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EXTRACTION OF CAROTENOPROTEIN FROM BLACK TIGER SHRIMP SHELLS WITH THE AID OF BLUEFISH TRYPSIN |
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| Authors: | S KLOMKLAO S BENJAKUL W VISESSANGUAN H KISHIMURA BK SIMPSON |
| Affiliation: | Department of Food Science and Technology, Faculty of Technology and Community Development, Thaksin University Phattalung Campus, Phattalung, 93110; Department of Food Technology Faculty of Agro-Industry, Prince of Songkla University Hat Yai, Songkhla, 90112; National Center for Genetic Engineering and Biotechnology National Science and Technology Development Agency 113 Paholayothin Rd., Klong 1, Klong Luang, Pathumthani, 12120, Thailand; Laboratory of Marine Products and Food Science Research Faculty of Fisheries Sciences, Hokkaido University Hakodate, Hokkaido, 041-8611, Japan; Department of Food Science and Agricultural Chemistry McGill University, Macdonald Campus 21111 Lakeshore Road, Ste. Anne de Bellevue, Quebec, H9X 3V9, Canada |
| Abstract: | The effect of bluefish (Pomatomus saltatrix) trypsin on the recovery and characteristics of carotenoprotein from black tiger shrimp (Penaeus monodon) shells was investigated. Trypsin concentration and reaction time both affected the hydrolysis and the recovery of carotenoproteins ( P < 0.05). The recovery of carotenoproteins from shrimp shells was maximized by the hydrolysis of shrimp shells using 1.2 trypsin units/g shrimp shells for 1 h at 25C. Freeze-dried carotenoprotein recovered contained 70.20% protein, 19.76% lipid, 6.57% ash, 1.50% chitin, and 87.91 µg total astaxanthin/g sample, indicating a substantial reduction in the levels of antinutrients associated with shrimp waste, while enriching the product in carotenoid pigments and valuable essential nutrients (proteins and lipids). Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of the recovered carotenoprotein revealed that protein with molecular weight of 45 kDa was the major constituent. When hydrolytic activities of bluefish and bovine trypsins toward carotenoproteins in black tiger shrimp shells were compared, the recovery efficacy of protein and pigment by bluefish trypsin was similar to that achieved by trypsin from bovine pancreas. Therefore, bluefish trypsin could be used as an alternative cheap proteinase for extraction of carotenoproteins from black tiger shrimp shells. PRACTICAL APPLICATIONSCarotenoproteins from black tiger shells, the byproduct of shrimp processing, can be recovered with the aid of fish trypsin. This product can be used for both food and feed applications. Additionally, the fish trypsin can be used instead of bovine trypsin. As a whole, the utilization of fish and shellfish processing wastes can be maximized. |
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