Close

Current Research in Nutrition and Food Science - An open access, peer reviewed international journal covering all aspects of Nutrition and Food Science

lock and key

Sign in to your account.

Account Login

Forgot your password?

Plant Seed Proteins: Chemistry, Technology and Applications

Sachin K Sonawane, Shalini S Arya*

Food Engineering and Technology Department, Institute of Chemical Technology, NM Parikh Marg, Matunga, Mumbai, Maharashtra, India- 400 019.

Corresponding author Email: shalu.ghodke@gmail.com

DOI : https://dx.doi.org/10.12944/CRNFSJ.6.2.20

Article Publishing History

Received: 22-12-2017

Accepted: 17-05-2018

Plagiarism Check: Yes

Reviewed by: Dr. Anil Panghal (India)

Second Review by: Aamir Raina (India)

Final Approval by: Dr. Daniel Cozzolino

Article Metrics

Views  

PDF Download  PDF Downloads: 3229
Abstract:

This review deals with the significance of plant seed proteins. Plant seed proteins are known to provide various beneficial activities like antimicrobial, antihypertensive, antiviral and antioxidant. They are essential source of amino acids; act as a source of nutrition booster. Present review elaborates on extraction of proteins and hydrolysis with their advantages and disadvantages, their nutritional property, health benefits and challenges associated with the peptides.

Keywords:

Antimicrobial activity; Bioactive peptides; Protein hydrolysate; Plant seed.

Download this article as: 

Copy the following to cite this article:

Sonawane S. K, Arya S. S. Plant Seed Proteins: Chemistry, Technology and Applications. Curr Res Nutr Food Sci 2018;6(2). doi : http://dx.doi.org/10.12944/CRNFSJ.6.2.20


Copy the following to cite this URL:

Sonawane S. K, Arya S. S. Plant Seed Proteins: Chemistry, Technology and Applications. Curr Res Nutr Food Sci 2018;6(2). http://www.foodandnutritionjournal.org/?p=5464


Introduction

Plants and their products have been used for their potential nutraceutical properties. Plant proteins are considered as an economical and environmentally sustainable source of protein as compared to that of animal proteins. The needs of the people in developing country like India could be met through the plant proteins to cure protein malnutrition. The 80% of energy and 70% of protein is supplied from plant source.1 According to the studies reported by Pimentel & Pimentel, (2003), animal and fish proteins are unsustainable sources compare to that of soy, legume, canola and cereal.2 Legumes and seeds are a major portion of plant and familiar for substantially as a source of nutrition.3

A large volume of wastes and byproducts are produced in fruit industries during its processing such as making of juices, jellies and candies. This waste includes large no of seeds, peels which are generally used as animal feed. The recent trend is focused on the utilization of such wastes in making value added functional food products.4

Consumption of seeds in human diet as protein source and other bioactive constituents has been known from last two decades. There have been numerous studies and reports indicating the nutritional, functional health benefits provided by seeds in human diet,3,4,7 such as  carbohydrate content,8 antioxidant activity,9 fatty acid content10 and protein content.11

The consumer diet is nowadays more focused on functional and health benefits with balance nutrient profile instead of targeting energy providing diets12 which lead to increased intake of natural and health foods.13 Research towards exploring inexpensive plant-based protein supplements, as well as developing new food products,14 has resulted in the investigation of the potential of underutilized dicotyledonous seeds (with substantial traditional knowledge) for humans, as well as for livestock consumption.15,16

The present review deals to introduce the plant seeds as source of nutrition booster, extraction of proteins and hydrolysis, nutritional property, health benefits and challenges associated with the peptides.

Plant based sources of proteins

Seeds could be used an alternative booster of protein to overcome the protein deficiencies and to replace animal proteins which are high in cost.  The present section deals with the protein from different seeds Table 1.

Table 1: Different type of seeds with its nutritional significance

Seeds Scientific name Description Reference
Date Phoenix dactylifera L rich source of protein [17]
Belinjau seed Gnetum gnemon L. rich in protein, crude fiber, carbohydrates, total dietary fiber and encompassed with essential amino acids, fatty acids and minerals [18]
Kiwi seed Actinidia chinensis Planch. rich source of lipids, polyphenols, and crude fibers [19]
Cumin seed Cuminum cyminum antimicrobial, anti-carcinogenic and antioxidant, antidiabetic [20,21]
Watermelon seeds and Wood apple seeds Citrullus lanatus and L acidissima  large amounts of content proteins and ample amount of minerals [16]
Grape seeds Vitis vinifera L. rich in lipids, carbohydrates and proteinsessential amino acids [23,24]
Tamarind  seed Tamarindus indica L Source of essential amino acids, gums and carbohydrates [25]

 

Extraction and hydrolysis methods of proteins

Protein extraction in plants is technically interesting due to high abundance of some proteins in plant extracts which interfere with the resolution of proteins of similar molecular weight as well as protein quantization.26 Hence, this section deals with the different methods that are used during extraction of seed proteins and the factors affecting on efficacy of extraction based on different reported literature (represented in Fig 1).

Figure 1 A simplified flow chart showing methods of protein extraction (PEM) and factors affecting on protein extraction Figure 1: A simplified flow chart showing methods of protein extraction (PEM) and factors affecting on protein extraction 


Click here to View figure

 

Pure protein can extracted using alkaline extraction which is a commonly practiced to obtain a high yield.27 Different buffers like acetate-urea, SDS-buffer, NH-40 buffer phosphate and Tris- HCL buffers can also be used to enhance the extractability of protein with addition of chemical ingredients (like citric acid, cysteine hydrochloride, polyethylene glycol, and mercaptoethanol. The common activity of protease can be obstructed by high pH or high alkali extraction which causes ionization of phenolic compounds and prevents formation of hydrogen bonding with protein.28,29 To prevent protein oxidation by using reducing agent like β-mercaptoethanol; protein extraction can be enhancing using KCl, EDTA, and SDS with buffers.30,31 They are TPP (three phase partitioning) well known biosepration method is also available to extract the protein from the sources.

Protein hydrolysis method

Different hydrolysis method for hydrolysis of protein is given in Table 2.

Acid hydrolysis Alkali hydrolysis Enzymatic hydrolysis
oldest methods of hydrolysis simple and straight forward process Most acceptable method to developed bioactive peptides
Application: used as flavor enhancers Protein hydrolysates prepared by this method commercially use in food industry Bioactive peptides, supplements
Hydrolysis accomplished with sulfuric and hydrochloric acid Alkali used or alkaline pH maintain Different digestive and gastrointestinal enzymes, employed in hydrolysis [26,27, 28]
Mechanism: Formation of free amino acid or smaller peptides due to disruptions of proteins Solubility of protein enhance by heating with addition of  alkaline agents like calcium, sodium or potassium hydroxide Enzymes are very target specific cleave the peptide bond at particular amino acids
Factors for hydrolysis:·         Concentration·         Type of acid·         Temperature ranged between 120–140°C·         32–45 psi pressure·         2–8 h time of hydrolysis·          50–65% concentration of protein. Desired degree of hydrolysis at desired time by maintaining temperature within typical range that is 27–55°C can be achieved. Factors: enzyme substrate ratio, time, temperature
Disadvantage:·         uncontrolled process·         many amino acids get destroyed during the process due to high concentration of acid, for example: tryptophan, methionine, and cysteine Disadvantage·         amino acids like serine and threonine are destroyed Advantage·         controlled process·         does not require high end physiological conditions·         enzyme generally works at mild situations

 

Properties of peptide

The peptides which are hydrolyze by using acid, alkali of enzymatic method which is inactive part of the protein composed with bi, tri of poly peptides chain possess various properties. The human body endangered to stress and exposure to toxic materials interrupting normal functions of body leading to various health conditions. Physiological homeostasis or health-promoting agents have potential to control these abnormalities. Consumes  are looking for more healthy, nutritional oppositionists derived from  natural sources falls under the category of functional foods and nutraceuticals have arisen as alternative to chemotherapy to protect from diseases.34

Protein is well known constituent and key for building blocks of human body. Raw food proteins force their action in their original form or on the hydrolysis both in vivo and in vitro. After hydrolyzed proteins get into small fractions and amino acids to get absorb into body by digestive track enzymes. These dietary peptides possess beneficial pharmacological properties35 which are recognized as bioactive peptides. The activities shown by peptides depicted in Fig 2.

Fig 2. Various activities shown by peptides Figure 2: Various activities shown by peptides

Click here to View figure

 

Antimicrobial activity

Peptides which show activity against the microorganisms are known as antimicrobial peptides. One group of peptides acts on cytoplasmic membrane whereas another group performed neutral role the cytoplasmic membrane of the target microorganism.36,37 Antimicrobial peptides are recognized by their influence on microorganism targeted to cytoplasmic membrane.36 The magnetism between the peptide and the target cell created due to electrostatic binding which may be twisted due to cationic peptide and negatively charged outer cell membrane.37

In this, electrostatic interaction removes Mg2+, Ca2+ (divalent cations) from surface. The smooth entry of the peptide and subsequent peptide connection with the cytoplasmic membrane due to disruption of cell outer membrane and report auto-promoted uptake.36 The cytoplasmic membrane creates an arrangement of the peptide to act on target cell and permeabilizes cytoplasmic membrane and/or translocate through it.

Factors such as electrostatic interactions, hydrophobicity and flexibility of peptide have influence on antimicrobial activity. Foeniculum vulgare, Cucumis sativus, Ammi majus, Allium ascolinicum, Cichorium intybus and Rumex vesicarius plant seeds have shown an antimicrobial activity against Staphylococcus aureus (ATCC 25923), Escherichia coli (ATCC 25922), Pseudomonas aeruginosa (ATCC 27853) and Proteus vulgaris (ATCC 6380).38 The excellent antimicrobial activity from Cucurbita moschata and Lagenaria siceraria seed proteins hydrolyaste against gram negative bacteria A. baumannii were reported by Dash & Ghosh, (2017).34

Song, Wei, Zhang, (2012) ascertained that the improvement in the hydrophobicity helps to initiate hydrophobic reaction between lipid acyl chains in bacterial membrane one of the crucial parameter to enhance the membrane permeabilization of bacteria. The amino acids like cysteine, histidine, proline, tyrosine, glycine, arginine, lysine and serine are accountable for antimicrobial property.41 According Song, Wei, Zhang, (2012),  if peptide contain major amino acids like lysine and arginine which are responsible for interaction with bacterial membrane.

Antifungal activity

Plant antifungal proteins act as shield against fungal invasion and organized into different groups. This groups include thaumatin-like proteins, lectins, cyclophilin-like proteins, lipid transfer proteins, ribonucleases, storage 2S albumins, ribosome-inactivating proteins and many mores.42,44 Different mechanism of action for this protein observed with degradation of  fungal cell wall polymer, formation of  pore, inhibition of DNA synthesis.45 An antifungal protein with 14.3 kDa extracted from the seeds of butterfly pea (Clitoria ternatea) showed lytic activity and fungicidal activity.46 Bard et al., (2014) segregated peptides from Capsicum baccatum seeds which exhibited inhibitory effects against α-amylase and antimicrobial activity.42

Sm-AMP-X (33 residues) was isolated from chickweed (Stellaria media) seeds. This shows high activity against fungal phytopathogens and discovered as a novel antifungal peptide [48]. Actually this is consist of helix-loop-helix fold which stabilized by two disulfide bridges C1–C4 and C2–C3 .48

Antiviral activity

There are two ways to prevent viral infection. In first it can be blocked viral entry through interaction with the virus and another way is to obstruct virus entry through interaction with the host cell. The cationic peptides have potential to effectively inhibit viral infections. Peptides react with viral receptors by blocking the virus and prevent binding intra-cellularly.37 Protein microbicides composed with antiviral lectins and antibodies which aid in blocking human immunodeficiency virus (HIV).45 He observed antiviral lectin griffithsin (GRFT) in the endosperm of transgenic rice plants (Oryza sativa) which exhibit persuasive neutralizing activity against HIV.50 The GRFT isolated from Griffithsia spp. having MW of 12.7 kDa lectin which impedes HIV-1 by binding with mannose-rich glycans on the virus envelope glycoproteins.51 The antiviral activity of GRFT against severe acute respiratory syndrome-associated coronavirus (SARS-CoV) and other coronaviruses,52,53 hepatitis C virus,54,55 Japanese encephalitis virus56 and herpes simplex virus 57 was validated.

Antihypertensive activity

Blood pressure is risk factor in developing cardiovascular diseases which causes due to the Angiotensin II. These occur due to the deliverance of rennin from kidney which break downs the circulating angiotensinogen. Angiotensin I (decapeptide) is formed by the conversion of angiotensinogen which may cleave to the octapeptide (angiotensin II). This activity performed in the existence of angiotensin converting enzyme (ACE) which originates arterial constriction and elevation in blood pressure. Peptides produce by hydrolysis of lupin seed protein with pepsin able to inhibit the angiotensin-converting enzyme.58  Peptides from canary seed prolamins showed an antihypertensive activity and reported as an accessible and cheap source to encourage better human health.54

Antioxidant activity

Protein hydrolysates composed of 2–20 amino acids or peptides longer than 20 amino acid residues showed bioactivity.60 Recently, the scrutiny of novel functional food from vegetable proteins is a valuable source of protein to enrich food use.61 Savadkoohi and Farahnaky (2012) reported that tomato seed proteins has nutraceutical properties.62 Ziziphus jujbee, C. Lantus and L. accidama protein hydrolyaste shows antioxidant activity.58,59,60,61

Applications of peptides

Due to increased consumer awareness regarding use of natural preservatives; there is demand of healthy natural food additives derived from natural sources like plant seeds.  Therefore, peptides derived from the plant seeds are in demand due to their antimicrobial property and having voluminous applications as in devices used in biomedical and food processing. The creation of antimicrobial packaging by fusing peptides into materials has an essential role in safety and quality of food. This employed to stretch food shelf life and to shrink growth of bacteria on the surface of product.63,64

Many researchers enhanced the nutritional values of foods by employing protein hydrolysate from different plant sources like soybean, rice endosperm, and rice bran which may have their low costs and safety.65–68 Akin & Ozcan, (2017), developed new healthy dairy fermented milk drinks (non-fat) using plant protein. This was formulated by using wheat gluten, soy protein isolate, rice protein, and pea protein isolate which improved the physico-chemical, nutritional and sensory properties.

From the industry point of view, the application of protein hydrolyzes are limited due to bitter taste which overcome using different approaches. Hydrolysis of bitter peptides with aminopeptidase, alkaline/neutral protease and carboxypeptidase is one of the approaches with having disadvantage that hydrolyze the previously generated bioactive peptides. The masking additives like using monosodium glutamate, addition of cyclodextrins and encapsulation, could be preferably used to remove bitterness from the peptides.

Conclusion

From the above literature it can be concluded that plant seeds could be an alternative source of protein for replacement of animal protein that has associated with many health benefits. There is need to elaborate the research in plant seed protein to find health benefits and meet the demand of protein of growing population.

References

  1. Panghal, A., Khatkar, B.S. and Singh U. Cereal proteins and their role in food industry. Indian Food Ind. 2006;25:58.
  2. Pimentel D, Pimentel M. Sustainability of meat-based and plant-based diets and the environment. Am. J. Clin. Nutr. 2003. doi:10.1177/0956247808089156.
    CrossRef
  3. Khursheed, S., Raina, A., Khan S. Improvement of yield and mineral content in two cultivars of Vicia faba L. through physical and chemical mutagenesis and their character association analysis. Arch Curr Res Int. 2016;4:1–7.
    CrossRef
  4. El-adawy TA, Taha KM. Characteristics and Composition of Watermelon , Pumpkin , and 2001.
  5. Al-Jassir MS. Chemical composition and microflora of black cumin (Nigella sativa L.) seeds growing in Saudi Arabia. Food Chem. 1992. doi:10.1016/0308-8146(92)90153-S.
    CrossRef
  6. Barampama Z, Simard RE. Nutrient composition, protein quality and antinutritional factors of some varieties of dry beans (Phaseolus vulgaris) grown in Burundi. Food Chem. 1993. doi:10.1016/0308-8146(93)90238-B.
    CrossRef
  7. Raina, A., Laskar, R.A., Khursheed, S., Khan, S., Parveen, K., Amin, R., Khan S. Induce physical and chemical mutagenesis for improvement of yield attributing traits and their correlation analysis in chickpea. Int Lett Sci. 2017;61:14–22.
  8. Tavares MIB, Bathista ALBS, Silva EO, Filho NP, Nogueira JS. A molecular dynamic study of the starch obtained from the Mangifera indica Cv. Bourbon and Espada seeds by 13C solid state NMR. Carbohydr Polym. 2003. doi:10.1016/S0144-8617(03)00049-3.
    CrossRef
  9. Wang W, Bostic TR, Gu L. Antioxidant capacities, procyanidins and pigments in avocados of different strains and cultivars. Food Chem. 2010. doi:10.1016/j.foodchem.2010.03.114.
    CrossRef
  10. Ennouri M, Evelyne B, Laurence M, Hamadi A. Fatty acid composition and rheological behaviour of prickly pear seed oils. Food Chem. 2005. doi:10.1016/j.foodchem.2004.10.020.
    CrossRef
  11. Sogi DS, Arora MS, Garg SK, Bawa AS. Fractionation and electrophoresis of tomato waste seed proteins. Food Chem. 2002. doi:10.1016/S0308-8146(01)00304-1.
    CrossRef
  12. Panghal A, Janghu S, Virkar K, Gat Y, Kumar V, Chhikara N. Potential non-dairy probiotic products – A healthy approach. Food Biosci. 2018. doi:10.1016/j.fbio.2017.12.003.
    CrossRef
  13. Panghal, A., N. Dhull KBN. Whey Based Strawberry Ready to Serve (RTS) Beverage. Beverage Food World. 2009;36:28–30.
  14. Panghal A, Kumar V, Dhull SB, Gat Y, Chhikara N. Utilization of dairy industry waste-whey in formulation of papaya RTS beverage. Curr Res Nutr Food Sci. 2017. doi:10.12944/CRNFSJ.5.2.14.
    CrossRef
  15. Bhat R, Sridhar KR, Tomita-Yokotani K. Effect of ionizing radiation on antinutritional features of velvet bean seeds (Mucuna pruriens). Food Chem. 2007. doi:10.1016/j.foodchem.2006.09.037.
    CrossRef
  16. Bhat R. The Disease – Preventive Potential of Some Popular and Underutilized Seeds. Funct. Foods, Nutraceuticals, Degener. Dis. Prev., 2011. doi:10.1002/9780470960844.ch7.
    CrossRef
  17. Ali A, Waly M, Essa MM, Devarajan S. Nutritional and Medicinal Value of Date Fruit. Dates Prod Process Food Med Values. 2014.
  18. Bhat R, Yahya N. Evaluating belinjau ( Gnetum gnemon L .) seed flour quality as a base for development of novel food products and food formulations. FOOD Chem. 2014;156:42–9. doi:10.1016/j.foodchem.2014.01.063.
    CrossRef
  19. Schieber A, Stintzing FC, Carle R. By-products of plant food processing as a source of functional compounds – Recent developments. Trends Food Sci Technol. 2001. doi:10.1016/S0924-2244(02)00012-2.
    CrossRef
  20. Allahghadri T, Rasooli I, Owlia P, Nadooshan MJ, Ghazanfari T, Taghizadeh M, et al. Antimicrobial Property, Antioxidant Capacity, and Cytotoxicity of Essential Oil from Cumin Produced in Iran. J Food Sci. 2010. doi:10.1111/j.1750-3841.2009.01467.x.
    CrossRef
  21. Dhandapani S, Subramanian VR, Rajagopal S, Namasivayam N. Hypolipidemic effect of Cuminum cyminum L. on alloxan-induced diabetic rats. Pharmacol Res. 2002. doi:10.1016/S1043-6618(02)00131-7.
    CrossRef
  22. Sonawane, SK; Bagul MB; Guy LeBlanc JAS. Nutritional, functional, thermal and structural characteristics of Citrullus lanatus and Limonia acidissima seed flours. J Food Meas Charact 2016;10:72–79.
    CrossRef
  23. Pesavento IC, Bertazzo A, Flamini R, Vedova AD, De Rosso M, Seraglia R, et al. Differentiation of Vitis vinifera varieties by MALDI-MS analysis of the grape seed proteins. J Mass Spectrom 2008. doi:10.1002/jms.1295.
    CrossRef
  24. Zhou T, Li Q, Zhang J, Bai Y, Zhao G. Purification and characterization of a new 11S globulin-like protein from grape (Vitis vinifera L.) seeds. Eur Food Res Technol. 2010. doi:10.1007/s00217-009-1211-0.
    CrossRef
  25. Bagul M, Sonawane SK, Arya SS. TARs. 2015;34.
  26. Mehraj SS, Kamili AN, Nazir R, Haq E, Balkhi HM. Comparative evaluation of extraction methods for total proteins from Crocus sativus L. (Saffron). Saudi J Biol Sci. 2016. doi:10.1016/j.sjbs.2016.04.011.
    CrossRef
  27. Horax R, Hettiarachchy N, Kannan A, Chen P. Protein extraction optimisation, characterisation, and functionalities of protein isolate from bitter melon (Momordica charantia) seed. Food Chem. 2011. doi:10.1016/j.foodchem.2010.06.068.
    CrossRef
  28. Loomis WD, Battaile J. Plant phenolic compounds and the isolation of plant enzymes. Phytochemistry. 1966. doi:10.1016/S0031-9422(00)82157-3.
    CrossRef
  29. Hochstrasser DF, Harrington MG, Hochstrasser AC, Miller MJ, Merril CR. Methods for increasing the resolution of two-dimensional protein electrophoresis. Anal Biochem. 1988. doi:10.1016/0003-2697(88)90209-6.
    CrossRef
  30. Carpentier SC, Witters E, Laukens K, Deckers P, Swennen R, Panis B. Preparation of protein extracts from recalcitrant plant tissues: An evaluation of different methods for two-dimensional gel electrophoresis analysis. Proteomics. 2005. doi:10.1002/pmic.200401222.
    CrossRef
  31. Wang W, Scali M, Vignani R, Spadafora A, Sensi E, Mazzuca S, et al. Protein extraction for two-dimensional electrophoresis from olive leaf, a plant tissue containing high levels of interfering compounds. Electrophoresis. 2003. doi:10.1002/elps.200305500.
    CrossRef
  32. Gobbetti M, Minervini F, Rizzello CG. Angiotensin I-converting-enzyme-inhibitory and antimicrobial bioactive peptides. Int. J. Dairy Technol., 2004. doi:10.1111/j.1471-0307.2004.00139.x.
    CrossRef
  33. FitzGerald RJ, Murray B a, Walsh DJ. Hypotensive peptides from milk proteins. J Nutr. 2004. doi:10.1002/2014GB005021.
    CrossRef
  34. Kris-Etherton PM, Keen CL. Evidence that the antioxidant flavonoids in tea and cocoa are beneficial for cardiovascular health. Curr Opin Lipidol. 2002. doi:10.1097/00041433-200202000-00007.
    CrossRef
  35. Hartmann R, Meisel H. Food-derived peptides with biological activity: from research to food applications. Curr Opin Biotechnol. 2007. doi:10.1016/j.copbio.2007.01.013.
    CrossRef
  36. Powers JPS, Hancock REW. The relationship between peptide structure and antibacterial activity. Peptides. 2003. doi:10.1016/j.peptides.2003.08.023.
    CrossRef
  37. Jenssen H, Hamill P, Hancock REW. Peptide antimicrobial agents. Clin Microbiol Rev. 2006. doi:10.1128/CMR.00056-05.
    CrossRef
  38. Al Akeel R, Al-Sheikh Y, Mateen A, Syed R, Janardhan K, Gupta VC. Evaluation of antibacterial activity of crude protein extracts from seeds of six different medical plants against standard bacterial strains. Saudi J Biol Sci. 2014. doi:10.1016/j.sjbs.2013.09.003.
    CrossRef
  39. Dash P, Ghosh G. Fractionation , amino acid profiles , antimicrobial and free radical scavenging activities of Citrullus lanatus seed protein. Nat Prod Res. 2017;6419:0. doi:10.1080/14786419.2017.1305385.
    CrossRef
  40. Song R, Wei R, Zhang B WD. Optimization of the antibacterial activity of half-fin anchovy (Setipinna taty) hydrolysates. Food Bioprocess Technol. 2012;5:1979–1989.
    CrossRef
  41. Hegedüs N, Marx F. Antifungal proteins: More than antimicrobials? Fungal Biol Rev 2013. doi:10.1016/j.fbr.2012.07.002.
    CrossRef
  42. Kondori N, Baltzer L, Dolphin GT, Mattsby-Baltzer I. Fungicidal activity of human lactoferrin-derived peptides based on the antimicrobial ???? region. Int. J. Antimicrob. Agents. 2011. doi:10.1016/j.ijantimicag.2010.08.020.
    CrossRef
  43. Ho VSM, Wong JH, Ng TB. A thaumatin-like antifungal protein from the emperor banana. Peptides. 2007. doi:10.1016/j.peptides.2007.01.005.
    CrossRef
  44. Wong JH, Ng TB, Cheung RCF, Ye XJ, Wang HX, Lam SK, et al. Proteins with antifungal properties and other medicinal applications from plants and mushrooms. Appl Microbiol Biotechnol. 2010. doi:10.1007/s00253-010-2690-4.
    CrossRef
  45. Selitrennikoff CP. Antifungal Proteins. Appl Environ Microbiol. 2001. doi:10.1128/AEM.67.7.2883-2894.2001.
    CrossRef
  46. Ajesh K, Sreejith K. A novel antifungal protein with lysozyme-like activity from seeds of Clitoria ternatea. Appl Biochem Biotechnol. 2014. doi:10.1007/s12010-014-0880-8.
    CrossRef
  47. Bard GCV, Nascimento V V., Oliveira AEA, Rodrigues R, Da Cunha M, Dias GB, et al. Vicilin-like peptides from Capsicum baccatum L. seeds are ??-amylase inhibitors and exhibit antifungal activity against important yeasts in medical mycology. Biopolym – Pept Sci Sect. 2014. doi:10.1002/bip.22504.
    CrossRef
  48. Slavokhotova AA, Rogozhin EA, Musolyamov AK, Andreev YA, Oparin PB, Berkut AA, et al. Novel antifungal alpha-hairpinin peptide from Stellaria media seeds: structure, biosynthesis, gene structure and evolution. Plant Mol Biol. 2014. doi:10.1007/s11103-013-0127-z.
    CrossRef
  49. Vamvaka E, Arcalis E, Ramessar K, Evans A, O’Keefe BR, Shattock RJ, et al. Rice endosperm is cost-effective for the production of recombinant griffithsin with potent activity against HIV. Plant Biotechnol J. 2016. doi:10.1111/pbi.12507.
    CrossRef
  50. Mori T, O’Keefe BR, Sowder RC, Bringans S, Gardella R, Berg S, et al. Isolation and characterization of Griffithsin, a novel HIV-inactivating protein, from the red alga Griffithsia sp. J Biol Chem. 2005. doi:10.1074/jbc.M411122200.
    CrossRef
  51. Balzarini J. Targeting the glycans of gp120: A novel approach aimed at the Achilles heel of HIV. Lancet Infect Dis. 2005. doi:10.1016/S1473-3099(05)70271-1.
    CrossRef
  52. O’Keefe BR, Giomarelli B, Barnard DL, Shenoy SR, Chan PKS, McMahon JB, et al. Broad-Spectrum In Vitro Activity and In Vivo Efficacy of the Antiviral Protein Griffithsin against Emerging Viruses of the Family Coronaviridae. J Virol. 2010. doi:10.1128/JVI.02322-09.
    CrossRef
  53. Ziółkowska NE, O’Keefe BR, Mori T, Zhu C, Giomarelli B, Vojdani F, et al. Domain-Swapped Structure of the Potent Antiviral Protein Griffithsin and Its Mode of Carbohydrate Binding. Structure. 2006. doi:10.1016/j.str.2006.05.017.
    CrossRef
  54. Meuleman P, Albecka A, Belouzard S, Vercauteren K, Verhoye L, Wychowski C, et al. Griffithsin has antiviral activity against hepatitis C virus. Antimicrob Agents Chemother. 2011. doi:10.1128/AAC.00633-11.
    CrossRef
  55. Takebe Y, Saucedo CJ, Lund G, Uenishi R, Hase S, Tsuchiura T, et al. Antiviral Lectins from Red and Blue-Green Algae Show Potent In Vitro and In Vivo Activity against Hepatitis C Virus. PLoS One. 2013. doi:10.1371/journal.pone.0064449.
    CrossRef
  56. Ishag HZ a, Li C, Huang L, Sun M-X, Wang F, Ni B, et al. Griffithsin inhibits Japanese encephalitis virus infection in vitro and in vivo. Arch Virol. 2012. doi:10.1007/s00705-012-1489-2.
    CrossRef
  57. Nixon B, Stefanidou M, Mesquita PMM, Fakioglu E, Segarra T, Rohan L, et al. Griffithsin Protects Mice from Genital Herpes by Preventing Cell-to-Cell Spread. J Virol. 2013. doi:10.1128/JVI.00012-13.
    CrossRef
  58. Boschin G, Scigliuolo GM, Resta D, Arnoldi A. Optimization of the Enzymatic Hydrolysis of Lupin ( Lupinus ) Proteins for Producing ACE-Inhibitory Peptides. 2014.
  59. Valverde ME, Orona-Tamayo D, Nieto-Rend??n B, Paredes-L??pez O. Antioxidant and Antihypertensive Potential of Protein Fractions from Flour and Milk Substitutes from Canary Seeds (Phalaris canariensis L.). Plant Foods Hum Nutr. 2017. doi:10.1007/s11130-016-0584-z.
    CrossRef
  60. Capriotti AL, Caruso G, Cavaliere C, Samperi R, Ventura S, Zenezini Chiozzi R, et al. Identification of potential bioactive peptides generated by simulated gastrointestinal digestion of soybean seeds and soy milk proteins. J Food Compos Anal. 2015. doi:10.1016/j.jfca.2015.08.007.
    CrossRef
  61. Ruiz, G.A., Arts, A., Minor, M., Schutyser M. A hybrid dry and aqueous fractionation method to obtain protein-rich fractions from quinoa (Chenopodium quinoa Willd). Food Bioprocess Technol. 2016;9:1502–1510.
    CrossRef
  62. Savadkoohi S, Farahnaky A. Dynamic rheological and thermal study of the heat-induced gelation of tomato-seed proteins. J Food Eng. 2012. doi:10.1016/j.jfoodeng.2012.06.010.
    CrossRef
  63. Appendini P, Hotchkiss JH. Review of antimicrobial food packaging. Innov Food Sci Emerg Technol. 2002. doi:10.1016/S1466-8564(02)00012-7.
    CrossRef
  64. Soares N de FF, Pires ACS, Camilloto GP, Santiago-Silva P, Espitia PJP, Silva W a. Recent patents on active packaging for food application. Recent Pat Food Nutr Agric. 2009. doi:10.2174/2212798410901020171.
    CrossRef
  65. Shih FF, Daigle KW. Preparation and characterization of rice protein isolates. J Am Oil Chem Soc. 2000. doi:10.1007/s11746-000-0141-2.
    CrossRef
  66. Adebiyi AP, Adebiyi AO, Yamashita J, Ogawa T, Muramoto K. Purification and characterization of antioxidative peptides derived from rice bran protein hydrolysates. Eur Food Res Technol. 2009. doi:10.1007/s00217-008-0962-3.
    CrossRef
  67. Elias RJ, Kellerby SS, Decker EA. Antioxidant Activity of Proteins and Peptides. Crit Rev Food Sci Nutr. 2008.
  68. Li Y, Jiang B, Zhang T, Mu W, Liu J. Antioxidant and free radical-scavenging activities of chickpea protein hydrolysate (CPH). Food Chem. 2008;106:444–50. doi:10.1016/j.foodchem.2007.04.067.
    CrossRef
  69. Akin Z, Ozcan T. Functional properties of fermented milk produced with plant proteins. LWT – Food Sci Technol. 2017. doi:10.1016/j.lwt.2017.07.025.
    CrossRef


Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.