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Pepsin from the stomach of albacore tuna, skipjack tuna, and tongol tuna was characterized. Pepsin from all tuna species showed maximal activity at pH 2.0 and 50 degrees C when hemoglobin was used as a substrate. Among the stomach extract of all species tested, that of albacore tuna showed the highest activity (40.55 units/g tissue) (P < 0.05). Substrate-Native-PAGE revealed that pepsin from albacore tuna and tongol tuna consisted of 2 isoforms, whereas pepsin from skipjack tuna had only 1 form. The activity was completely inhibited by pepstatin A, while EDTA (ethylenediaminetetraacetic acid), SBTI (soybean trypsin inhibitor), and E-64 (1-(L-trans-epoxysuccinyl-leucylamino)-4-guanidinobutane) exhibited negligible effect. The activity was strongly inhibited by SDS (sodium dodecyl sulfate) (0.05% to 0.1%, w/v). Cysteine (5 to 50 mM) also showed an inhibitory effect in a concentration dependent manner. ATP, molybdate, NaCl, MgCl(2), and CaCl(2) had no impact on the activity. When tuna pepsin (10 units/g defatted skin) was used for collagen extraction from the skin of threadfin bream for 12 h, the yield of collagen increased by 1.84- to 2.32-fold and albacore pepsin showed the comparable extraction efficacy to porcine pepsin. The yield generally increased with increasing extraction time (P < 0.05). All collagen obtained with the aid of tuna pepsin showed similar protein patterns compared with those found in acid-solubilized collagen. Nevertheless, pepsin from skipjack tuna caused the degradation of alpha and beta components. All collagens were classified as type I with large portion of beta-chain. However, proteins with molecular weight (MW) greater than 200 kDa were abundant in acid-solubilized collagen.

BACKGROUND: Clown featherback (Chitala ornata) skin, a by-product from the filleting process line, could serve as a good aquatic collagenous source. Nevertheless, the typical collagen extraction method is a time-consuming process providing a relatively low yield. Ultrasound had been reported to be an alternative technique for enhancing the extraction efficiency of several compounds, although the harsh conditions of ultrasound could affect their physicochemical and molecular characteristics. Thus, the application of ultrasonication under appropriate conditions could comprise a promising means for improving the extraction efficiency of collagen from clown featherback skin. RESULTS: Ultrasonication using different amplitudes (20-80%) and times (10-30 min) was implemented during extraction. An ultrasound-assisted process (UAP) was able to increase the yield of collagen (P < 0.05) and could also result in a collagen purity decrease as evaluated by hydroxyproline content. There was no dramatic change in the solubility of resulting collagens. UAP induced protein degradation, particularly with an increasing amplitude and time, where slight changes in the isoelectric point value of collagen were observed. UAP had no adverse effect on molecular structure, where a triple-helical structure was still retained when an 80% amplitude was employed for 10 min (UAP-80/10-C). The amino acid composition of UAP-80/10-C reconfirmed the unique characteristic of collagen containing imino acid. CONCLUSION: An UAP under appropriate conditions could be used to improve the extraction yield with minimal effects on the molecular integrity of the resulting collagen. In addition, fish skin waste from the cutting process line, particularly clown featherback skin, could be exploited as a value-added product, comprising fish skin collagen.

Water-soluble proteins extracted from two species of grasshoppers, Patanga succincta (WSPP) and Chondracris roseapbrunner (WSPC), were characterized as well as their functional properties and antioxidant activities were investigated. e extraction yield, on a wet weight basis, was 7.35% and 7.46% for WSPP and WSPC, respectively. e most abundant amino acid in both proteins was glutamic acid, followed by aspartic, alanine, and leucine, in that order. e electrophoretic study revealed that proteins with MW of 29, 42, 50, 69, and 146 kDa were the major protein components in WSPP and WSPC. FTIR analysis showed that those proteins remained their structural integrity. e surface hydrophobicity at pH 7 of WSPC was higher than WSPP, but the sulfhydryl group content did not show significant difference between the proteins from two species. Both grasshopper proteins were mostly soluble in strong acidic and alkaline aqueous solutions with a minimum value at pH 4. ose proteins exhibited poor emulsifying properties and foaming capacity, but they had greater foaming stability compared with bovine serum albumin (BSA) (p < 0.05). WSPC showed greater DPPH • and ABTS •+ scavenging activities and ferric-reducing antioxidant power (FRAP) than did WSPP (p < 0.05). erefore, based on characteristics and functional properties, water-soluble proteins from both edible grasshoppers can be used as an ingredient in food applications.