During the conversion of raw hides or skins into leather involves generation of enormous amount of solid waste which has been major concern for environment and cause detrimental effect on it. In leather industry solid wastes can be generated almost from all operations including pre-tanning, tanning, and even post tanning operation. Solid wastes are mainly raw trimmings, fleshing, chrome shaving, buffing dust, keratin, finished scraps etc. The economic development of a country depends on the utilization of indigenous raw materials and their by-products. This paper focuses on utilization of raw trimmings into useful product like non edible gelatin those demand is going up day by day due to its versatile application in various fields. Raw trimmings are mainly originated during sorting of leather before actual tanning process happens and best for non- edible gelatin production as it does not contain any harmful chemicals. This study will also describe the chemical properties of gelatin, gelatin manufacturing process, manufacturing parameters from the leather wastes like raw trimmings. Optimum extraction of non-edible gelatin from raw trimmings found at 75-85ₒC for 12 hours in slightly basic condition. This study found that huge amount of raw trimmings which generally thrown directly to environment can serve as potential raw materials for the manufacture of non-edible as well as edible gelatin.
M. A. C. P. C. R. C. I. L. L. &. J., Cot J, "Minimisation of Industrial wastes; Adding value to collagen materials," J Soc Leather Technol Chem: A.; Tomé, D.; L’Heureux-Bourdon, D.; Even, P.; Gietzen, pp. 87,97-99, (2003).
A. E. Postlethwaite, J. M. Seyer and A. H. ". Kang, "Chemotactic attraction of human fibroblasts to type I, II, and III collagens and collagen-derived peptides".," Proceedings of the National Academy of Sciences of the United States of America., p. 75 (2, (1978).
K. D. J. Haug, "In Handbook of Hydrocolloids," Vols. (Second Edition), 2009.
"The Science of Gelatin.," Accessed 01/21/2019. [Online]. Available: https://www.finecooking.com/article/the-science-of-gelatin,
N. M. N. K. e. a. A. Ayvazyan, “Collagen-gelatin scaffold impregnated with bFGF accelerates palatal wound healing of palatal mucosa in dogs,” Journal of Surgical Research, View at Publisher • View at Goo, Vols. vol. 171, no. 2, pp. e247–e257, 2011.
S. Sokolov, "Phisical Chemistry of Collagen and its Derivatives," Gizlegprom Moscow-Leningrad, , 1937.
S. e. a. C. o. g. f. t. s. o. b. s. P. t. a. P. m. F. C. BENJAKUL, 2009. [Online]. Available: http://dx.doi.org/10.1016/j.foodchem.2009.02.063.
in Gelatin Handbook, the original on 16 May 2017. Retrieved 27 September 2017.
"The Science of Gelatin".
R. Moskowitz, ""Role of collagen hydrolysate in bone and joint disease".," Seminars in Arthritis and Rheumatism. doi:10.1053/sarh.2000.9622. PMID 11071580, vol. 30 (2): 87–99., (2000).
D. D., "Enzymatic dehairing as an alternative to sulphide dehairing.," World Leath. [Google Scholar], vol. 1:29–34., 1988;
M. C. e. a. GÓMEZ-GUILLÉN, "Functional and bioactive properties of collagen and gelatin from alternative sources:A review. Food Hydrocolloids," http://dx.doi.org/10.1016/j.foodhyd.2011.02.007, Vols. v. 25, pp. p. 1813-1827, 2011.
K. D. J. Haug, in Handbook of Hydrocolloids (Second Edition), 2009.
S. GROSSMAN and M. BERGMAN, " Process for the production of gelatin from fish skins. US Patent 5.093.474," 1992.
F. a. K. N. Badii, "BSI., Methods for sampling and testing gelatin (physical and chemical methods).," British Standards Institution, London. Fish gelatin: Structure, gelling properties and interaction with egg albumen proteins. Food Hydrocolloids, 20: 630-640, 1975.
M. A. C. P. C. R. C. I. L. L. &. J. Cot J, "Minimisation of Industrial wastes; Adding value to collagen materials," J Soc Leather Technol Chem,, pp. 97-99,87, (2003),.
D. R. L. O. M. G. A. R. E. B. a. M. K. I. C. T. Silveira, "“Low temperature conversion of sludge and shavings from leather industry,”," Water Science and Technology, View at Google Scholar • , Vols. vol. 46, no. 10,, pp. pp. 277–283,, 2002..
W. M. 1. Ames, "The preparation of gelathe,," J. Soc. Chem. Ind.London, 63 200,234,277,303.Ames, W. M. , Vols. Parts 1, II, III, IV., 1952..
A. a. H. R. Ashgar, "The conversion of collagen to gelatin and their molecular structure.," J.Sci. Food Agric, 1982.
B. R. K. R. M. D. S. J. S. L. K. F.M., "Chemical, biochemical, functional andnutritional characteristics of collagen in food systems. In:" Advances in FoodResearch, Academic Press, LondonAusubel,, vol. Vol. 28., 1992..
G. a. B. J. N.Y.Babisn, "Current protocols in molecular biology.," Green publishing andWiley-Interscience,, 1977.
e. (A.G. Ward and Courts., "The structure and properties of collagen. In: TheScience and Technology of Gelatin," Academic Press, London.
A. R. L. K. B. K. P. D. H. a. Yang B, " Effect of structural change of collagen fibrils on the durability of dentin bonding.," Biomaterials 26: 5021–5031. [PubMed] [Google Scholar], (2005).
B. M. Bhattacharjee A, "Collagen structure: the Madras triple helix and the current scenario. IUBMB Life 57: 161–172. [PubMed]," [Google Scholar], (2005).
V. K. C. B. N. S. S. Kanagraj J, "Solid Wastes Generation in the leather industry and Its Utilization for Cleaner Environment-A review," J Scientific and Industrial Research 65: 541-548., (2006).
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