Gelatine was extracted from chicken waste shown in fig 4. The comparison of yield and physiochemical properties of acid processed gelatine was done. The gelatine extracted is shown in fig 5. We were able to cut the jelly formed after boiling and cooling the extracted powder of gelatine in water. 3.1 Qualitative analysis of Gelatine Colour of the gelatine was determined and observed to be off white. Setting temperature was recorded to be 80C and setting time was 190 seconds. Melting temperature was recorded to be 220C and Melting time was found to be 80 seconds. 3.2 Quantitative analysis of Gelatine % Yield = ( Dry weight of gelatine/ weight of chicken waste)*100 = (15/100)g *100 =15% Results show that the yield of chicken acidic gelatine is 15%, which is higher than other reported gelatine of 7.5% from fish3 and 2-3% from bugs2 but quality factors of acidic gelatine were also good. 3.3 Analysis of extracted gelatine Analysis was performed by TA-XT Plus Texture Analyser measures texture and Capable of measuring any physical characteristic such as hardness, adhesiveness, strength, firmness, rupture point, brittleness is extremely efficient, coupled with our exponent software. Analyzers are simple to calibrate and easy to validate, the instrument is extraordinarily welldesigned, high speed testing, long-term reliability and accuracy by stable micro systems. Switch on the TA.XT Plus analyzer coupled with texture Exponent 32 program, Click on ?TA? and ?TA setting? and Click on ?Library? and then ?Return to start?.Load the following settings such as Mode: Measure:Force, Option:Return to start, Pre test speed:1.0 mm/sec,Test speed: 1.0 mm/sec.Post test speed: 5m/sec,Distance: 10mm then Fix the P/25 aluminum cylindrical probe to the machine and calibrate probe height to 50mm. set gelatine sample on the platform and bring the probe closer to the sample surface. Run a test? and enter details and Click on ?probe selection? and select P/25 probe. Select data acquisition rate 200 PPS.Click on ?Active information? and then ?Run a test? which allow computer to execute the program.The probe travels 10mm into the sample from the surface and then returns to the original position generating a force-time curve. Determine the maximum force on the positive peak of the curve and express it as firmness, area of the positive peak with the help of anchors and express it as consistency, negative area gives the adhesiveness.
1. A.A. Karim, Rajeev Bhat, 2008. Fish gelatin: properties, challenges, and prospects as an alternative to mammalian gelatins, Food Hydrocolloids. 23 , 563?576. 2. Abdalbasit Adam Mariod, Hadia Fadol Adam,2013.Gelatin, sources, extraction and industrial application, ACTA, 135-147. 3. Hamid Tava Kolipour ,2011 Extraction and evaluation of gelatin from silver crap waste, World Journal Of Fish And Marine Science, (IAUS), 3(1), 10-15. 4. Ratnasari I,sudarminto S.Y,Nusyamt H, simon B .Widjanarko ,2014 extraction process modification to enhance properties of skin gelatin of Pangas Catfish, Food And Public Health, e-ISSN, 2162- 8440. 5. G?mez-Guill?n, M.C., J. Turnay, M.D. Fern?ndezDiaz, N. Ulmo, M.A. Lizarbe and P. Montero, 2002. Structural and Physical Properties of Gelatin Extracted from Different MarineSpecies: AComparative Study. Food Hydrocolloids, 16: 25- 34 6. AOAC, 2000. Official Methods of Analysis. Association of Official Analytical Chemists, 17th Edition. 7. GMIA. 2012. Gelatin handbook. Gelatin Manufact. Inst.Am. New York, [online], http://www.gelatin-gmia.com/ html/qanda.html [retrieved: 22.09.2012]. 8. G?mez-Guill?n M.C., Montero P., 2001. Extraction of gelatin from megrim (Lepidorhombus boscii) skins with several organic acids. J. Food Sci. 66, 213-216 9. Grossman S., Bergman M., 1992. Process for the production of gelatin from fish skins. U.S. patent 5,093, 474. 10. Norizah Mhd Sarbon,Farah Badii,Nazlin K Howell. Preparation and characterization of chicken skin gelatine as alternative to mammalian gelatine, 30 (2013), 143-151. 11. Piez, K.A. and J. Gross, 1960. The amino acid composition of some fish collagens: the relations between composition and structure. J. Biol. Chem. 23: 995-999. 12. Zhou P., Regenstein J.M. Effects of alkaline and acid Pre treatments on Alaska pollock skin gelatin extraction.J. Food Sci. 70 (6), 392-396. 13. Choi, S.S. and J.M. Regenstein, 2000. Physicochemical and Sensory Characteristics of Fish Gelatin. J. Food Sci., 65: 194-199. 14. BSI, 1975. British Standard Institution. Methods for Sampling and Testing Gelatin (Physical and Chemical Methods). British Standards Institution, BS No.757. 15. Gelatin Manufacturers of Europe (GME). (2000). Standardised methods for the testing of edible gelatin. Gelatin Monograph, version July 2000. 16. Bailey A.J., Paul R.G., 1998. Collagen ? A not so simple protein. J. Soc. Leather Techn. Chem. 82 (3), 104-110. 17. Karim A.A., Bhat R., 2008. Gelatin alternatives for the food industry: Recent developments, challenges and prospects. Trends Food Sci. Techn. 19:644-656.
In chicken Industry, Chicken skin and other waste is major by-product of the chicken-processing part, causing waste and pollution. This being utilized could provide a valuable alternative source of gelatine to be used in food and pharmaceutical industry. Thus the low cost production may meet the demand of the global market to a certain extent.
The authors extend gratitude to the management of PES Institute of Technology, Bangalore for encouragement and research facilities to carry out this Project.
The author?s declares none.
Gelatine is a polypeptide produced by partial hydrolysis of collagen derived from animal skin, connective tissues and bones, the chemical structure is depicted in fig. 1. It is translucent, colourless, brittle, flavourless solidifying agent. It is Emulsifying, thickening, jellying, foaming, and viscosity enhancing, filming agents. It is a mixture of peptides and proteins, and structurally similar to collagen. It forms a viscous solution when dissolved in hot water that sets to a gel on cooling. The development of gelatine alternatives has gained importance in recent years due to BSE (Bovine Spongiform Encephalopathy) crises and for religious and social reasons10 . Waste generated in industries of meat products are frequently very large and represent a serious problem due to high content of organic matter. Moreover, the environmental problems are worsened by inadequate treatment of industrial solid waste.10 Thus; our study was based on low cost extraction of gelatin from food waste. Gelatine forms gels similar to those of carbohydrates by forming a micro structural network upon heating and cooling as represented in Fig 2. The global demand for gelatine has always been increasing all these years. It has been reported that the annual world output of gelatine is nearly 326,000 tons, with pig skin-derived gelatine being the highest (46%) output, bovine hides being 29.4%, bones 23.1%, and other sources 1.5%1 . Strong competition exists among manufacturers for the procurement of pigskin or other mammalian sources that has resulted in increased demand as well costs. There are few alternative sources available, where Researchers from academia and industry are researching to get an alternative to gelatine, and to find new low cost sources of gelatine that might be more favourable and accepted in industry1 . Gelatine has various applications in numerous industries, our study focuses on its applications in pharmaceutical industry. In the pharmaceutical health industry, gelatine is used to make the shells of hard and soft capsules, tablets, granulation, suppositories, plasma substitute for medicines, dietary/health supplements, syrups, etc. It is highly digestible and serves as a natural protective coating for medicines.7 It is reported that Amoxicillin, Celebrex, Oxycodone, Lyrica and many such medications contain gelatine. FDA recognises gelatine as safe for use in pharmaceutical industries. Applications of gelatine in industries are vast like gelatine is used in the food industry is probably best recognized in gelatine desserts and confectionery applications such as marshmallows and gummy-candies. It is also used as a binding and/or glazing agent in meat and aspics. Gelatine is also used in making jelliesGelatine is also abundantly used in Photography Industry. The first account of its use in photography was reported in the British Journal of Photography in September 1871, when Dr. Richard Leach Maddox suggested that the sensitizing chemicals could be coated on a glass plate in gelatine rather than a collodion emulsion.7 Gelatine has been used for many years in the cosmetics industry as ?hydrolyzed animal protein? in shampoos, conditioners, lipsticks, and fingernail formulas. Recently additional uses for gelatine are being found as a collagen source in topical creams and other value added cosmetic products. Gelatine is used to make smooth surface in paper industries as well. Gelatine is a protein consisting of various amino acids such as aspartic acid, arginine, glycine, proline, glutamic acid and alanine. The composition in percentage
2.1 Sampling Chicken waste was got from local market. The chicken waste sample comprising of skin and feet were used for extraction of gelatin.7 2.2 Sample processing and extraction Chicken waste consisting of skin and feet, were cleaned using tap water and drained. Traditionally two methods have been employed, acid extraction and alkali extraction. In the present work, Gelatine extraction is carried out by acid extraction method. Extraction has to be carried out at optimum temperature. It has been Divya et al. Int. J. Fund. Appl. Sci. Vol. 5, No. 2 (2016) 44-48 Fig 2: Partial hydrolysis of collagen Fig 3: Amino acid composition in gelatine 46 reported that lower temperature results in fewer yields and higher temperature leads to lower gelatine quality 2.3 Acid extraction method The extraction process comprised of three major steps: Pre-treatment, Extraction and Recovery. 100g of unfrozen chicken waste was cut into 10-20cm pieces. The sample was incubated in water bath, consisting 380ml distilled water and 0.4ml hydrogen peroxide for 20minutes. Hydrogen peroxide is basically used to prevent microbial growth. Subsequently, the sample was rinsed with clean water for 15minutes. It was then transferred to acid bath containing 250ml of distilled water and 1.3ml glacial acetic acid at 3.5 pH for 5hours. This was done to remove undesirable components. Organic acids like glacial acetic acid are better than stronger acids, as stronger acids denature collagen to give lower yield. After 5 hours, sample was rinsed until pH 5 was obtained. Sample was poured into a beaker containing 500ml water and incubated in hot water bath at 90OC for four hours, then transferred to another hot water bath at 50OC and incubated for four hours. The extracted gelatine was bleached with charcoal, filtered through pumice stone to remove insolubles, such as lipids and hydrolysed collagen fibres. Gelatine solution was dehydrated in hot air oven at 50-60OC until dry and made into thin layers or powder 2.4 Qualitative analysis of Gelatine Colour determination: Colour of obtained gelatine was determined by putting on white background. Gelatine colour must be pale yellow to amber 2.5 Setting Point And Setting Temperature 10% (w/v) gelatine solution was prepared in warm water bath. 30ml of this solution was transferred to test tube and placed in water bath at 40 OC. The water bath was slowly cooled by addition of cold water to get it to 2 OC Thermometer is placed into the solution and taken out every 15 seconds until a drop of the the sample does not drips; this temperature was recorded as setting point and setting time of gelatin 2.6 Melting Point And Melting Temperature 10%(w/v) gelatine solution was prepared in the same manner as previous section and stored in refrigerator at 7 OC for 2 hours and then transferred to water bath at 10OC with gradual addition of warm water at 450C and melting time and melting temperature was noted.2 2.7 Quantitative analysis of Gelatine Percentage yield is calculated with the formula10 % Yield = ( Dry weight of gelatine/ weight of chicken waste)*100