Optimization for preparation of collagen peptide with hyaluronidase inhibition activity by response surface method

Authors

HAN Qiu-yu, College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China; Graduate School of Marine Science and Technology, Tokyo University of Marine Science and Technology, Tokyo 1080075, Japan; National Experimental Teaching Demonstration Center for Food Science and Engineering 〔Shanghai Ocean University〕, Shanghai 201306, China
ISHIZAKI Shioichiro, Graduate School of Marine Science and Technology, Tokyo University of Marine Science and Technology, Tokyo 1080075, Japan
BAO Bin, College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China; National Experimental Teaching Demonstration Center for Food Science and Engineering 〔Shanghai Ocean University〕, Shanghai 201306, China

Abstract

Objective: The extraction process of collagen peptides from the skin of swordfish （Xiphias gladius） was optimized in order to efficiently obtain collagen peptides with hyaluronidase inhibition activity by single factor and response surface method. Methods: The response surface method was used to optimize the preparation of collagen peptide with hyaluronidase inhibition activity. In this paper, the enzyme-soluble collagen was extracted from swordfish skin by pepsin, and then the salting-out method was carried out to purify the collagen initially. The specie of collagen was identified by polyacrylamide gel chromatography with 7.5% separation gel. After the basic test carried out by single-factor method according to the degree of hydrolysis and hyaluronidase inhibition rate, the hyaluronidase inhibition rate was selected as the response value for the optimization of hydrolysis conditions of collagen peptide derived from the skin of swordfish via Box-Behnken response surface experimental method. Results: The results showed that the pepsin-soluble collagen was identified as the type I collagen. The optimized hydrolysis conditions for the type I collagen peptide with hyaluronidase inhibition activity were: 6 h of hydrolysis time, 8∶2 of complex enzyme ratio, 32 ℃ of hydrolysis temperature and 6% of enzyme mixture addition. The hyaluronidase inhibition rate of the type I collagen peptide under these conditions was 42.35%. According to the statistical analysis, the response surface model fitted well and there was no significant difference between the predicted and actual values of hyaluronidase inhibition rate （P>0.05）. Conclusion: Therefore, this hydrolysis process could be applied to the production of type I collagen peptide with hyaluronidase inhibition activity derived from the skin of swordfish.

Publication Date

11-28-2021

First Page

142

Last Page

147

DOI

10.13652/j.issn.1003-5788.2021.11.025

Recommended Citation

Qiu-yu, HAN; Shioichiro, ISHIZAKI; and Bin, BAO (2021) "Optimization for preparation of collagen peptide with hyaluronidase inhibition activity by response surface method," Food and Machinery: Vol. 37: Iss. 11, Article 25.
DOI: 10.13652/j.issn.1003-5788.2021.11.025
Available at: https://www.ifoodmm.cn/journal/vol37/iss11/25

References

[1] FAO. The state of world fisheries and aquaculture 2020[M]. FAO: Roma, 2020: 14.
[2] MAEVE H, MARY M C, JIM O. Transforming beef by-products into valuable ingredients: Which spell/recipe to use?[J]. Frontiers in Nutrition, 2016, 3: 53.
[3] 杨子帆, 张科, 刘莹, 等. 鲟鱼和草鱼鱼鳔酶溶性胶原蛋白的理化性质比较[J]. 食品工业科技, 2021, 42（15）: 27-32.
[4] KOIZUMI S, INOUE N, SHIMIZU M, et al. Effects of dietary supplementation with fish scales-derived collagen peptides on skin parameters and condition: A randomized, placebo-controlled, double-blind study[J]. International Journal of Peptide Research & Therapeutics, 2018, 24（3）: 397-402.
[5] KARAYANNAKIDIS P D, CHATZIANTONIOU S E, ZOTOS A. Effects of selected process parameters on physical and sensorial properties of yellowfin tuna （Thunnus albacares） skin gelatin[J]. Journal of Food Process Engineering, 2014, 37（5）: 461-473.
[6] WEIGEL P H, HASCALL V C, TAMMI M. Hyaluronan synthases[J]. Journal of Biological Chemistry, 1997, 272（22）: 13 997-14 000.
[7] NOBLE P W, LAKE F R, HENSON P M, et al. Hyaluronate activation of CD44 induces insulin-like growth factor-1 expression by a tumor necrosis factor-alpha-dependent mechanism in murine macrophages[J]. The Journal of Clinical Investigation, 1993, 91（6）: 2 368-2 377.
[8] CLARE D, SWAISGOOD H. Bioactive milk peptides: A prospectus[J]. Journal of Dairy Science, 2000, 83（6）: 1 187-1 195.
[9] UDENIGWE C C. Bioinformatics approaches, prospects and challenges of food bioactive peptide research[J]. Trends in Food Science & Technology, 2014, 36（2）: 137-143.
[10] 李东东. 罗非鱼皮多肽抗皮肤光老化作用研究[D]. 湛江: 广东海洋大学, 2018: 47.
[11] XU Lin-lin, DONG Wen-hong, ZHAO Jie, et al. Effect of marine collagen peptides on physiological and neurobehavioral development of male rats with perinatal asphyxia[J]. Marine Drugs, 2015, 13（6）: 3 653-3 671.
[12] ALEMN A, GMEZ-GUILLN M, MONTERO P. Identification of ace-inhibitory peptides from squid skin collagen after in vitro gastrointestinal digestion[J]. Food Research International, 2013, 54（1）: 790-795.
[13] 杨玉亮, 衣大龙, 刘春雨, 等. 体外模拟消化对牦牛骨胶原蛋白肽抗氧化活性的影响[J]. 食品与发酵工业, 2021, 47（13）: 79-84.
[14] ALEMN A, MARTNEZ-ALVAREZ O. Marine collagen as a source of bioactive molecules: A review[J]. The Natural Products Journal, 2013, 3（2）: 105-114.
[15] VENKATESAN J, ANIL S, KIM S K, et al. Marine fish proteins and peptides for cosmeceuticals: A review[J]. Marine Drugs, 2017, 15（5）: 143.
[16] ARUNKUMAR K, RAJ R, RAJA R, et al. Brown seaweeds as a source of anti-hyaluronidase compounds[J]. South African Journal of Botany, 2021, 139（9）: 470-477.
[17] ARYANI A, SUPRAYITNO E, SASMITO B B, et al. Characterization and identification of charcoal of inedible Kerandang fish （Channa pleurophthalmus Blkr） body parts and potential antiallergenic properties[J]. Veterinary World, 2020, 13（7）: 1 480-1 486.
[18] CHEMISTS A O O A. Official method of analysis of AOAC International[M]. AOAC International: George W. Latimer, Jr. 1995: 314.
[19] LAEMMLI U K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4[J]. Nature, 1970, 227（5 259）: 680-685.
[20] ADLER-NISSEN J. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid[J]. Journal of Agricultural and Food Chemistry, 1979, 27（6）: 1 256-1 262.
[21] MEYER K. The biological significance of hyaluronic acid and hyaluronidase[J]. Physiological Reviews, 1947, 27（3）: 335-359.
[22] BLANCO M, VZQUEZ J A, PREZ-MARTN R I, et al. Hydrolysates of fish skin collagen: An opportunity for valorizing fish industry byproducts[J]. Marine Drugs, 2017, 15（5）: 131.
[23] 曹少谦, 夏珊珊, 刘亮, 等. 马面鱼皮胶原蛋白的提取及其特性研究[J]. 中国食品学报, 2014, 14（10）: 117-123.
[24] 陈涛, 李伟峰. 野生绿鳍马面鲀（Navodon septentrionalis）幼鱼、成鱼肌肉营养成分分析[J]. 黑龙江畜牧兽医, 2018（17）: 185-187.
[25] SADOWSKA M, KOODZIEJSKA I, NIECIKOWSKA C. Isolation of collagen from the skins of Baltic cod （Gadus morhua）[J]. Food Chemistry, 2003, 81（2）: 257-262.
[26] RIGBY B. Amino-acid composition and thermal stability of the skin collagen of the Antarctic ice-fish[J]. Nature, 1968, 219（5 150）: 166-167.
[27] KITTIPHATTANABAWON P, BENJAKUL S, VISESSANGUAN W, et al. Characterisation of acid-soluble collagen from skin and bone of bigeye snapper （Priacanthus tayenus）[J]. Food Chemistry, 2005, 89（3）: 363-372.
[28] KIMURA S, OHNO Y. Fish type i collagen: Tissue-specific existence of two molecular forms, （α1）₂α2 and α1α2α3, in alaska pollack[J]. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1987, 88（2）: 409-413.
[29] DUAN Rui, ZHANFG Jun-jie, DU Xiu-qiao, et al. Properties of collagen from skin, scale and bone of carp （Cyprinus carpio）[J]. Food Chemistry, 2009, 112（3）: 702-706.
[30] SUN Lei-lei, HOU Hu, LI Ba-fang, et al. Characterization of acid-and pepsin-soluble collagen extracted from the skin of Nile tilapia （Oreochromis niloticus）[J]. International Journal of Biological Macromolecules, 2017, 99: 8-14.
[31] AMBIGAIPALAN P, AL-KHALIFA A S, SHAHIDI F. Antioxidant and angiotensin I converting enzyme （ACE） inhibitory activities of date seed protein hydrolysates prepared using Alcalase, Flavourzyme and Thermolysin[J]. Journal of Functional Foods, 2015,13（B）: 1 125-1 137.
[32] NAKCHUM L, KIM S M. Preparation of squid skin collagen hydrolysate as an antihyaluronidase, antityrosinase, and antioxidant agent[J]. Preparative Biochemistry & Biotechnology, 2016, 46（2）: 123-130.
[33] KUMAR J P, MANDAL B B. Inhibitory role of silk cocoon extract against elastase, hyaluronidase and UV radiation-induced matrix metalloproteinase expression in human dermal fibroblasts and keratinocytes[J]. Photochemical & Photobiological Sciences, 2019, 18（5）: 1 259-1 274.
[34] MAACHE-REZZOUG Z, PIERRE G, NOUVIAIRE A, et al. Optimizing thermomechanical pretreatment conditions to enhance enzymatic hydrolysis of wheat straw by response surface methodology[J]. Biomass and Bioenergy, 2011, 35（7）: 3 129-3 138.
[35] KARKI B, MAURER D, KIM T H, et al. Comparison and optimization of enzymatic saccharification of soybean fibers recovered from aqueous extractions[J]. Bioresource Technology, 2011, 102（2）: 1 228-1 233.