The Betta fish displays a remarkable variety of phenotypes selected during domestication. However, the genetic basis underlying these traits remains largely unexplored. Here, we report a high-quality ...genome assembly and resequencing of 727 individuals representing diverse morphotypes of the Betta fish. We show that current breeds have a complex domestication history with extensive introgression with wild species. Using a genome-wide association study, we identify the genetic basis of multiple traits, including coloration patterns, the “Dumbo” phenotype with pectoral fin outgrowth, extraordinary enlargement of body size that we map to a major locus on chromosome 8, the sex determination locus that we map to
dmrt1
, and the long-fin phenotype that maps to the locus containing
kcnj15
. We also identify a polygenic signal related to aggression, involving multiple neural system-related genes such as
esyt2
,
apbb2
, and
pank2
. Our study provides a resource for developing the Betta fish as a genetic model for morphological and behavioral research in vertebrates.
Betta genomics reveal its domestication history and genetic basis of enormous diversity in morphology and behavior.
The study evaluated the amino acid composition, and the antioxidant and antihypertensive characteristics of micropeptides in skim milk powder. Milk proteins were slightly destroyed during the ...production of skim milk powder based on results sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The skim milk powder was rehydrated and salted-out. After centrifugation, the supernatants were subjected to microfiltration and then separated with Superdox-30G column fractionation, producing three fractions (PF-1, PF-2 and PF-3). The molecular weight of fraction PF-3 was about 1.0 KDa with a yield of 10.9 plus or minus 0.73 mg/g skim milk powder. Fraction PF-3 at 10 mg/mL showed modest antioxidant activity with a 1.1 - diphenyl - 2 - picrylhydraxyl (DPPH) free radical scavenging rate of 36.69 plus or minus 0.92%. The inhibitory rate of the angiotensin I-converting enzyme (ACE) activity of PF-3 at a concentration of 3 mg/mL was about 20.12 plus or minus 7.59%. Fraction PF-3 was found to be rich in Gly, Phe, Leu, Glu and Asp, and its total hydrophobic amino acid content was as high as 50.53%, which may have contributed to the antioxidant and ACE-inhibitory activities.
