Gene Technology for Improved Weed, Insect, and Disease Control and for Seed Protein Quality.

Author(s):  
H. E. Schroeder ◽  
J. E. Barton ◽  
L. M. Tabe ◽  
L. Molvig ◽  
J. E. Grant ◽  
...  
Author(s):  
Bidyut Kumar Sarmah ◽  
Rubi Gupta ◽  
Sumita Acharjee

Background: Evaluation of the nutritional composition of genetically modified (GM) crops is mandatory for their deregulation. Chickpea is known for its high-quality protein and demonstrating that the seed protein quality of transgenic chickpea remains unaltered is important for its acceptance. Amino acid content, seed storage protein profile and the digestibility of chickpea protein are important determinants of seed protein quality. Thus, in the present study, we assessed the effect of Bt (Cry2Aa) gene expression on the Bt chickpea seed protein quality. Methods: We assessed the amino acid profile, in vitro protein digestibility and factors affecting protein digestibility like trypsin inhibitor, tannins and phytic acid contents of the transgenic Bt chickpea expressing a codon modified Cry2Aa gene and its non-transgenic counterpart. Furthermore, the seed storage proteins were also fractionated and separated on SDS-PAGE followed by mass spectroscopy of the major peptides. Result: Amino acid profile and factors affecting protein digestibility revealed no significant variations between transgenic and non-transgenic chickpeas. Seed storage protein profile confirmed the presence of legumin, vicilin and albumin. No potential change in the digestibility pattern of seed proteins was revealed. Our findings suggest no potential unintended changes in chickpea seed protein quality due to the expression of Cry2Aa gene.


Author(s):  
L. Molvig ◽  
L. M. Tabe ◽  
J. Hamblin ◽  
V. Ravindran ◽  
W. L. Bryden ◽  
...  

1993 ◽  
Vol 35 (1-2) ◽  
pp. 95-115 ◽  
Author(s):  
Patrice Martin ◽  
François Grosclaude

Foods ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 391 ◽  
Author(s):  
Khazaei ◽  
Subedi ◽  
Nickerson ◽  
Martínez-Villaluenga ◽  
Frias ◽  
...  

Grain legumes are widely recognized as staple sources of dietary protein worldwide. Lentil seeds are an excellent source of plant-based proteins and represent a viable alternative to animal and soybean proteins for food processing formulations. Lentil proteins provide not only dietary amino acids but are also a source of bioactive peptides that provide health benefits. This review focuses on the current knowledge of seed protein, extraction and isolation methods, bioactive peptides, and food applications of lentil protein. Lentil is the most rapidly expanding crop for direct human consumption, and has potential for greater impact as a protein source for food processing applications. Improvements in lentil protein quality, amino acid composition, and processing fractions will enhance the nutritional quality of this rapidly expanding crop globally.


1984 ◽  
Vol 32 (4) ◽  
pp. 815-819 ◽  
Author(s):  
David F. Hildebrand ◽  
Makoto Kito

2011 ◽  
Vol 62 (9) ◽  
pp. 765 ◽  
Author(s):  
Shahidul Islam ◽  
Wujun Ma ◽  
Junhong Ma ◽  
Bevan J. Buirchell ◽  
Rudi Appels ◽  
...  

Narrow-leafed lupin (NLL) is one of the major legume crops in Australian farming systems which is largely used as animal feed. Several modern cultivars have been developed through breeding making NLL feasible for use as human food. Significant health benefits have been recognised for NLL. The current study characterised protein polymorphism among 25 Australian cultivars through mass spectrometry (MALDI-TOF) with the aim of developing molecular breeding strategies to improve protein quality and content. A total of 364 seed protein mass peaks were clearly identified by MALDI-TOF and 50 protein mass peaks were cultivar specific. In addition, 9 protein mass peaks were found present in all cultivars and 61 protein mass peaks present in 2–3 cultivars only. Phylogenic analysis based on the protein profile categorised the cultivars into 2 major groups, which are broadly supported by pedigree information. The low proportion (2.4%) of common protein mass peaks among the cultivars suggested a high level of diversity in seed protein of NLL.


1993 ◽  
Vol 58 (2) ◽  
pp. 264S-269S ◽  
Author(s):  
B A Larkins ◽  
C R Lending ◽  
J C Wallace

1975 ◽  
Vol 39 (2) ◽  
pp. 102-105
Author(s):  
Pinkham ◽  
G Ori ◽  
SH Wei ◽  
CA Full ◽  
FM Parkins

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