Effect of enzymatic hydrolysis on bioactive properties and allergenicity of cricket (Gryllodes sigillatus) protein

Felicia Hall, Philip E. Johnson, Andrea Liceaga

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Food-derived bioactive peptides have gained attention for their role in preventing chronic diseases. Edible insects are viable sources of bioactive peptides owing to their high protein content and sustainable production. In this study, whole crickets (Gryllodes sigillatus) were alcalase-hydrolyzed to a degree of hydrolysis (DH) ranging from 15 to 85%. Antioxidant activity, angiotensin converting enzyme (ACE), and dipeptidyl peptidase-4 (DPP-IV)- inhibition of the cricket protein hydrolysates (CPH) were evaluated before and after simulated gastrointestinal digestion (SGD). Antioxidant activity was similar among CPH, whereas ACE and DPP-IV inhibition was greater (p < 0.05) in CPH with 60–85% DH. Bioactivity improved after SGD. CPH allergenicity was evaluated using human shrimp-allergic sera. All sera positively reacted to tropomyosin in the unhydrolyzed cricket and CPH with 15–50% DH, whereas 60–85% DH showed no reactivity. In conclusion, CPH (60–85% DH) had the greatest bioactive potential and lowest reactivity to tropomyosin, compared with other CPH and the unhydrolyzed control.

Original languageEnglish (US)
Pages (from-to)39-47
Number of pages9
JournalFood Chemistry
Volume262
DOIs
StatePublished - Oct 1 2018

Fingerprint

Gryllodes sigillatus
Protein Hydrolysates
Gryllidae
allergenicity
Enzymatic hydrolysis
enzymatic hydrolysis
protein hydrolysates
bioactive properties
Hydrolysis
hydrolysis
Proteins
proteins
Tropomyosin
Peptidyl-Dipeptidase A
tropomyosins
peptidyl-dipeptidase A
Antioxidants
Subtilisins
Dipeptidyl Peptidase 4
Digestion

Keywords

  • ACE inhibition
  • Allergenicity
  • Antioxidant
  • Bioactive properties
  • Cricket protein hydrolysates
  • DPP-IV inhibition

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science

Cite this

Effect of enzymatic hydrolysis on bioactive properties and allergenicity of cricket (Gryllodes sigillatus) protein. / Hall, Felicia; Johnson, Philip E.; Liceaga, Andrea.

In: Food Chemistry, Vol. 262, 01.10.2018, p. 39-47.

Research output: Contribution to journalArticle

@article{ac0d4bf96ef041cc9afb980cf8b4be89,
title = "Effect of enzymatic hydrolysis on bioactive properties and allergenicity of cricket (Gryllodes sigillatus) protein",
abstract = "Food-derived bioactive peptides have gained attention for their role in preventing chronic diseases. Edible insects are viable sources of bioactive peptides owing to their high protein content and sustainable production. In this study, whole crickets (Gryllodes sigillatus) were alcalase-hydrolyzed to a degree of hydrolysis (DH) ranging from 15 to 85{\%}. Antioxidant activity, angiotensin converting enzyme (ACE), and dipeptidyl peptidase-4 (DPP-IV)- inhibition of the cricket protein hydrolysates (CPH) were evaluated before and after simulated gastrointestinal digestion (SGD). Antioxidant activity was similar among CPH, whereas ACE and DPP-IV inhibition was greater (p < 0.05) in CPH with 60–85{\%} DH. Bioactivity improved after SGD. CPH allergenicity was evaluated using human shrimp-allergic sera. All sera positively reacted to tropomyosin in the unhydrolyzed cricket and CPH with 15–50{\%} DH, whereas 60–85{\%} DH showed no reactivity. In conclusion, CPH (60–85{\%} DH) had the greatest bioactive potential and lowest reactivity to tropomyosin, compared with other CPH and the unhydrolyzed control.",
keywords = "ACE inhibition, Allergenicity, Antioxidant, Bioactive properties, Cricket protein hydrolysates, DPP-IV inhibition",
author = "Felicia Hall and Johnson, {Philip E.} and Andrea Liceaga",
year = "2018",
month = "10",
day = "1",
doi = "10.1016/j.foodchem.2018.04.058",
language = "English (US)",
volume = "262",
pages = "39--47",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier Limited",

}

TY - JOUR

T1 - Effect of enzymatic hydrolysis on bioactive properties and allergenicity of cricket (Gryllodes sigillatus) protein

AU - Hall, Felicia

AU - Johnson, Philip E.

AU - Liceaga, Andrea

PY - 2018/10/1

Y1 - 2018/10/1

N2 - Food-derived bioactive peptides have gained attention for their role in preventing chronic diseases. Edible insects are viable sources of bioactive peptides owing to their high protein content and sustainable production. In this study, whole crickets (Gryllodes sigillatus) were alcalase-hydrolyzed to a degree of hydrolysis (DH) ranging from 15 to 85%. Antioxidant activity, angiotensin converting enzyme (ACE), and dipeptidyl peptidase-4 (DPP-IV)- inhibition of the cricket protein hydrolysates (CPH) were evaluated before and after simulated gastrointestinal digestion (SGD). Antioxidant activity was similar among CPH, whereas ACE and DPP-IV inhibition was greater (p < 0.05) in CPH with 60–85% DH. Bioactivity improved after SGD. CPH allergenicity was evaluated using human shrimp-allergic sera. All sera positively reacted to tropomyosin in the unhydrolyzed cricket and CPH with 15–50% DH, whereas 60–85% DH showed no reactivity. In conclusion, CPH (60–85% DH) had the greatest bioactive potential and lowest reactivity to tropomyosin, compared with other CPH and the unhydrolyzed control.

AB - Food-derived bioactive peptides have gained attention for their role in preventing chronic diseases. Edible insects are viable sources of bioactive peptides owing to their high protein content and sustainable production. In this study, whole crickets (Gryllodes sigillatus) were alcalase-hydrolyzed to a degree of hydrolysis (DH) ranging from 15 to 85%. Antioxidant activity, angiotensin converting enzyme (ACE), and dipeptidyl peptidase-4 (DPP-IV)- inhibition of the cricket protein hydrolysates (CPH) were evaluated before and after simulated gastrointestinal digestion (SGD). Antioxidant activity was similar among CPH, whereas ACE and DPP-IV inhibition was greater (p < 0.05) in CPH with 60–85% DH. Bioactivity improved after SGD. CPH allergenicity was evaluated using human shrimp-allergic sera. All sera positively reacted to tropomyosin in the unhydrolyzed cricket and CPH with 15–50% DH, whereas 60–85% DH showed no reactivity. In conclusion, CPH (60–85% DH) had the greatest bioactive potential and lowest reactivity to tropomyosin, compared with other CPH and the unhydrolyzed control.

KW - ACE inhibition

KW - Allergenicity

KW - Antioxidant

KW - Bioactive properties

KW - Cricket protein hydrolysates

KW - DPP-IV inhibition

UR - http://www.scopus.com/inward/record.url?scp=85046139656&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85046139656&partnerID=8YFLogxK

U2 - 10.1016/j.foodchem.2018.04.058

DO - 10.1016/j.foodchem.2018.04.058

M3 - Article

C2 - 29751919

AN - SCOPUS:85046139656

VL - 262

SP - 39

EP - 47

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

ER -