Effect of Particle Size on the Kinetic Parameters of the Deproteinization Process of Galactose Supplemented Shrimp Shells by Aspergillus niger

Authors

  • Nesreen Mahmoud Department of Agricultural Engineering, Faculty of Agriculture, Cairo University, Giza, Egypt
  • Abdel Ghaly Department of Process Engineering and Applied Science, Faculty of Engineering, Dalhousie University, Halifax, Nova Scotia, Canada

DOI:

https://doi.org/10.12970/2311-1755.2015.03.01.3

Keywords:

 Shrimp shells, protein, chitin, minerals, deproteinization, Aspergillus. niger, proteases, galactose, temperature, pH, moisture content.

Abstract

The aim of the research was to evaluate the ability of the fungus Aspergillus niger to carry out the deproteinization of shrimp shells supplemented with galactose as a carbon source and study the effect of the particle size of the shrimp shells on the kinetic parameters of the deproteinization process. Grounding of the shells resulted in a higher specific growth rate of A. niger and enhanced protease production by 2.6 fold. The temperatures of the shrimp shells and exhaust gas declined at the beginning as the heat losses from the bioreactor (due to evaporation) were higher than the heat generated by the metabolic activity. After 24h, the temperature of the shrimp shells and exhaust gas started to rise as a result of increased metabolic activity. Temperature peaks of 38.3 °C and 37.8 °C for the shrimp shells and 29.1 ºC and 29.0 ºC for the exhaust gas were noticed after 60 and 72 h of deproteinization for the ground and intact shrimp shells, respectively. There were no temperature gradients in the radial or axial direction because of mixing. The pH first decreased with time due to production of acid protease and then increased due to the buffering capacity of the calcium carbonate released from shrimp shells and the production of ammonium nitrogen. A significant reduction in the moisture content was noticed during the deproteinization process. In order to maintain the moisture in the bioreactor at the desired level, the exhaust gas should be passed through a condensation tower and the recovered water be pumped back into the bioreactor through the aeration tube. The galactose concentration decreased with time and the rate of galactose utilization was significantly higher in case of ground shrimp shells. Size reduction results in higher surface area and shorter pathways for nutrients diffusion. The protein removal efficiency (30.45% - 33.23%) did not correspond to the protease production. This could be a result of unsuitable pH and temperature conditions for the hydrolysis of shells proteins. The chitin concentration increased over time from the initial value of 16.59 % to final values of 21.99 %and 22.68% for the intact and ground shells, respectively. The color of the intact and ground shells was pale pink-orange with some tan patches. Some of the ground shrimp shells agglomerated and formed small balls. This problem was not observed with the intact shells. The ground shells had more white precipitants which were believed to be a result of break down of substances from the shell matrix.

References

Dutta PK, Dutta J, Tripathi VS. Chitin and chitosan: chemistry, properties and applications. J Sci Ind Res 2001; 63(1): 20-31.

Zakaria MB, Jais MJ, Alimuniar A, Harahap ZA, Nagah WSW. Chitosan as a chemical agent in the treatment of water and waste waters. In: Chitin and Chitosan the Versatile Environmentally Friendly Modern Materials, Zakaria MB, Muda WMW, Abdullah MP (Eds.), Universiti Kebangsaan Malaysia, Malaysia 1995.

Zakaria Z, Hall GM, Shama G. Lactic acid fermentation of scampi waste in a rotating horizontal bioreactor for chitin recovery. Process Biochem 1998; 33(1): 1-6. http://dx.doi.org/10.1016/S0032-9592(97)00069-1

Gagné N, Simpson BK. Use of proteolytic enzymes to facilitate the recovery of chitin from shrimp wastes. Food Biotechnol 1993; 7(3): 253-263. http://dx.doi.org/10.1080/08905439309549861

Bustos RO, Healy MG. Microbial deproteinisation of waste prawn shell. Int Symp Environ Biotechnol, Three-Day Symp, 2nd pp. 13-15. Dep Chem Eng Queen;s Univ Belfast Belfast, 1994; UK BT9 5AG. CAN122: 38064.

Hall GM, De Silva S. Lactic acid fermentation of shrimp (Peneaus monodon) waste for chitin recovery. In: Advances in Chitin and Chitosan, Brine CJ, Sandford PA, Zikakis JP (Eds.) 1992; Elsevier Applied Sciences, London, UK; 663-638. CAN119: 117735

Hall GM, Reid CL, Zakaria Z. Fermentation of prawn waste by lactic acid bacteria. In: Chitin World, Karnicki ZS, Wojtasz-Pająk A, Brzeski MM, Bykowski PJ (Eds.), Sea Fisheries Institute Gdynia, Poland. Proceeding from the 6th International Conference on Chitin and Chitosan, Wirtschaftsverlag, NW 1994.

Hall GM, Reid CL. Scale up of lactic acid fermentation process for the recovery of chitin from prawn waste. In: Chitin and Chitosan the Versatile Environmentally Friendly Modern Materials, edited by: Zakaria MB, Muda WMW, Abdullah MP, Universiti Kebangsaan Malaysia 1995; pp. 47-52. CAN123:343984.

Beaney P, Mendoza JL, Healy M. Comparison of chitins produced by chemical and bioprocessing methods. J Chem Technol Biot 2005; 80(2): 145-150. http://dx.doi.org/10.1002/jctb.1164

Shimahara K, Ohkouchi K, Ikeda M. A new isolation method of crustacean chitin using a proteolytic bacterium, Pseudomonas maltophilia. In: Chitin and Chitosan, Proceeding of the second International Conference on Chitin and Chitosan, Hirano S, Tokura S, (Eds.), Japanese Society of Chitin and Chitosan 1992.

Cano-Lopez A, Simpson BK, Haard NF. Extraction of carotenoprotein from shrimp process wastes with the aid of trypsin from Atlantic cod. Journal of Food Science 1987; 52(2): 503-506. http://dx.doi.org/10.1111/j.1365-2621.1987.tb06656.x

Shimahara K, Takiguchi Y. Preparation of crustacean chitin. Methods Enzymol 1988; 161(47): 417-423.

Wang S, Chio S. Deproteinization of shrimp and crab shell with the protease of Pseudomonas aeruginosa K-187. Enzyme Microb Tech 1998; 22(7): 629-633. http://dx.doi.org/10.1016/S0141-0229(97)00264-0

Teng WL, Khor E, Tan TK, Lim LY, Tan SC. Cocurrent production of chitin from shrimp shells and fungi. Carbohydrate Research 2001; 332: 305-316. http://dx.doi.org/10.1016/S0008-6215(01)00084-2

Takeda M, Katsuura H. Isolation of crustacean chitin – II. Removing of protein by some proteases, organic solvents and surface active agents. Norinsho Suisan Koshujo kenkyu hokoku 1964; 13(2): 35-42.

Berka RM, Dunn-Coleman N, Ward M. Industrial enzymes from Aspergillus species. In: Aspergillus Biology and Industrial Applications, Bennett JW, MA Klich (Eds.), Butterworth-Heinemann, Stoneham, MA 1992.

Ray B. Fundamental Food Microbiology. CRC Press, Florida, USA 1996.

Naidu GSN, Panda T. Studies on pH and thermal deactivation of pectolytic enzymes from Aspergillus niger. Biochem Eng J 2003; 16(1): 57-67. http://dx.doi.org/10.1016/S1369-703X(03)00022-6

Pandey A. Recent process developments in solid-state fermentation. Process Biochem 1992; 27(2): 109-117. http://dx.doi.org/10.1016/0032-9592(92)80017-W

Kong N. A feasibility study of new routes to the marine polymers chitin and chitosan. Unpublished master’s thesis. University of Washington, Washington, USA 1975.

Hesseltine CW. Solid State Fermentation, Part I. Process Biochem 1977; 12: 24-27. doi:10.1002/bit.260140402

Wehr M, Frank JF. Standard Methods for the Examination of Dairy Products, 17th ed. American Public Health Association, Washington, DC. 2004. http://dx.doi.org/10.2105/9780875530024

Hansen HO, Aschan M. Growth size- and age-at-maturity of shrimp, Pandalus Borealis, at Svalbard related to environmental parameters. J Northw Atl Fish Sci 2000; 27: 83-91. http://dx.doi.org/10.2960/J.v27.a8

Masuko T, Minami A, Iwasaki M, Majima T, Nishimura S. Carbohydrate analysis by phenol sulfuric acid method in microplate format. Anal Chem 2005; 339(1): 69-72. http://dx.doi.org/10.1016/j.ab.2004.12.001

Zakaria Z. Lactic acid purification of chitin from prawn waste using a horizontal rotating bioreactor. Unpublished PhD thesis, Loughborough University. Loughborough, UK 1997. doi:10.1016/S0032-9592(97)00069-1

Pandey A. Solid-state fermentation. Biochem Eng J 2003; 13(2-3): 81-84. http://dx.doi.org/10.1016/S1369-703X(02)00121-3

Ghildyal NP, Ramakrishna M, Lonsane BK, Karanth NG, Krishnaiah MM. Temperature variations and amylogluco-sidase levels at different bed depths in a solid state fermentation system. Chem Eng J 1993; 51(2): B17-B23. http://dx.doi.org/10.1016/0300-9467(93)80019-K

Ghaly AE, Mahmoud NS. Influence of ambient air temperature on the cooling/heating load of a single cell protein jacketed fermenter operating on cheese whey under continuous conditions. Biotechnol Prog 2002; 18(4): 713-722. http://dx.doi.org/10.1021/bp020053f

Pandey A. Production of glucoamylase enzyme in solid-state fermentation. International Symposium on Ind Biotechnol, Hyderabad, India, 18-20. 1990. CAN120:52739.

Ghildyal NP, Gowthaman MK, Raghava Rao KSMS Karanth NG. Interaction of transport resistances with biochemical reaction in packed-bed solid-state fermentors: effect of temperature gradients. Enzyme Microb Technol 1994; 16(3): 253-257. http://dx.doi.org/10.1016/0141-0229(94)90051-5

Saucedo-Castañeda G, Gutiérrez-Rojas M, Bacquet G, Raimbault M, Viniegra-González G. Heat transfer simulation in solid substrate fermentation. Biotechnol Bioeng 1990; 35(8): 802-808. http://dx.doi.org/10.1002/bit.260350808

Ben-Hassan RM, Ghaly AE, Ben-Abdallah N. Heat generation during batch and continuous production of single cell protein from cheese whey. Biomass Bioenergy 1993; 4(3): 213-225. http://dx.doi.org/10.1016/0961-9534(93)90060-H

Ghaly AE, Kamal M, Avery A. Influence of temperature rise on kinetic parameters during propagation of Kluyveromyces fragilis in cheese whey under ambient condition. World J Microbiol Biotechnol 2003; 19(5): 741-749. http://dx.doi.org/10.1023/A:1025148022934

Ghaly AE, Kok R, Ingrahm JM. Growth rate determination of heterogeneous microbial population in swine manure. Appl Biochem Biotechnol 1989; 22(1): 59-78.

Yang SS. Protein enrichment of sweet potato residue with amylolytic yeasts by solid state fermentation. Biotechnol Bioeng 1988; 32: 886-890. http://dx.doi.org/10.1002/bit.260320706

Andrade VS, Sarubbo LA, Fukushima K, Miyaji M, Nishimura K, Takaki GMC. Production of extracellular proteases by Mucor circinelloides using D-Glucose as carbon source/substrate. Braz J Microbiol 2002; 33(2): 106-110. http://dx.doi.org/10.1590/S1517-83822002000200002

Mudgett RE. Solid-state fermentations. In: Manual of Industrial Microbiology and Biotechnology, Demain AL, Nadine AS (Eds.), American Society for Microbiology, Washington, D.C., 1986; 66-83.

Diaz L, Savage F, Eggerth G, Golueke M. Composting and Recycling of Municipal Solid Waste. Lewis Publishers, Boca Raton, FL 1993.

Molony AP, O’Rorke A, Considine PJ, Coughlan MP. Enzymatic saccharification of sugar beet pulp. Biotechnol Bioeng 1984; 26: 714-718. http://dx.doi.org/10.1002/bit.260260713

Pandey A, Nigam P, Vogel M. Simultaneous saccharification and protein enrichment fermentation of sugar beet pulp. Biotechnol Lett 1988; 10(1): 67-72. http://dx.doi.org/10.1007/BF01030026

Bellon-Maurel V, Orliac O, Christen P. Sensors and measurements in solid state fermentation: a review. Process Biochem 2003; 38(6): 881-896. http://dx.doi.org/10.1016/S0032-9592(02)00093-6

Ghildyal NP, Ramakrishna M, Lonsane BK, Karanth NG. Gaseous concentration gradients in tray type solid state fermentors – effect on yields and productivities. Bioprocess Eng 1992; 8(1-2): 67-72. http://dx.doi.org/10.1007/BF00369266

Carrizalez V, Rodriguez H, Sardina I. Determination of the specific growth of molds on semisolid cultures. Biotechnol Bioeng 1981; 23(2): 321-333. http://dx.doi.org/10.1002/bit.260230207

Pandey A. Effect of particle size of substrate on enzyme production in solid-state fermentation. Bioresour Technol 1991; 37(2): 169-172. http://dx.doi.org/10.1016/0960-8524(91)90206-Y

Krishna C, Chandrasekaran M. Banana waste as substrate for α-amylase production by Bacillus subtilis (CBTK 106) under solid-state fermentation. Appl Microbiol Biotechnol 1996; 46(2): 106-111. http://dx.doi.org/10.1007/s002530050790

Chakraborty R, Srinivasan M, Sarkar SK, Raghavan SV. Production of acid protease by a new Aspergillus niger by solid substrate fermentation. J Microbiol Biotechnol 1995; 10(1): 17-30. ISSN: 0256-8551

Diniz FM, Martin AM. Fish protein hydrolysates by enzymatic processing. Agro Food Industry Hi-Tech 1997; 8(3): 9-13.

Bailey JE, Ollis DF. Biochemical Engineering Fundamentals. 2nd ed., McGraw-Hill Inc, New York, NY 1986.

Cira LA, Huerta S, Hall GM, Shirai K. Pilot scale lactic acid fermentation of shrimp wastes for chitin recovery. Process Biochem 2002; 37(12): 1359-1366. http://dx.doi.org/10.1016/S0032-9592(02)00008-0

Lonsane BK, Ghildyal NP, Budiatman S, Ramakrishna SV. Engineering aspects of solid state fermentation. Enzyme Microb Technol 1985; 7(6): 258-265. http://dx.doi.org/10.1016/0141-0229(85)90083-3

Downloads

Published

2015-08-03

Issue

Section

Articles