| Summary: | 碩士 === 國立臺灣海洋大學 === 食品科學系 === 102 === Collagen peptide is made from collagen through an enzymatic hydrolysis process. Compare with collagen, it has better water–soluble feature and more extensive physiological activity, which can be easily absorbed by human body. The purpose of this study is to establish the enzymatic conditions for preparing collagen peptide from tilapia fish skin, and fractionate different molecular weight (5–10 kDa, 3–5 kDa, 1-3 kDa, < 1 kDa) using an ultrafiltration system. The collagen peptides obtained were compared with their calcium binding ability. Finally, using Caco-2 cell model to study on the calcium bioavailability of the fish skin collagen peptide. Among them, collagen peptides from fish skin treated with Alcalase plus Flavourzyme showed higher calcium binding ability, and were selected in the following study. The optimal conditions in two enzymes system were listed as follows : temperature 50℃, pH 7.5, hydrolysis time 2 hr, showed higher calcium binding ability. Using an ultrafiltration system, the fraction (<1 kDa) had higher calcium binding ability, named it ‘fish skin collagen peptide (FSCP)’. The results of stability of calcium binding ability of FSCP were listed as follows : temperature 25℃, pH 7.8, showed higher calcium binding ability and addition of lactose was conducive to bind Ca2+ to FSCP. Effect of 5 mg/mL FSCP on growth of Caco-2 cell after 24 hr of treatment, its cell viability reach up to 100%. Intestinal permeability test showed that the fish skin collagen peptide can promote calcium uptake.
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