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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Main Authors: Qiu-Yu Han, Tomoyuki Koyama, Shugo Watabe, Yuji Nagashima, Shoichiro Ishizaki
Format: Article
Language:English
Published: MDPI AG 2023-01-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/28/2/889
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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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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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