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See also: Protein methods

Protein detection is used for clinical diagnosis, treatment and biological research.[1] Protein detection evaluates the concentration and amount of different proteins in a particular specimen.[2] There are different methods and techniques to detect protein in different organisms. Protein detection has demonstrated important implications for clinical diagnosis, treatment and biological research.[3] Protein detection technique has been utilized to discover soybean protein in processed foods because amount of consumers from soybean protein allergy have showed a increase trend in the last a number of years.[4]

Protein Detection in Soybeans, Walnuts, Beef

Detection of Functional Modes in Protein
Main articles: Soybean and Walnut

Purpose for protein detection in food

Soybean Plant

Allergies from food have been noted to become common illness nowadays. The food allergies in the clinical demonstration present different signs, for example mild symptoms from itching in the mouth and swelling of the lips to critical anaphylactic response result in deadly consequences.[5] According to statistic, about 2% adults and 8% children are experiencing hypersensitivity from industrialized countries. In order to reduce potential threatening reactions for life, avoiding the consumption from these allergenic foods strictly is  the valid therapy. Therefore, sufficient description in term of potentially allergenic ingredients existing in food products is crucial and indispensable which can be monitored through protein detection.[6] Soybean allergy has showed to be one common food allergy in the world, thus protein detection in soybeans has illustrated that it is important and necessary.[7]

Rationale for protein detection in soybeans

During the last 30 years, broad methods and techniques were experimented to discover soybean protein. These methods and techniques can be conveyed to lab environment easily.[8] The original and traditional methods were designed and tested in molecular biology spectrum. The soybean has been consumed in processed foods all over the word because of its high nutrient and easy processing characteristic such as soybean milk, tofu, meat alternatives, and brewed soybean products.[5] microorganisms is used in brewage process for brewed soybean products like miso, soy sauce, natto and tempeh. Allergenicity stays in brewed soybean products. In Asian countries, these foods are popular and traditional. The amount of patients from soybean allergy and the nearly infinite uses for soybean have gone up in the past a couple of years. The labeling for soybean protein declaimed by protein detection has indicated to be the most important solution.[9] Detailed labeling description for the soybean ingredients in refined foods is required to protect the consumer.[9]

Previous method for protein detection in soybeans

Enzyme‐Linked Immunosorbent Assay technique containing high susceptibility and specificity is reliable method to investigate soybean proteins through applying a protein which can identify a foreign molecule. This has been evaluated as a vacuolar protein including a molecular block of 34 kDa. The ELISA illustrated sufficient repeatability and reproducibility in lab assessment. But it can not test protein in soybean existing in brewed soybean products.[10] There are different studies to conduct experiments to assess soybean protein through ELISA. However, reproducibility, cross-reactivity and low repeatability make measurement difficult to be reliable in processed foods. These methods can not discover soybean protein staying in brewed soybean products.[11]

Current method for protein detection in soybeans

Compared with previous method, a heating process is involved in current abstraction technique to investigate soybean protein existing in brewed products. Since the heating process can deactivate the microbial proteolytic enzymes, the current abstraction technique can be used to disclose soybean protein in brewed soybean products.[12] The heating abstraction technique can be demonstrated as the following. To produce the good dispersibility for the specimen in the extraction buffer to carry out the heating process, 19mL of abstraction buffer is mixed with five glass beads in five millimeter diameter and 1 g of food homogenate. At 5, 15 and 60 min variable time, the mixture is abstracted under 25, 40, 60, 80 and 100 ° variable temperature through the heating in a water bath followed by every 5 min vortexing. Food abstractions generated through the previous and the current technique are centrifuged for 20 min at three thousand gram, then the supernatant is filtered off by a filter paper. The filtrate is gathered and applied for analysis immediately acting as the food specimen abstract.[13] The calibration standard solutions needs to be prepared to disclose soybean proteins by using ELISA.  A three hundred milligram soybean powder specimen is mixed with a twenty milliliter compound including 0.5 M NaCl, 0.5% SDS, 20 mM Tris-HCl (pH 7.5), and 2% 2-ME. The compound is then shaken at room temperature for 16 h for abstraction. The abstract is centrifuged for 30 min at twenty thousand gram, then the supernatant is selected by a 0.8-μm microfilter paper. The protein substance from the initial abstract is inspected with a 2-D Quant Kit. The initial abstract is diluted to 50 ng/mL combined with 0.1% SDS, 0.1% 2-ME, 0.1 M PBS (pH 7.4), 0.1% BSA, and 0.1% Tween 20, and it is deposited for ELISA at 4 °C playing as the calibration standard solution.[14]

Conclusion for current protein detection method in soybeans.

The detection limit for the ELISA is 1 μg/g and it can not assess soybean proteins existing in brewed soybean products due to degradation of the proteins in soybean through microbial proteolytic enzymes staying in the brewed products. The microbial proteolytic enzymes possibly restrain the detection of soybean protein storing in the brewed soybean products. The current abstraction technique can control protein degradation through the microbial proteolytic enzymes. The microbial proteolytic enzymes can be inhibited by heating, pH, and protease inhibitors in general.[15] The variable heating temperatures and abstraction times are examined to decide the ideal heating temperature and time to control microbial proteolytic enzymes. The heating conditions showed to optimize the control of microbial proteolytic enzymes is 80 °C for 15 min. So the heating temperature for the abstraction is set to 80 °C and the time is set to 15 min for the current abstraction technique.[16]

In conclusion, the current abstraction technique can restrain the degradation of soybean proteins through microbial proteolytic enzymes and can detect soybean proteins staying in most brewed soybean products. The current abstraction technique combined with the heating is a useful and sensitive tool to discover soybean protein stored in processed foods and brewed soybean products. Without impacting microbial proteolytic enzymes, this method is appropriate to quantify soybean protein existing in processed foods. The proposed extraction and ELISA technique can be applied to control labeling systems through a trusty manner.[9]

Black Walnut
English Walnut

Rationale for protein detection in walnuts

English walnuts (Juglans regia) and black walnuts (Juglans nigra) are two main types of walnuts in the market across the world. Walnuts are utilized as a valuable ingredient due to favorable health attributes, sensory properties and consumer sensation.[17][18] Shelled walnuts are broadly applied as ingredients in different foods such as salad, ice creams, bread and meat alternate. Walnut oil is introduced as a good source of mono- and polyunsaturated fatty acids and tocopherols.[19] And it is adopted as a food ingredient in salad dressings particularly. Walnut hull extract is considered as a dietary supplement and a seasoning in the food industry. In addition, ground walnut shells can be used in industrial field as extenders, carriers, fillers and abrasives for example jet cleaners. Tree nuts are regarded as one of the most common allergenic foods around the world.[20]  Allergic reactions from tree nuts can be fierce and life threatening.[21][22] Individuals with walnut allergies can have result in fatal and near-fatal reactions from the unintended ingestion of walnuts, other tree nuts or possibly contamination of food with the walnuts ingredient.[23][24][25][26][27][28][29][30][31][32] To prevent walnut allergic reactions, the only effective way is to avoid walnuts in the diet.[33] The appropriate labeling of processed foods with walnuts ingredient is critical to protect walnut-allergic consumers. There are a couple of circumstances cause undeclared walnut residues such as sharing equipment between walnut-containing and other formulations and undeclared walnuts in ingredients.[34] The enzyme-linked immunosorbent assay (ELISA) can be used as the technique to detect walnuts residues with great sensitivity and specificity since walnuts allergic Individuals can have allergic reactions with low (milligram) amounts of walnuts.[35] Several different techniques can be applied to discover walnut residues as well such as polymerase chain reaction (PCR) methods and ELISA method on the basis of polyclonal antisera raised against a particular 2S albumin walnut protein.[36][37][38]

Current method for protein detection in walnuts

The sandwich-type walnut ELISA is the current method used to detect protein in walnuts.

Immunogen preparation

A mixture of several brands of English walnuts are used to produce the immunogen. The mixed walnuts need to be washed by deionized distilled water 6 times and air-dried. Portion of the walnuts are dry-roasted for 10 minutes at 270 ◦F. The roasted or raw walnuts are cleaved, frozen, and ground to a refined particle size through the blender. The ground roasted and ground raw walnuts are defatted and filtered. Then, the powdered raw or roasted walnuts are air-dried thoroughly. Both the defatted, powdered raw, and roasted walnuts can be utilized as immunogens. Protein concentrations of the defatted powdered immunogens are set through the Kjeldahl method with 46.4% raw defatted walnut and 34.9% roasted defatted walnut.

Polyclonal antibody production and titer determination

Polyclonal antibodies are generated in 1 sheep, 1 goat, and 3 New Zealand white rabbits with each immunogen. The initial subcutaneous injections are given to the 10 animals including 3 rabbits, 1 sheep, and 1 goat on multiple sites with the defatted powdered immunogen and Freunds Complete Adjuvant. Titer values of collected antisera are evaluated by a noncompetitive ELISA method with walnut protein from abstracts of the proper raw or roasted immunogen.  

Cross-reactivity study and ELISA method

A variety of tree nuts, seeds, legumes, fruits and food ingredients are assessed for cross-reactivity in the walnut ELISA assay. The modified sandwich ELISA can be used to detect walnuts residues with sheep antiroasted walnut and rabbit antiroasted walnut antisera used as the capture and detector antibodies respectively.  

Conclusion for current protein detection method in walnuts

The sandwich-type walnut ELISA can be applied as a critical analytical technique by food manufacturers and regulatory agencies for hygiene validation and the assessment of allergen control strategies. Walnut residues can be disclosed at 1 ppm quantitation limit in a diversity of food such as ice cream, muffins, cookies and chocolate. The walnut ELISA can be conducted to detect possible walnut residues allergy in other foods from sharing equipment and to evaluate the sanitation procedures targeted on removal of walnut residues from shared equipment in the food industry.

Cattle

Rationale for protein detection in processed animal protein in feedingstuffs for cattle

It has been reported that animal feedingstuffs containing processed animal protein (PAP) contaminated with prions have caused BSE infection of the cattle. Processed animal proteins (PAP) has been prohibited to apply as feed material for all farmed animals except fish meal currently. The specific polymerase chain reaction (PCR) based procedure parallelled with microscopic method is utilized to detect processed animal protein (PAP) in feedingstuffs.

The limit detection for PCR has been evaluated on 0.05% for beef, 0.1% for pork and 0.2% for poultry meat and bone meal. Microscopic method can disclose 66.13% doubtful samples of feedingstuffs. Combined the results from the use of the microscopic and PCR methods, it has been stated that the molecular biology methods can be executed as a supplementary method for PAP detection

Implication from protein detection

Further information: Protein microarray

Protein detection in cells from the human rectal mucous membrane can imply colorectal disease such as colon tumours, inflammatory bowel disease.[39] Protein detection based on antibody microarrays can implicate life signature for example organics and biochemical compounds in the solar system in astrobiology field.[40] Protein detection can monitor soybean protein labeling system in processed foods to protect consumers in a reliable way.[9]

Reference

  1. ^ Engineering the bioelectronic interface : applications to analyte biosensing and protein detection. Davis, Jason J., Royal Society of Chemistry (Great Britain). Cambridge, UK: RSC Pub. 2009. ISBN 9781615836932. OCLC 701819884.{{cite book}}: CS1 maint: others (link)
  2. ^ "Protein Detection", Electrophoresis in Practice, Wiley-VCH Verlag GmbH & Co. KGaA, pp. 131–164, 2016-02-26, doi:10.1002/9783527695188.ch6, ISBN 9783527695188, retrieved 2019-05-17
  3. ^ Zhang, Hongquan; Li, Feng; Dever, Brittany; Wang, Chuan; Li, Xing-Fang; Le, X. Chris (2013-10-04). "Assembling DNA through Affinity Binding to Achieve Ultrasensitive Protein Detection". Angewandte Chemie International Edition. 52 (41): 10698–10705. doi:10.1002/anie.201210022.
  4. ^ Liu, Bin; Teng, Da; Wang, Xiumin; Wang, Jianhua (2013-01-30). "Detection of the Soybean Allergenic Protein Gly m Bd 28K by an Indirect Enzyme-Linked Immunosorbent Assay". Journal of Agricultural and Food Chemistry. 61 (4): 822–828. doi:10.1021/jf303076w. ISSN 0021-8561.
  5. ^ a b Wang, Xiaoyu; Jiang, Xiaofeng; Zhu, Shuxian; Liu, Lu; Xia, Junhan; Li, Lidong (2017). "Preparation of optical functional composite films and their application in protein detection". Colloids and Surfaces A: Physicochemical and Engineering Aspects. 535: 69–74. doi:10.1016/j.colsurfa.2017.09.026.
  6. ^ Cheng, Lin; Zhang, Jie; Lin, Yan; Wang, Qiong; Zhang, XiuXiu; Ding, YanHua; Cui, Hanfeng; Fan, Hao (2015). "An electrochemical molecular recognition-based aptasensor for multiple protein detection". Analytical Biochemistry. 491: 31–36. doi:10.1016/j.ab.2015.08.023.
  7. ^ Shimojo, Naoshi; Nakamura, Masashi; Sato, Nayu; Sano, Akiyo; Kobayashi, Tsukane; Yagami, Akiko; Kojima, Atsushi; Matsunaga, Kayoko (2016). "Utility of Immunoproteomics in Soybean Allergy". Journal of Allergy and Clinical Immunology. 137 (2): AB139. doi:10.1016/j.jaci.2015.12.587.
  8. ^ Protein blotting and detection : methods and protocols. Kurien, Biji T., Scofield, R. Hal. New York: Humana Press. 2009. ISBN 9781597455428. OCLC 371501294.{{cite book}}: CS1 maint: others (link)
  9. ^ a b c d Morishita, Naoki; Matsumoto, Takashi; Morimatsu, Fumiki; Toyoda, Masatake (2014). "Detection of Soybean Proteins in Fermented Soybean Products by Using Heating Extraction: Detection of soybean in fermented food…". Journal of Food Science. 79 (5): T1049 – T1054. doi:10.1111/1750-3841.12461.
  10. ^ Morales-Narváez, Eden; Guix, Maria; Medina-Sánchez, Mariana; Mayorga-Martinez, Carmen C.; Merkoçi, Arben (2014). "Micromotor Enhanced Microarray Technology for Protein Detection". Small. 10 (13): 2542–2548. doi:10.1002/smll.201303068.
  11. ^ Detection of blotted proteins : methods and protocols. Kurien, Biji T.,, Scofield, R. Hal,. New York, NY. ISBN 9781493927180. OCLC 913123725.{{cite book}}: CS1 maint: extra punctuation (link) CS1 maint: others (link)
  12. ^ Lin, Chenxiang; Katilius, Evaldas; Liu, Yan; Zhang, Junping; Yan, Hao (2006-08-11). "Self-Assembled Signaling Aptamer DNA Arrays for Protein Detection". Angewandte Chemie International Edition. 45 (32): 5296–5301. doi:10.1002/anie.200600438. ISSN 1433-7851.
  13. ^ Park, Do Hyun; Lee, Jae-Seung (2015). "Functionalized nanoparticle probes for protein detection". Electronic Materials Letters. 11 (3): 336–345. doi:10.1007/s13391-014-4383-0. ISSN 1738-8090.
  14. ^ Morishita, Naoki; Matsumoto, Takashi; Morimatsu, Fumiki; Toyoda, Masatake (2014). "Detection of Soybean Proteins in Fermented Soybean Products by Using Heating Extraction: Detection of soybean in fermented food…". Journal of Food Science. 79 (5): T1049 – T1054. doi:10.1111/1750-3841.12461.
  15. ^ Nong, Rachel Yuan; Gu, Jijuan; Darmanis, Spyros; Kamali-Moghaddam, Masood; Landegren, Ulf (2012). "DNA-assisted protein detection technologies". Expert Review of Proteomics. 9 (1): 21–32. doi:10.1586/epr.11.78. ISSN 1478-9450.
  16. ^ Detection of highly dangerous pathogens : microarray methods for the detection of BSL 3 and BSL 4 agents. Kostic, Tanja., Butaye, Patrick., Schrenzel, Jacques. Weinheim: Wiley-VCH. 2009. ISBN 9783527626687. OCLC 463436671.{{cite book}}: CS1 maint: others (link)
  17. ^ Ros, E; Nunez, I; Perez-Heras, A (2004). "A walnut diet improves endothelial function in hypercholesterolemic subjects. A randomized crossover trial". ACC Current Journal Review. 13 (6): 19–20. doi:10.1016/j.accreview.2004.06.062.
  18. ^ Almoosawi, Suzana Fyfe, Lorna Ho, Clement Al-Dujaili, Emad A S (2009-10-13). The effect of polyphenol-rich dark chocolate on fasting capillary whole blood glucose, total cholesterol, blood pressure and glucocorticoids in healthy overweight and obese subjects. Cambridge University Press. OCLC 706594347.{{cite book}}: CS1 maint: multiple names: authors list (link)
  19. ^ Savage, G. P.; Dutta, P. C.; McNeil, D. L. (1999). "Fatty acid and tocopherol contents and oxidative stability of walnut oils". Journal of the American Oil Chemists' Society. 76 (9): 1059–1063. doi:10.1007/s11746-999-0204-2.
  20. ^ Preparation and use of food-based dietary guidelines : report of a Joint FAO/WHO Consultation. Joint FAO/WHO Consultation on the Preparation and Use of Food-Based Dietary Guideline., World Health Organization. Geneva: World Health Organization. 1998. ISBN 9241208805. OCLC 40216171.{{cite book}}: CS1 maint: others (link)
  21. ^ Silver, M.; Comline, R. S. (1975). "Transfer of gases and metabolites in the equine placenta: a comparison with other species". Journal of Reproduction and Fertility. Supplement (23): 589–594. ISSN 0449-3087. PMID 1529.
  22. ^ Teuber, Suzanne S.; Comstock, Sarah S.; Sathe, Shridhar K.; Roux, Kenneth H. (2003). "Tree nut allergy". Current Allergy and Asthma Reports. 3 (1): 54–61. doi:10.1007/s11882-003-0013-x. ISSN 1529-7322.
  23. ^ Asthma '84: Pharmacologic Update (1984 : Rancho Mirage, Calif.) (1985). Asthma '84: Pharmacologic Update : October 31 to November 3, 1984, Rancho Mirage, California. Mosby. OCLC 12425311.{{cite book}}: CS1 maint: numeric names: authors list (link)
  24. ^ Bock, S.Allan; Muñoz-Furlong, Anne; Sampson, Hugh A. (2001). "Fatalities due to anaphylactic reactions to foods". Journal of Allergy and Clinical Immunology. 107 (1): 191–193. doi:10.1067/mai.2001.112031.
  25. ^ Lawrence Berkeley National Laboratory. United States. Department of Energy. Office of Scientific and Technical Information. (2008). Decreased expression of RNA interference machinery, Dicer and Drosha, is associated with poor outcome in ovarian cancer patients. Lawrence Berkeley National Laboratory. OCLC 727220807.
  26. ^ Sampson, Hugh A.; Mendelson, Louis; Rosen, James P. (1992-08-06). "Fatal and Near-Fatal Anaphylactic Reactions to Food in Children and Adolescents". New England Journal of Medicine. 327 (6): 380–384. doi:10.1056/NEJM199208063270603. ISSN 0028-4793.
  27. ^ Baker, D.G. (1997). Relationship between posttraumatic stress disorder and self-reported physical symptoms in Persian Gulf War veterans. OCLC 772409021.
  28. ^ Kemp, Stephen F. (1995-09-11). "Anaphylaxis: A Review of 266 Cases". Archives of Internal Medicine. 155 (16): 1749. doi:10.1001/archinte.1995.00430160077008. ISSN 0003-9926.
  29. ^ Warner, J.O. (2002). "How dangerous is food allergy in childhood?". Pediatric Allergy and Immunology. 13 (3): 149–150. doi:10.1034/j.1399-3038.2002.00059.x. ISSN 0905-6157.
  30. ^ ScienceDirect (Service en ligne). The journal of pediatrics. OCLC 798778572.
  31. ^ Oki, T.; Yoshimoto, A.; Sato, S.; Takamatsu, A. (1975-12-18). "Purine nucleotide pyrophosphotransferase from Streptomyces morookaensis, capable of synthesizing pppApp and pppGpp". Biochimica Et Biophysica Acta. 410 (2): 262–272. ISSN 0006-3002. PMID 1088.
  32. ^ Boyd, George K. (1989-07-01). "Fatal Nut Anaphylaxis in a 16-Year-Old Male: Case Report". Allergy and Asthma Proceedings. 10 (4): 255–257. doi:10.2500/108854189778959966. ISSN 1088-5412.
  33. ^ Taylor, Stephen L.; Bush, Robert K.; Busse, William W. (1986-11-01). "Avoidance Diets—How Selective Should We Be?". Allergy and Asthma Proceedings. 7 (6): 527–532. doi:10.2500/108854186779045502. ISSN 1088-5412.
  34. ^ Dawson, R. M. (1975). "The reaction of choline and 3,3-dimethyl-1-butanol with the acetylenzyme from acetylcholinesterase". Journal of Neurochemistry. 25 (6): 783–787. ISSN 0022-3042. PMID 1471.
  35. ^ Prado, M.; Ortea, I.; Vial, S.; Rivas, J.; Calo-Mata, P.; Barros-Velázquez, J. (2016-11-17). "Advanced DNA- and Protein-based Methods for the Detection and Investigation of Food Allergens". Critical Reviews in Food Science and Nutrition. 56 (15): 2511–2542. doi:10.1080/10408398.2013.873767. ISSN 1040-8398.
  36. ^ Brežná, B.; Hudecová, L.; Kuchta, T. (2006). "A novel real-time polymerase chain reaction (PCR) method for the detection of walnuts in food". European Food Research and Technology. 223 (3): 373–377. doi:10.1007/s00217-005-0214-8. ISSN 1438-2377.
  37. ^ Yano, Takeo; Sakai, Yumiko; Uchida, Kohji; Nakao, Yoshiki; Ishihata, Kimie; Nakano, Shigeru; Yamada, Toshihiro; Sakai, Shinobu; Urisu, Atsuo (2007-07-23). "Detection of Walnut Residues in Processed Foods by Polymerase Chain Reaction". Bioscience, Biotechnology, and Biochemistry. 71 (7): 1793–1796. doi:10.1271/bbb.70118. ISSN 0916-8451.
  38. ^ Doi, Hirotoshi; Touhata, Yuki; Shibata, Haruki; Sakai, Shinobu; Urisu, Atsuo; Akiyama, Hiroshi; Teshima, Reiko (2008-09-10). "Reliable Enzyme-Linked Immunosorbent Assay for the Determination of Walnut Proteins in Processed Foods". Journal of Agricultural and Food Chemistry. 56 (17): 7625–7630. doi:10.1021/jf801550h. ISSN 0021-8561.
  39. ^ Anderson, Neil; Suliman, Ibnauf; Bandaletova, Tatiana; Obichere, Austin; Lywood, Rupert; Loktionov, Alexandre (2011). "Protein biomarkers in exfoliated cells collected from the human rectal mucosa: implications for colorectal disease detection and monitoring". International Journal of Colorectal Disease. 26 (10): 1287–1297. doi:10.1007/s00384-011-1263-z. ISSN 0179-1958.
  40. ^ Parro, Víctor; Rivas, Luis A.; Gómez-Elvira, Javier (2008). "Protein Microarrays-Based Strategies for Life Detection in Astrobiology". Space Science Reviews. 135 (1–4): 293–311. doi:10.1007/s11214-007-9276-1. ISSN 0038-6308.
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References

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