**5. Storage proteins**

Seed yield is a complex trait as it is the product of several individual yield components such as number of inflorescences per plant, number of pods per inflorescence, number of pods per plant, number of seeds per inflorescence, seed weight per pods, seed weight per inflorescence and mean seed weight [45]. In oilseed crops oil is an essential component obtained from seeds. There are many factors that influence seed yield and seed quality such as genotype, agronomic techniques nutritional disorder and the environment. Seed quality is reflected in seedling density, seedling vigor, the competitiveness and uniformity of crop growth [46]. The quality of grains is basically depended on the storage proteins

**181**

*Impact of Inadequate Concentration of Boron in Seed Storage Proteins Content in Oilseed Crops*

present in their seeds. These proteins are mainly stored in seeds and came into existence at the time of seed development and acts as a nitrogen source during germination. [47] suggested that the polypeptide Polymorphic characteristics of storage protein is due to the existence of multigene families and this polymorphism can be seen within single genotypes as well as among genotypes of the

The storage protein present in seeds ranging from ~10% (in cereals) to 40% (in certain legumes and oilseeds) of dry weight, are the fruitful source of dietary protein. Seeds comprised of one or more groups of proteins that are in abundance and acts as a store house for amino acids which can be use all along the seed germination and seedling growth. The total protein content present in seeds in the form of storage reserve determined the quality of seeds for various purposes [47]. Among several kinds of proteins four major types of storage proteins are known- globulins (insoluble in water), albumins (soluble in water), prolamins and glutelins, which are alcohol and alkali soluble respectively [48]. Globulins and albumins are the major storage seed proteins of legumes and oilseed crops whereas prolamins and glutelins are mostly found in cereal seeds. All four types of storage proteins are

Albumin proteins are mostly found in dicot seeds. These storage proteins are accumulated in the protein bodies of developing seeds and are serve as a source of sulfur-containing amino acids and carbon skeletons for providing nutrition to the growing seedlings and germination of the seeds. Despite of their physiological role, these small globular proteins in plants are also having an area of interest in the field of nutritional and clinical studies [49]. Agizzio *et al*. [50] have investigated that 2S albumins can also acts as defensive weapons for the protection against fungal invasion in plants. Arabidopsis and oilseed rape (family- Cruciferae) plants are most commonly used to study these proteins. In oilseed rape plants this protein is named as napins. Ericson et al. [51] suggested that the napins consist of two polypeptide chains with *M,* values of −9000 and 4000, linked together with interchain disulfide bonds. The synthesis of napins gave rise a single precursor proteins in which proteolytic cleavage occurred. Due to this cleavage the loss of a linker peptide and short peptides from both the N and C termini was reported [51, 52]. All the 2 s albumins are compact globular proteins with conserved cysteine residues inspite of differing

Globulin storage proteins are found to be stored in the embryo and outer aleurone layer of the endosperm [53]. These proteins having sedimentation coefficients, approximately 7 and are found to be quickly dissolve in dilute salt solution. Kriz and Wallace [53] examined that the protein bodies are the main storage site for 7S globulins. The most primitive cupin superfamily is the representative of globulin proteins. On the basis of their sedimentation coefficients, they are of 11S legumin and 7S vicilin types. Globulins perform various functions such as sucrose binding, desiccation, defense against microbes, hormone binding and oxidative stress etc. in plant and also have nutritional values in seeds [54]. The functioning of globulin proteins in seed development was investigated by Hye-Jung Lee *et al.* [55]. According to their findings, deficiency in globulin induces the reduction in the expression of other seed storage proteins (glutelins and prolamins) in dry seeds of a rice mutant (Glb-RNAi) as compared to wild type. They also suggested that the

*DOI: http://dx.doi.org/10.5772/intechopen.95873*

classified as simple globular proteins.

in their subunit structure and synthesis.

same species.

**5.1 Albumins**

**5.2 Globulin**

*Impact of Inadequate Concentration of Boron in Seed Storage Proteins Content in Oilseed Crops DOI: http://dx.doi.org/10.5772/intechopen.95873*

present in their seeds. These proteins are mainly stored in seeds and came into existence at the time of seed development and acts as a nitrogen source during germination. [47] suggested that the polypeptide Polymorphic characteristics of storage protein is due to the existence of multigene families and this polymorphism can be seen within single genotypes as well as among genotypes of the same species.

The storage protein present in seeds ranging from ~10% (in cereals) to 40% (in certain legumes and oilseeds) of dry weight, are the fruitful source of dietary protein. Seeds comprised of one or more groups of proteins that are in abundance and acts as a store house for amino acids which can be use all along the seed germination and seedling growth. The total protein content present in seeds in the form of storage reserve determined the quality of seeds for various purposes [47]. Among several kinds of proteins four major types of storage proteins are known- globulins (insoluble in water), albumins (soluble in water), prolamins and glutelins, which are alcohol and alkali soluble respectively [48]. Globulins and albumins are the major storage seed proteins of legumes and oilseed crops whereas prolamins and glutelins are mostly found in cereal seeds. All four types of storage proteins are classified as simple globular proteins.

#### **5.1 Albumins**

*Grain and Seed Proteins Functionality*

apple; 'Water core' of turnip'; 'Hard fruit' of Citrus; 'Yellows' of alfa alfa; 'Hen and chicken' of grapes; 'Heart rot' of sugarbeet; 'Stem crack' of celery; 'Hollow stem' of cauliflower and broccoli and 'Tipburn' of chinese cabbage ([41, 42]; **Figure 1**). Boron deficiency also creates an unfavorable situation for the pollen-stigma interaction and limits fertilization leading to poor reproductive yield ([42]; **Figure 1**). Boron takes part in various vital functioning of crops like translocation of sugars, metabolism of RNA, protein, indole acetic acid, phenols, ascorbate, osmotic and

*Various symptoms in plants received inadequate boron nutrition (data source online except 11 and 12 these are* 

Seed yield is a complex trait as it is the product of several individual yield components such as number of inflorescences per plant, number of pods per inflorescence, number of pods per plant, number of seeds per inflorescence, seed weight per pods, seed weight per inflorescence and mean seed weight [45]. In oilseed crops oil is an essential component obtained from seeds. There are many factors that influence seed yield and seed quality such as genotype, agronomic techniques nutritional disorder and the environment. Seed quality is reflected in seedling density, seedling vigor, the competitiveness and uniformity of crop growth [46]. The quality of grains is basically depended on the storage proteins

**180**

oxidative stress etc. [1, 43, 44].

*original data from our experiment).*

**5. Storage proteins**

**Figure 1.**

Albumin proteins are mostly found in dicot seeds. These storage proteins are accumulated in the protein bodies of developing seeds and are serve as a source of sulfur-containing amino acids and carbon skeletons for providing nutrition to the growing seedlings and germination of the seeds. Despite of their physiological role, these small globular proteins in plants are also having an area of interest in the field of nutritional and clinical studies [49]. Agizzio *et al*. [50] have investigated that 2S albumins can also acts as defensive weapons for the protection against fungal invasion in plants. Arabidopsis and oilseed rape (family- Cruciferae) plants are most commonly used to study these proteins. In oilseed rape plants this protein is named as napins. Ericson et al. [51] suggested that the napins consist of two polypeptide chains with *M,* values of −9000 and 4000, linked together with interchain disulfide bonds. The synthesis of napins gave rise a single precursor proteins in which proteolytic cleavage occurred. Due to this cleavage the loss of a linker peptide and short peptides from both the N and C termini was reported [51, 52]. All the 2 s albumins are compact globular proteins with conserved cysteine residues inspite of differing in their subunit structure and synthesis.

#### **5.2 Globulin**

Globulin storage proteins are found to be stored in the embryo and outer aleurone layer of the endosperm [53]. These proteins having sedimentation coefficients, approximately 7 and are found to be quickly dissolve in dilute salt solution. Kriz and Wallace [53] examined that the protein bodies are the main storage site for 7S globulins. The most primitive cupin superfamily is the representative of globulin proteins. On the basis of their sedimentation coefficients, they are of 11S legumin and 7S vicilin types. Globulins perform various functions such as sucrose binding, desiccation, defense against microbes, hormone binding and oxidative stress etc. in plant and also have nutritional values in seeds [54]. The functioning of globulin proteins in seed development was investigated by Hye-Jung Lee *et al.* [55]. According to their findings, deficiency in globulin induces the reduction in the expression of other seed storage proteins (glutelins and prolamins) in dry seeds of a rice mutant (Glb-RNAi) as compared to wild type. They also suggested that the

globulin might have a crucial role in a transcriptional mechanism and in the de novo protein maturation process of storage proteins in the rice endosperm.
