Nano collagen of the grouper swim bladder in compliance with quality standard of cosmetics materials

Abstract

Research of swim bladders on many species revealed that this organ has a high protein content that very potential as a source of collagen. This research aimed to isolate collagen from swim bladders of grouper, convert it into nano collagen, and determine the conformity of collagen with the quality standard of cosmetic materials. Collagen isolation was initiated by the process of elimination all non-collagen protein and other impurities (pre-extraction) with alkaline (NaOH) 0.05 M for 10 hours, followed by extraction with acetic acid 0.5 M (CH3COOH) for 48 hours with a sample and solvent volume ratio of 1:20 w/v at 4°C. The yield of the extracted collagen was 18.96±1.53%, solubility 81.10±0.88%, and whiteness 90.58±0.13%. Analysis of functional groups showed the presence of amide A, amide B, amide I, amide II, and amide III which indicated as a type 1 collagen. Collagen extract showed positive result for the coloring of Casson's trichrome. Ultrasonicated nano collagen for 150 minutes had a particle size of 404.1 nm and a polydispersity index of 0.446. The chemical compositions of collagen overall have met the quality requirements of collagen standards as a cosmetic material based on SNI 8076-2014.