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Protein hydrolysates from fishery byproducts have resulted to be nutraceutical ingredients with potential to be applied in human nutrition; however, critical quality attributes are dependent on some process parameters such as enzyme source and degree of hydrolysis. This study analyzed the biochemical properties and in vitro antioxidant activity (using DPPH, ABTS, and FRAP assays), of protein hydrolysates at 10, 20, and 30% degree of hydrolysis (DH), measured by pH-STAT and prepared from sea catfish (Bagre panamensis) muscle and casein as protein sources by treatment with alcalase (ALC) and a semi-purified protease extract (SPE) from B. panamensis intestinal tissues as enzyme sources. With SPE, the DH was reached faster than ALC regardless of the protein substrate used. Sea catfish muscle (MUSC) hydrolysate made with SPE at 30% DH showed the highest antioxidant activity (DPPH: 118.8 μmoles TE/mg; ABTS: EC 50 of 1.5 mg/mL). In FRAP assay, the MUSC hydrolysates produced with SPE or ALC at 20% DH showed the higher activity (0.38 and 0.40 μmoles TE/mg, respectively). MUSC hydrolysates made with SPE contained the highest proportion of peptides with MW < 1.35 kDa and had a high protein content (72 to 78%), and almost 50% of the amino acids were essential. These results suggest that intestinal proteases and muscle of marine catfish represent a potential source to elaborate antioxidant protein hydrolysates. Our results promote the full utilization of this fish species and offer a biotechnological strategy for the management and valorization of its byproducts., (© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)

The chilhuil sea catfish ( Bagre panamensis ) is an ecologically relevant species contributing to the structure, organization, and functioning of the ecosystems it inhabits. Also, it is an important artisanal fishery resource in the Mexican Pacific coast. This study aimed to determine the genetic diversity, population structure, and historical demography of B. panamensis in the Mexican Pacific. The mitochondrial DNA was amplified from two distinct regions, r16S and COI, resulting in an 1142 bp of the concatenated genes. Low genetic diversity levels were detected for r16S ( H  = 12; h =  0.131 ; π  =  0.0003 ) and high genetic diversity levels for COI ( H  = 57; h =  0.9128; π = 0.0039 ) and the concatenated gene fragments ( H  = 62; h =  0.9307; π = 0.0023 ). Population structure analysis indicated 'panmixia' for B. panamensis along the Mexican Pacific. Furthermore, historical demographic analysis (Tajima's D , Fu's F s, mismatch distribution, and Bayesian Skyline plot analyses) supported a population expansion scenario for the studied species.

The chihuil sea catfish ( Bagre panamensis ) is endemic of the Eastern Pacific and is a species of fishery importance in the Mexican Pacific. The complete mitochondrial genome of Bagre panamensis has been assembled from Illumina sequencing data. The circular genome was 16,714 bp in lengh, and consist of 13 protein-coding, two ribosomal RNAs (rRNAs), and 22 transfer RNA (tRNA) genes. Base composition is 30.8% A, 26.6% T, 28.2% C, and 14.4% G, and 42.6% GC content. Protein-coding genes present two start codon (ATG and GTG) and eight stop codon (TAA, TCT, CCT, TTA, CAT, AAT, ATT, and TAG). The control region possesses the highest A + T (64.4%) and lowest G + C content (35.6%) among all mitochondrial regions. These data would contribute to the evolutionary studies of related taxa., Competing Interests: The authors report no conflicts of interest. They alone are responsible for the content and writing of the manuscript., (© 2017 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.)