Isolation and Characterization of Collagen and Collagen Peptides with Hyaluronidase Inhibition Activity Derived from the Skin of Marlin (<i>Istiophoridae</i>)
Type I and V collagens are the major components of fibrillogenic proteins in fish skin, and their hydrolysis products possess hyaluronidase inhibitory activity. In this study, for the first time, type I and V collagens were isolated from the skin of shortbill spearfish and striped marlin. Type I (2α...
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MDPI AG
2023-01-01
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author | Qiu-Yu Han Tomoyuki Koyama Shugo Watabe Yuji Nagashima Shoichiro Ishizaki |
author_facet | Qiu-Yu Han Tomoyuki Koyama Shugo Watabe Yuji Nagashima Shoichiro Ishizaki |
author_sort | Qiu-Yu Han |
collection | DOAJ |
description | Type I and V collagens are the major components of fibrillogenic proteins in fish skin, and their hydrolysis products possess hyaluronidase inhibitory activity. In this study, for the first time, type I and V collagens were isolated from the skin of shortbill spearfish and striped marlin. Type I (2α1[I]α2[I]) and type V (α1[V]α3[V]α2[V]) collagens composed of distinct α-peptide chains with comparable structures were investigated using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and UV spectrophotometric chromatography. After enzymatic digestion, the collagen peptides were purified by using ultrafiltration (30 KDa) and high-performance liquid chromatography (RP-HPLC) to yield CPI-F3 and CPV-F4 fractions with strong hyaluronidase inhibition rates (42.17% and 30.09%, respectively). Based on the results of simulated gastrointestinal fluid, temperature, and pH stability assays, CPI-F3 and CPV-F4 exhibited stability in gastric fluid and showed no significant changes under the temperature range from 50 to 70 °C (<i>p</i> > 0.05). The results of this first research on the bioactivity of type V collagen peptides provide valuable information for the biomedical industry and show the potential for future bioactivity investigations of type V collagen and its peptides. |
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language | English |
last_indexed | 2024-03-09T11:33:44Z |
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spelling | doaj.art-993a930b9d1040d6bec27489725b69352023-11-30T23:46:23ZengMDPI AGMolecules1420-30492023-01-0128288910.3390/molecules28020889Isolation and Characterization of Collagen and Collagen Peptides with Hyaluronidase Inhibition Activity Derived from the Skin of Marlin (<i>Istiophoridae</i>)Qiu-Yu Han0Tomoyuki Koyama1Shugo Watabe2Yuji Nagashima3Shoichiro Ishizaki4Graduate School of Marine Science and Technology, Tokyo University of Marine Science and Technology, Tokyo 108-8477, Tokyo, JapanGraduate School of Marine Science and Technology, Tokyo University of Marine Science and Technology, Tokyo 108-8477, Tokyo, JapanSchool of Marine Biosciences, Kitasato University, Minami, Sagamihara 252-0373, Kanagawa, JapanGraduate School of Marine Science and Technology, Tokyo University of Marine Science and Technology, Tokyo 108-8477, Tokyo, JapanGraduate School of Marine Science and Technology, Tokyo University of Marine Science and Technology, Tokyo 108-8477, Tokyo, JapanType I and V collagens are the major components of fibrillogenic proteins in fish skin, and their hydrolysis products possess hyaluronidase inhibitory activity. In this study, for the first time, type I and V collagens were isolated from the skin of shortbill spearfish and striped marlin. Type I (2α1[I]α2[I]) and type V (α1[V]α3[V]α2[V]) collagens composed of distinct α-peptide chains with comparable structures were investigated using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and UV spectrophotometric chromatography. After enzymatic digestion, the collagen peptides were purified by using ultrafiltration (30 KDa) and high-performance liquid chromatography (RP-HPLC) to yield CPI-F3 and CPV-F4 fractions with strong hyaluronidase inhibition rates (42.17% and 30.09%, respectively). Based on the results of simulated gastrointestinal fluid, temperature, and pH stability assays, CPI-F3 and CPV-F4 exhibited stability in gastric fluid and showed no significant changes under the temperature range from 50 to 70 °C (<i>p</i> > 0.05). The results of this first research on the bioactivity of type V collagen peptides provide valuable information for the biomedical industry and show the potential for future bioactivity investigations of type V collagen and its peptides.https://www.mdpi.com/1420-3049/28/2/889type I collagentype V collagencollagen peptidehyaluronidase inhibition activitymarlin skin |
spellingShingle | Qiu-Yu Han Tomoyuki Koyama Shugo Watabe Yuji Nagashima Shoichiro Ishizaki Isolation and Characterization of Collagen and Collagen Peptides with Hyaluronidase Inhibition Activity Derived from the Skin of Marlin (<i>Istiophoridae</i>) Molecules type I collagen type V collagen collagen peptide hyaluronidase inhibition activity marlin skin |
title | Isolation and Characterization of Collagen and Collagen Peptides with Hyaluronidase Inhibition Activity Derived from the Skin of Marlin (<i>Istiophoridae</i>) |
title_full | Isolation and Characterization of Collagen and Collagen Peptides with Hyaluronidase Inhibition Activity Derived from the Skin of Marlin (<i>Istiophoridae</i>) |
title_fullStr | Isolation and Characterization of Collagen and Collagen Peptides with Hyaluronidase Inhibition Activity Derived from the Skin of Marlin (<i>Istiophoridae</i>) |
title_full_unstemmed | Isolation and Characterization of Collagen and Collagen Peptides with Hyaluronidase Inhibition Activity Derived from the Skin of Marlin (<i>Istiophoridae</i>) |
title_short | Isolation and Characterization of Collagen and Collagen Peptides with Hyaluronidase Inhibition Activity Derived from the Skin of Marlin (<i>Istiophoridae</i>) |
title_sort | isolation and characterization of collagen and collagen peptides with hyaluronidase inhibition activity derived from the skin of marlin i istiophoridae i |
topic | type I collagen type V collagen collagen peptide hyaluronidase inhibition activity marlin skin |
url | https://www.mdpi.com/1420-3049/28/2/889 |
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