglina ◽  
Fernando Vallejo ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Ferulic Acid ◽  
Hydrolytic Enzymes ◽  
Structural Complexity ◽  
Triticum Aestivum L ◽  
Feed Supplement ◽  
Degrading Enzymes ◽  
Secale Cereale L ◽  
Pre Treatment ◽  
By Products

Historically Triticum aestívum L. and Secale cereále L. are widely used in the production of bakery products. From the total volume of grain cultivated, roughly 85% is used for the manufacturing of flour, while the remaining part is discarded or utilized rather inefficiently. The limited value attached to bran is associated with their structural complexity, i.e., the presence of cellulose, hemicellulose, and lignin, which makes this material suitable mostly as a feed supplement, while in food production its use presents a challenge. To valorize these materials to food and pharmaceutical applications, additional pre-treatment is required. In the present study, an effective, sustainable, and eco-friendly approach to ferulic acid (FA) production was demonstrated through the biorefining process accomplished by non-starch polysaccharides degrading enzymes. Up to 11.3 and 8.6 g kg−1 of FA was released from rye and wheat bran upon 24 h enzymatic hydrolysis with multi-enzyme complex Viscozyme® L, respectively.

Protection of Italian ryegrass (Lolium multiflorum L.) seedlings from salinity stress following seed priming with L-methionine and casein hydrolysate

2020 ◽  
pp. 1-9
Author(s):  
Keum-Ah Lee ◽  
Youngnam Kim ◽  
Hossein Alizadeh ◽  
David W.M. Leung
Keyword(s):  
Oxidative Stress ◽  
Amino Acids ◽  
Salinity Stress ◽  
Lolium Multiflorum ◽  
Casein Hydrolysate ◽  
Seed Priming ◽  
Germination Percentage ◽  
Italian Ryegrass ◽  
Significant Difference ◽  
Protein Amino Acids

Abstract Seed priming with water (hydropriming or HP) has been shown to be beneficial for seed germination and plant growth. However, there is little information on the effects of seed priming with amino acids and casein hydrolysate (CH) compared with HP, particularly in relation to early post-germinative seedling growth under salinity stress. In this study, Italian ryegrass seeds (Lolium multiflorum L.) were primed with 1 mM of each of the 20 protein amino acids and CH (200 mg l−1) before they were germinated in 0, 60 and 90 mM NaCl in Petri dishes for 4 d in darkness. Germination percentage (GP), radicle length (RL) and peroxidase (POD) activity in the root of 4-d-old Italian ryegrass seedlings were investigated. Generally, when the seeds were germinated in 0, 60 and 90 mM NaCl, there was no significant difference in GP of seeds among various priming treatments, except that a higher GP was observed in seeds of HP treatment compared with the non-primed seeds when incubated in 60 mM NaCl. When incubated in 60 and 90 mM NaCl, seedlings from seeds primed with L-methionine or CH exhibited greater RL (greater protection against salinity stress) and higher root POD activity than those from non-primed and hydro-primed seeds. Under salinity stress, there were higher levels of malondialdehyde (MDA) in the root of 4-d-old Italian ryegrass seedlings, a marker of oxidative stress, but seed priming with CH was effective in reducing the salinity-triggered increase in MDA content. These results suggest that priming with L-methionine or CH would be better than HP for the protection of seedling root growth under salinity stress and might be associated with enhanced antioxidative defence against salinity-induced oxidative stress.

scholarly journals Characterization of the hydroxyproline-rich protein core of an arabinogalactan-protein secreted from suspension-cultured Lolium multiflorum (Italian ryegrass) endosperm cells

1989 ◽  
Vol 264 (3) ◽  
pp. 857-862 ◽  
Author(s):  
P A Gleeson ◽  
M McNamara ◽  
R E H Wettenhall ◽  
B A Stone ◽  
G B Fincher
Keyword(s):  
Polyclonal Antibodies ◽  
Lolium Multiflorum ◽  
Italian Ryegrass ◽  
Arabinogalactan Protein ◽  
Myeloma Protein ◽  
Protein Core ◽  
Liquid Suspension ◽  
Peptide Component ◽  
Immunodominant Epitopes

An arabinogalactan-protein (AGP) purified from the filtrate of liquid-suspension-cultured Italian-ryegrass (Lolium multiflorum) endosperm cells by affinity chromatography on myeloma protein J539-Sepharose was deglycosylated with trifluoromethanesulphonic acid to remove polysaccharide chains that are covalently associated with hydroxyproline residues in the peptide component of the proteoglycan. The protein core, which accounts for less than 10% (w/w) of the intact proteoglycan, was purified by h.p.l.c. It has an apparent Mr of 35,000, but reacts very poorly with both Coomassie Brilliant Blue R and silver stains. Amino-acid-sequence analysis of the N-terminus of the h.p.l.c.-purified protein core and of tryptic peptides generated from the unpurified protein reveals a high content of hydroxyproline and alanine. These are sometimes arranged in short (Ala-Hyp) repeat sequences of up to six residues. Polyclonal antibodies raised against the protein core do not cross-react with native AGP, the synthetic peptide (Ala-Hyp)4, poly-L-hydroxyproline or poly-L-proline. The results suggest that the polysaccharide chains in the native AGP render the protein core of the proteoglycan inaccessible to the antibodies and that the immunodominant epitopes include domains of the protein other than those rich in Ala-Hyp repeating units.

Seed germination behavior of glyphosate‐resistant and susceptible Italian ryegrass ( Lolium multiflorum Lam.)

2020 ◽  
Author(s):  
Afonso Henrique Schaeffer ◽  
Diógenes Cecchin Silveira ◽  
Otávio Augusto Schaeffer ◽  
Nadia Canali Lângaro ◽  
Leandro Vargas
Keyword(s):  
Seed Germination ◽  
Lolium Multiflorum ◽  
Italian Ryegrass
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