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Current Nutrition & Food Science

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ISSN (Print): 1573-4013
ISSN (Online): 2212-3881

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Research Article

Selar (Selar crumenophthalmus) Fish Protein Hydrolysate Has Antidiabetic Properties Possibly through GLP-1

Author(s): Rio J. Kusuma*, Aviria Ermamilia, Salehah N. Halimah, Ninda F. Pradani and Imroatus Sholikha

Volume 17, Issue 5, 2021

Published on: 09 October, 2020

Page: [516 - 522] Pages: 7

DOI: 10.2174/1573401316999201009145146

Price: $65

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Abstract

Background: Enzymatic hydrolysis of fish protein using protease or fish protein hydrolysate can form bioactive peptides that have antidiabetic activity. One potential mechanism of fish protein hydrolysate is reducing blood glucose through increased endogenous glucagon like peptide (GLP)-1 production. Tempeh is soy fermented food that has protease which is potential biocatalyst in producing fish protein hydrolysate.

Objective: To evaluate the antidiabetic properties of Selar (Selar crumenophthalmus) fish protein hydrolysate using tempeh protease as biocatalyst and duodenal gene expression of GLP-1.

Methods: Selar fish protein isolate was digested for 8 hours at 37°C using crude tempeh protease. Diabetes mellitus was induced in rats by intraperitoneal injection of streptozotosin (65 mg/kg bw) and nicotinamide (230 mg/kg bw). Fish protein isolate and hydrolysate in dose of 300 mg/bw and 500 mg/ bw were orally administered daily for 4 weeks. Blood was drawn for fasting serum glucose and lipid profile analysis. Total RNAs were isolated from duodenum and quantitative real time PCR was performed to quantify mRNA expression of GLP-1. Data were analyzed using one way ANOVA and gene expression analysis were performed using Livak.

Results and Discussion: There is a significant difference on fasting serum glucose, total cholesterol, triglyceride, LDL-cholesterol, HDL-cholesterol and duodenal GLP-1 mRNA expression level between groups (p<0.05). The duodenal GLP-1 mRNA expression was the highest in rats who received hydrolyzed fish protein 500 mg/ bw.

Conclusion: Hydrolysis of selar fish protein using tempeh protease has anti-diabetic properties possibly through GLP-1 production.

Keywords: Diabetes mellitus, fish protein isolate, tempeh, crude protease, fish protein hydrolysate, GLP-1.

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[1]
Ginter E, Simko V. Type 2 diabetes mellitus, pandemic in 21st century. Adv Exp Med Biol 2012; 771: 42-50.
[http://dx.doi.org/10.1007/978-1-4614-5441-0_6] [PMID: 23393670]
[2]
Jaacks LM, Siegel KR, Gujral UP, Narayan KMV. Type 2 diabetes: a 21st century epidemic. Best Pract Res Clin Endocrinol Metab 2016; 30(3): 331-43.
[http://dx.doi.org/10.1016/j.beem.2016.05.003] [PMID: 27432069]
[3]
Unnikrishnan R, Pradeepa R, Joshi SR, Mohan V. Type 2 diabetes: demystifying the global epidemic. Diabetes 2017; 66(6): 1432-42.
[http://dx.doi.org/10.2337/db16-0766] [PMID: 28533294]
[4]
Zimmet PZ. Diabetes and its drivers: the largest epidemic in human history? Clin Diabetes Endocrinol 2017; 3(1): 1.
[http://dx.doi.org/10.1186/s40842-016-0039-3] [PMID: 28702255]
[5]
Kanter JE, Bornfeldt KE. Impact of diabetes mellitus. Arterioscler Thromb Vasc Biol 2016; 36(6): 1049-53.
[http://dx.doi.org/10.1161/ATVBAHA.116.307302] [PMID: 27225786]
[6]
Maffi P, Secchi A. The burden of diabetes: emerging data. Dev Ophthalmol 2017; 60: 1-5.
[http://dx.doi.org/10.1159/000459641] [PMID: 28427059]
[7]
Papatheodorou K, Banach M, Bekiari E, Rizzo M, Edmonds M. Complications of Diabetes 2017. J Diabetes Res 2018; 2018: 3086167.
[8]
Association AD. 1. Strategies for improving care. Diabetes Care 2016; 39(Suppl. 1): S6-S12.
[http://dx.doi.org/10.2337/dc16-S004] [PMID: 26696683]
[9]
Bansal N. Prediabetes diagnosis and treatment: a review. World J Diabetes 2015; 6(2): 296-303.
[http://dx.doi.org/10.4239/wjd.v6.i2.296] [PMID: 25789110]
[10]
Golden SH, Maruthur N, Mathioudakis N, et al. The case for diabetes population health improvement: evidence-based programming for population outcomes in diabetes. Curr Diab Rep 2017; 17(7): 51.
[http://dx.doi.org/10.1007/s11892-017-0875-2] [PMID: 28567711]
[11]
Abdel-Megeid AA, Attia Ael-R, Elmarasy SS, Ibrahim AMA. Effect of different types of fish on rats suffering from diabetes. Nutr Health 2008; 19(4): 257-71.
[http://dx.doi.org/10.1177/026010600801900402] [PMID: 19326733]
[12]
Lavigne C, Tremblay F, Asselin G, Jacques H, Marette A. Prevention of skeletal muscle insulin resistance by dietary cod protein in high fat-fed rats. Am J Physiol Endocrinol Metab 2001; 281(1): E62-71.
[http://dx.doi.org/10.1152/ajpendo.2001.281.1.E62] [PMID: 11404223]
[13]
Tremblay F, Lavigne C, Jacques H, Marette A. Dietary cod protein restores insulin-induced activation of phosphatidylinositol 3-kinase/Akt and GLUT4 translocation to the T-tubules in skeletal muscle of high-fat-fed obese rats. Diabetes 2003; 52(1): 29-37.
[http://dx.doi.org/10.2337/diabetes.52.1.29] [PMID: 12502490]
[14]
Jacques H. Dietary cod protein improves the IGF1-Akt/PKB signaling pathway in rat skeletal Muscle during Recovery from Injury. Int J Food Nutr Sci 2015; 2(2): 140-6.
[15]
Madani Z, Louchami K, Sener A, Malaisse WJ, Ait Yahia D. Dietary sardine protein lowers insulin resistance, leptin and TNF-α and beneficially affects adipose tissue oxidative stress in rats with fructose-induced metabolic syndrome. Int J Mol Med 2012; 29(2): 311-8.
[PMID: 22085913]
[16]
Oishi Y, Dohmoto N. Alaska pollack protein prevents the accumulation of visceral fat in rats fed a high fat diet. J Nutr Sci Vitaminol (Tokyo) 2009; 55(2): 156-61.
[http://dx.doi.org/10.3177/jnsv.55.156] [PMID: 19436142]
[17]
van Woudenbergh GJ, van Ballegooijen AJ, Kuijsten A, et al. Eating fish and risk of type 2 diabetes: a population-based, prospective follow-up study. Diabetes Care 2009; 32(11): 2021-6.
[http://dx.doi.org/10.2337/dc09-1042] [PMID: 19675200]
[18]
Xun P, He K. Fish Consumption and incidence of diabetes: meta-analysis of data from 438,000 individuals in 12 independent prospective cohorts with an average 11-year follow-up. Diabetes Care 2012; 35(4): 930-8.
[http://dx.doi.org/10.2337/dc11-1869] [PMID: 22442398]
[19]
Tian S, Xu Q, Jiang R, Han T, Sun C, Na L. Dietary protein consumption and the risk of type 2 diabetes: a systematic review and meta-analysis of cohort studies. Nutrients 2017; 9(9): 982.
[20]
Dale HF, Jensen C, Hausken T, et al. Effect of a cod protein hydrolysate on postprandial glucose metabolism in healthy subjects: a double-blind cross-over trial. J Nutr Sci 2018; 7: e33. [published correction appears in J Nutr Sci 2019; 8: e1]
[http://dx.doi.org/10.1017/jns.2018.23] [PMID: 30524707]
[21]
Xia EQ, Zhu SS, He MJ, Luo F, Fu CZ, Zou TB. Marine peptides as potential agents for the management of type 2 diabetes mellitus-a prospect. Mar Drugs 2017; 15(4): 88.
[http://dx.doi.org/10.3390/md15040088] [PMID: 28333091]
[22]
Kehinde BA, Sharma P. Recently isolated antidiabetic hydrolysates and peptides from multiple food sources: a review. Crit Rev Food Sci Nutr 2020; 60(2): 322-40.
[PMID: 30463420]
[23]
Nobile V, Duclos E, Michelotti A, Bizzaro G, Negro M, Soisson F. Supplementation with a fish protein hydrolysate (Micromesistius poutassou): effects on body weight, body composition, and CCK/GLP-1 secretion. Food Nutr Res 2016; 60: 29857-7.
[http://dx.doi.org/10.3402/fnr.v60.29857] [PMID: 26829186]
[24]
Barus T, Wati L. Melani, Suwanto A, Yogiara. Diversity of protease-producing Bacillus spp. from fresh Indonesian tempeh based on 16S rRNA gene sequence. Hayati J Biosci 2017; 24(1): 35-40.
[http://dx.doi.org/10.1016/j.hjb.2017.05.001]
[25]
Sugimoto S, Fujii T, Morimiya T, Johdo O, Nakamura T. The fibrinolytic activity of a novel protease derived from a tempeh producing fungus, Fusarium sp. BLB. Biosci Biotechnol Biochem 2007; 71(9): 2184-9.
[http://dx.doi.org/10.1271/bbb.70153] [PMID: 17827689]
[26]
Slizyte R, Rommi K, Mozuraityte R, Eck P, Five K, Rustad T. Bioactivities of fish protein hydrolysates from defatted salmon backbones. Biotechnol Rep (Amst) 2016; 11: 99-109.
[http://dx.doi.org/10.1016/j.btre.2016.08.003] [PMID: 28352546]
[27]
Wang X, Yu H, Xing R, Li P. Characterization, preparation, and purification of marine bioactive peptides. BioMed Res Int 2017; 2017: 9746720.
[http://dx.doi.org/10.1155/2017/9746720] [PMID: 28761878]
[28]
Tian Y, Wang W, Yuan C, Zhang L, Liu J, Liu J. Nutritional and digestive properties of protein isolates extracted from the muscle of the common carp using pH-shift processing. J Food Process Preserv 2017; 41(1): e12847.
[http://dx.doi.org/10.1111/jfpp.12847] [PMID: 28239212]
[29]
Li B, Matter E, Hoppert H, Seeley R, Sandoval D. Identification of optimal reference genes for RT-qPCR in the rat hypothalamus and intestine for the study of obesity. Int J Obes 2005; 38(2): 192-7.
[30]
Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-delta delta C(T)) method. Methods 2001; 25(4): 402-8.
[http://dx.doi.org/10.1006/meth.2001.1262] [PMID: 11846609]
[31]
Team J. JASP (Version 0.9) 2018.https://jasp-stats.org/
[32]
Ryan JT, Ross RP, Bolton D, Fitzgerald GF, Stanton C. Bioactive peptides from muscle sources: meat and fish. Nutrients 2011; 3(9): 765-91.
[http://dx.doi.org/10.3390/nu3090765] [PMID: 22254123]
[33]
Nardo AE, Añón MC, Parisi G. Large-scale mapping of bioactive peptides in structural and sequence space. PLoS One 2018; 13(1): e0191063.
[http://dx.doi.org/10.1371/journal.pone.0191063]
[34]
Nielsen SD, Beverly RL, Qu Y, Dallas DC. Milk bioactive peptide database: a comprehensive database of milk protein-derived bioactive peptides and novel visualization. Food Chem 2017; 232: 673-82.
[http://dx.doi.org/10.1016/j.foodchem.2017.04.056] [PMID: 28490127]
[35]
Wang J, Yin T, Xiao X, He D, Xue Z, Jiang X, et al. StraPep: a structure database of bioactive peptides. Database 2018. Available at: https://academic.oup.com/database/article/doi/10.1093/database/bay038/4974332
[http://dx.doi.org/10.1093/database/bay038]
[36]
Priatni S, Ratnaningrum D, Kosasih W, et al. Protein and fatty acid profile of marine fishes from Java Sea, Indonesia. Biodiversitas (Surak) 2018; 19(5): 1737-42.
[http://dx.doi.org/10.13057/biodiv/d190520]
[37]
Ktari N, Mnafgui K, Nasri R, et al. Hypoglycemic and hypolipidemic effects of protein hydrolysates from zebra blenny (Salaria basilisca) in alloxan-induced diabetic rats. Food Funct 2013; 4(11): 1691-9.
[http://dx.doi.org/10.1039/c3fo60264h] [PMID: 24104463]
[38]
Cudennec B, Fouchereau-Peron M, Ferry F, Duclos E, Ravallec R. In vitro and in vivo evidence for a satiating effect of fish protein hydrolysate obtained from blue whiting (Micromesistius poutassou) muscle. J Funct Foods 2012; 4(1): 271-7.
[http://dx.doi.org/10.1016/j.jff.2011.12.003]
[39]
Harnedy PA, Parthsarathy V, McLaughlin CM, O’Keeffe MB, Allsopp PJ, McSorley EM, et al. Blue whiting (Micromesistius poutassou) muscle protein hydrolysate with in vitro and in vivo antidiabetic properties. J Funct Foods 2018; 40: 137-45.
[http://dx.doi.org/10.1016/j.jff.2017.10.045]
[40]
Gevrey JC, Malapel M, Philippe J, et al. Protein hydrolysates stimulate proglucagon gene transcription in intestinal endocrine cells via two elements related to cyclic AMP response element. Diabetologia 2004; 47(5): 926-36.
[http://dx.doi.org/10.1007/s00125-004-1380-0] [PMID: 15085339]
[41]
Huang S-L, Jao C-L, Ho K-P, Hsu K-C. Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates. Peptides 2012; 35(1): 114-21.
[http://dx.doi.org/10.1016/j.peptides.2012.03.006] [PMID: 22450467]
[42]
Afifah DN, Rustanti N, Anjani G, Syah D. Yanti, Suhartono MT. Proteomics study of extracellular fibrinolytic proteases from Bacillus licheniformis RO3 and Bacillus pumilus 2.g isolated from Indonesian fermented food. IOP Conf Ser Earth. Environ Sci (Ruse) 2017; 55: 012025.
[43]
Heskamp M-L, Barz W. Expression of proteases by Rhizopus species during tempeh fermentation of soybeans. Food Nahr 1998; 42(01): 23-8.
[http://dx.doi.org/10.1002/(SICI)1521-3803(199802)42:01<23::AID-FOOD23>3.0.CO;2-3]
[44]
Nauck M. Incretin therapies: highlighting common features and differences in the modes of action of glucagon-like peptide-1 receptor agonists and dipeptidyl peptidase-4 inhibitors. Diabetes Obes Metab 2016; 18(3): 203-16.
[http://dx.doi.org/10.1111/dom.12591] [PMID: 26489970]
[45]
Liu Y, Beyer A, Aebersold R. On the dependency of cellular protein levels on mRNA abundance. Cell 2016; 165(3): 535-50.
[http://dx.doi.org/10.1016/j.cell.2016.03.014] [PMID: 27104977]

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