Albacore tuna spleen trypsin: Potential application as laundry detergent additive and in carotenoprotein extraction from Pacific white shrimp shells. (January 2019)

• Record Type: Journal Article
• Authors: Poonsin, Tanchanok; Simpson, Benjamin K.; Benjakul, Soottawat; Visessanguan, Wonnop; Yoshida, Asami; Klomklao, Sappasith
• Is Part Of: Biocatalysis and agricultural biotechnology. Number 17(2019)
• Page Start: 638
• Page End: 646
• Publication Date: 2019-01
• Subjects: Trypsin -- Tuna -- Detergent -- Carotenoprotein -- Shrimp; Agricultural biotechnology -- Periodicals; Enzymes -- Biotechnology -- Periodicals; 660.6
• DOI: 10.1016/j.bcab.2019.01.013
• Languages: English
• ISSNs: 1878-8181

Abstract

Abstract: Partitioned trypsin from spleen of albacore tuna ( Thunnus alalunga ) by ATPS was evaluated for its potential applications in laundry detergents and in the recovery of carotenoprotein from Pacific white shrimp ( Litopenaeus vannamei ) shells. The partitioned trypsin was extremely stable toward various surfactants and bleach agents and showed excellent stability and compatibility with commercial liquid and solid detergents. Additionally, partitioned trypsin showed an efficient hydrolysis and recovery of carotenoprotein from Pacific white shrimp shells. The carotenoprotein recovery was maximized by the hydrolysis of shrimp shells using 0.8 trypsin units/g shrimp shells at 25 °C for 45 min and shrimp shells/buffer ratio of 1:2 (w/v). Carotenoprotein consisted of 72.4% protein, 18.8% lipid, 7.1% ash, 1.6% chitin, and 73.3 µg total astaxanthin/g sample. It was rich in essential amino acids. When the hydrolytic activities of albacore tuna and bovine trypsins used in the extraction of carotenoprotein in Pacific white shrimp shells were compared, the recovery efficacy of protein and pigment by albacore tuna trypsin was similar to that achieved by bovine trypsin. These results suggest that albacore tuna trypsin could be used as an ideal choice for application in detergent formulations and for extraction of carotenoproteins. Graphical abstract: fx1 Highlights: Partitioned trypsin was extremely stable toward surfactants and oxidising agent. The enzyme showed high stability and compatibility with commercial detergents. It was highly recommended for application in detergent formulations. The trypsin showed an efficient extraction of carotenoprotein from shrimp shells.