In vitro Anti-Cancer, Anti-Diabetic, Anti-Inflammation and Wound Healing Properties of Collagen Peptides Derived from Unicorn Leatherjacket (Aluterus Monoceros) at Different Hydrolysis

被引:23
作者
Kumar, Lakshmanan Vinoth [1 ]
Shakila, Robinson Jeya [2 ]
Jeyasekaran, Geevaretnam [3 ]
机构
[1] Tamil Nadu Dr J Jayalalithaa Fisheries Univ, Dept Fish Proc Technol, Fisheries Coll & Res Inst, Tuticorin, Tamil Nadu, India
[2] Tamil Nadu Dr J Jayalalithaa Fisheries Univ, Dept Fish Qual Assurance & Management, Fisheries Coll & Res Inst, Tuticorin, Tamil Nadu, India
[3] Tamil Nadu Dr J Jayalalithaa Fisheries Univ, Nagapattinam, Tamil Nadu, India
关键词
Fish skin; Collagen peptides; MTT assay; alpha-amylase inhibition assay; ANTIINFLAMMATORY ACTIVITY; ANTIMICROBIAL PEPTIDE; FISH; SKIN; ANTIOXIDANT; BONE; IDENTIFICATION; EXTRACTION; SCALES; GROWTH;
D O I
10.4194/1303-2712-v19_7_02
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
In this study, skin of unicorn leatherjacket (Aluterus monoceros) was hydrolyzed using collagenase at three different temperatures viz. 5 degrees C, 25 degrees C and 50 degrees C, to obtain collagen hydrolysates. Collagen peptides of low molecular masses (<3kDa) viz. CP-5, CP-25 and CP-50 were obtained by sequential ultrafiltration with tangential flow filtration (TFF) system. The results indicated that CP-5 exhibited the maximum in vitro anti-cancer, anti-diabetic and wound healing activities than CP-25 and CP-50. In MTT assay, CP-5 inhibited the viability of COLO320 cancer cells upto 49.78% at 1 mg/mL concentration, while the inhibition was only 29.92% by CP-50. Anti-diabetic activity as assessed by a-amylase inhibition was 80.45% by CP-5 at 1 mg/mL concentration, as against 75.81% and 71.17% by CP-25 and CP-50, respectively. Collagen peptides, in general, exhibited very low anti-inflammatory property, which ranged between 3.27% to 4.01%. In vitro wound healing tested by scratch assay showed good migration of 3T3-L1 cells in CP-5 treated than CP-25 and CP-50 at 0.2 mg/mL concentration. The study thus proved that collagen peptides derived from fish skin at low hydrolysis temperatures (50C) exhibited more bio-active activities than those hydrolysed at high temperatures (500C); and shall be effectively utilized in various bio-medical applications.
引用
收藏
页码:551 / 560
页数:10
相关论文
共 42 条
  • [1] DETERMINATION OF THE DEGREE OF HYDROLYSIS OF FOOD PROTEIN HYDROLYSATES BY TRINITROBENZENESULFONIC ACID
    ADLERNISSEN, J
    [J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1979, 27 (06) : 1256 - 1262
  • [2] Agarwal P., 2016, Res. Rev. J. Med. Health Sci, V5, P1
  • [3] Identification of ace-inhibitory peptides from squid skin collagen after in vitro gastrointestinal digestion
    Aleman, A.
    Gomez-Guillen, M. C.
    Montero, P.
    [J]. FOOD RESEARCH INTERNATIONAL, 2013, 54 (01) : 790 - 795
  • [4] [Anonymous], J BIOTECHNOLOGY
  • [5] Anti-inflammatory activity of the glandular extracts of Thunnus alalunga
    Azeem, A. K.
    Dilip, C.
    Prasanth, S. S.
    Shahima, V. Junise Hanan
    Sajeev, Kumsr
    Naseera, C.
    [J]. ASIAN PACIFIC JOURNAL OF TROPICAL MEDICINE, 2010, 3 (10) : 794 - 796
  • [6] Baehaki A, 2016, RES J PHARM BIOL CHE, V7, P1994
  • [7] A fish antimicrobial peptide, tilapia hepcidin TH2-3, shows potent antitumor activity against human fibrosarcoma cells
    Chen, Jyh-Yih
    Lin, Wei-Ju
    Lin, Tai-Lang
    [J]. PEPTIDES, 2009, 30 (09) : 1636 - 1642
  • [8] Marine Peptides: Bioactivities and Applications
    Cheung, Randy Chi Fai
    Ng, Tzi Bun
    Wong, Jack Ho
    [J]. MARINE DRUGS, 2015, 13 (07) : 4006 - 4043
  • [9] Antioxidant and Functional Properties of Collagen Hydrolysates from Spanish Mackerel Skin as Influenced by Average Molecular Weight
    Chi, Chang-Feng
    Cao, Zi-Hao
    Wang, Bin
    Hu, Fa-Yuan
    Li, Zhong-Rui
    Zhang, Bin
    [J]. MOLECULES, 2014, 19 (08): : 11211 - 11230
  • [10] Purification and Identification of Antioxidant Peptides from Enzymatic Hydrolysates of Tilapia (Oreochromis niloticus) Frame Protein
    Fan, Jian
    He, Jintang
    Zhuang, Yongliang
    Sun, Liping
    [J]. MOLECULES, 2012, 17 (11): : 12836 - 12850