Characterization and evolutionary relationship of methionine-rich legumin-like protein from buckwheat

Samardžić, Jelena; Milisavljevic, Мilan; Brkljačić, Jelena; Konstantinović, Miroslav; Maksimović, Vesna

doi:10.1016/j.plaphy.2003.11.001

Cited by 21 publications

(12 citation statements)

References 33 publications

(38 reference statements)

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“…Recently, several genomic clones corresponding to 13S buckwheat globulin have been characterized. The acidic and basic polypeptides were found to contain 293 and 191 amino acids, respectively, and the calculated M w of 13S buckwheat globulin was 342,258 Da (Fujino, Funatsuki, Inada, Shimono, & Kikuta, 2001;Nair & Adachi, 2002;Nair, Ohmoto, Woo, & Adachi, 1999;Samardzic, Milisavljevic, & Brkljacic, 2004).…”

Section: Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresismentioning

confidence: 99%

Extraction, purification and characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) seeds

Choi

2006

Food Research International

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Section: Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresismentioning

confidence: 99%

Extraction, purification and characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) seeds

Choi

2006

Food Research International

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“…Konishi and others () reported that its apparent MM is 440 kDa and that it is composed of at least 4 different subunit types (MMs of 18, 20, 32, and 36 kDa). It is now generally accepted that the 13S globulins exist as proteins with an apparent MM between 280 and 390 kDa (Maksimovic ; Marcone and others ; Fujino and others ; Nair and Adachi ; Samardžić and others ; Choi and Ma ; Choi and others ) made up of 6 nonidentical monomers (Maksimovic and others ; Choi and Ma ; Choi and others ). The monomers interact noncovalently and each consists of a smaller (16 to 29 kDa) basic subunit SS‐linked to a larger (30 to 47 kDa) acidic subunit (Maksimovic and others ; Radovic and others ; Rout and others ; Bharali and Chrungoo ; Choi and Ma ; Choi and others ; Tang ).…”

Section: Osborne‐type Fractionation and Structural Propertiesmentioning

confidence: 99%

Proteins of Amaranth (Amaranthus spp.), Buckwheat (Fagopyrum spp.), and Quinoa (Chenopodium spp.): A Food Science and Technology Perspective

Janssen

Pauly

Rombouts

et al. 2016

Comp Rev Food Sci Food Safe

137

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There is currently much interest in the use of pseudocereals for developing nutritious food products. Amaranth, buckwheat, and quinoa are the 3 major pseudocereals in terms of world production. They contain high levels of starch, proteins, dietary fiber, minerals, vitamins, and other bioactives. Their proteins have well-balanced amino acid compositions, are more sustainable than those from animal sources, and can be consumed by patients suffering from celiac disease. While pseudocereal proteins mainly consist of albumins and globulins, the predominant cereal proteins are prolamins and glutelins. We here discuss the structural properties, denaturation and aggregation behaviors, and solubility, as well as the foaming, emulsifying, and gelling properties of amaranth, buckwheat, and quinoa proteins. In addition, the technological impact of incorporating amaranth, buckwheat, and quinoa in bread, pasta, noodles, and cookies and strategies to affect the functionality of pseudocereal flour proteins are discussed. Literature concerning pseudocereal proteins is often inconsistent and contradictory, particularly in the methods used to obtain globulins and glutelins. Also, most studies on protein denaturation and techno-functional properties have focused on isolates obtained by alkaline extraction and subsequent isoelectric precipitation at acidic pH, even if the outcome of such studies is not necessarily relevant for understanding the role of the native proteins in food processing. Finally, even though establishing in-depth structure-function relationships seems challenging, it would undoubtedly be of major help in the design of tailor-made pseudocereal foods.

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“…To obtain a longer upstream region containing the leader intron, we designed a primer pair in which the forward primer (If) was from the 5 0 -UTR of FeAP9 cDNA and the reverse primer (Ir) was from the FeAP9 coding region. The reaction conditions for PCRs are described in Samardžić et al (2004). Amplification products were eluted and cloned in pGEM-T Easy vector (Promega) and then sequenced using the ABI PRISM 3100 DNA Sequencer (BMR Servizio Sequenciamento Service, Padova, Italy).…”

Section: Amplification Of the Genomic Sequencesmentioning

confidence: 99%

Ubiquitous aspartic proteinase as an actor in the stress response in buckwheat

Timotijević

Milisavljevic

Radović

et al. 2010

Journal of Plant Physiology

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Characterization and evolutionary relationship of methionine-rich legumin-like protein from buckwheat

Cited by 21 publications

References 33 publications

Extraction, purification and characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) seeds

Extraction, purification and characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) seeds

Proteins of Amaranth (Amaranthus spp.), Buckwheat (Fagopyrum spp.), and Quinoa (Chenopodium spp.): A Food Science and Technology Perspective

Ubiquitous aspartic proteinase as an actor in the stress response in buckwheat

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