No abstract

Acid-soluble collagen (ASC) and pepsin solubilized collagen (PSC) were isolated from the skins of black drum (Pogonias cromis) and sheepshead seabream (Archosargus probatocephalus) harvested in the Gulf of Mexico coastal waters. The yields of ASCs on dry basis from black drum and sheepshead were estimated at 2.3 and 2.6%, and the yields of PSCs were 15.8 and 29.3%, respectively. Analyses of molecular weight profile, amino acid composition, and secondary structure showed that the skin collagens from both species were typical type-I collagen. The molecular mass of alpha(1) and alpha(2) subunits, as determined by SDS-PAGE using Tris-Acetate gels, was 127 kDa and 116 kDa, respectively. The amino acid composition of ASC and PSC for both species was closer to calf skin ASC than to cod skin ASC. Thermal denaturation temperatures, measured by melting point using circular dichroism, gave the following values: black drum ASC, 34.2 degrees C; sheepshead ASC, 34.0 degrees C; black drum PSC, 35.8 degrees C; sheepshead PSC, 34.3 degrees C. The literature value for the heat stability of calf skin collagen is 36.3 degrees C. The potentials of collagens from black drum and sheepshead skins in the functional food, healthcare, and pharmaceutical industries are discussed.

Proteases in grass shrimp (Penaeus monodon) digestive tract were extracted. Four fractions, A, B, C and D, demonstrated caseinolytic activity and were purified to electrophoretic homogeneity. A, C and D were trypsin-like, while B was a chymotrypsin-like protease. Optimal temperature for proteases A, B and C were 65"C, and that for D was 55°C for hydrolysis of casein. Optimal pH of proteases A and C was 8.0, and that of D was 7.0 for hydrolysis of p-toluenesulfonyl-L-arginine methyl ester. Optimal pH of protease B for hydrolysis of N-b&zoyl-L-tyrosine ethyl ester &as 8.b. Inactivation of SO-% enzyme activity in 5 min occurred at 67°C for protease B and 50°C for proteases A, C and D.

The foodborne pathogen Listeria monocytogenes represents a major concern to the food industry and particularly to producers of ready-to-eat (RTE) foods because of the severity of human listeriosis infections and because of the ubiquitous nature of this organism. Although several studies on the prevalence and sources of L monocytogenes in various RTE seafoods have been conducted, limited information is available on the presence and potential sources of this organism in RTE crawfish products. We thus monitored the presence of L monocytogenes and other Listeria spp. in the processing environment, in raw, whole crawfish, and in cooked crawfish meat from two processing plants. Samples were collected from the two plants throughout one crawfish season (April to June 2001) at 5 and 8 separate visits, respectively. At each visit, 6 raw, whole crawfish, 6 finished product samples (crawfish meat), and 14 mid- or end-of-processing environmental sponge samples were collected and tested for L. monocytogenes and Listeria spp. Of the 337 samples tested, 31 contained Listeria spp. Although Listeria innocua was the predominant Listeria spp. found (20 samples), four samples were positive for L monocytogenes. L. monocytogenes was detected in three raw material samples and in one environmental sample. Listeria spp. were found in 29.5% of raw, whole crawfish (n = 78) and in 4.4% of environmental samples (n = 181) but in none of the finished product samples. Among the environmental samples, Listeria spp. were found in 15.4% of the drains (n = 39) and in 5.1% of the employee contact surfaces (gloves and aprons) (n = 39) but in none of the samples from food contact surfaces. Even though a high prevalence of Listeria spp. was detected on raw materials, it appears that the heat treatment during the processing of crawfish and the practices preventing postprocessing recontamination can significantly reduce Listeria contamination of RTE crawfish meat.