Enzymatic hydrolysis of insect<i>Alphitobius diaperinus</i>towards the development of bioactive peptide hydrolysates

Sousa, Pedro; Borges, Sandra; Pintado, Manuela

doi:10.1039/d0fo00188k

Cited by 42 publications

(43 citation statements)

References 54 publications

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“…The combination of Flavourzyme TM 500L and Alcalase TM 2.4L (run 4) resulted in an increase of 62% in ABTS radical scavenging activity of the protein hydrolysates compared to the control sample. The antioxidant activity values were higher than those obtained for lesser mealworm ( Alphitobius diaperinus) hydrolyzed with Alcalase 2.5L (E:S ratio of 1.5% for 4 hr) and Corolase PP (E:S ratio of 3% for 6 hr), in which both hydrolysates presented ABTS radical scavenging activities of approximately 95 µmol TEq g −1 (Sousa, Borges, & Pintado, 2020).…”

Section: Resultsmentioning

confidence: 77%

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Enzymatic hydrolysis of black cricket (Gryllus assimilis) proteins positively affects their antioxidant properties

Matos

Novelli

Castro

2021

Journal of Food Science

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The development of innovative ingredients through biotechnological routes has established insect proteins as an emerging source of bioactive peptides. The current study aimed to evaluate the antioxidant properties of black cricket (Gryllus assimilis) protein hydrolysates produced using the proteases FlavourzymeTM 500L, AlcalaseTM 2.4L, and NeutraseTM 0.8L, either individually or in binary/ternary combinations. The enzymatic hydrolysis promoted an increase of approximately 160% in total antioxidant capacity and 93% in the ferric reducing antioxidant power. The isolated use of the enzyme FlavourzymeTM 500L showed the most prominent positive effect on the antioxidant properties, presenting an IC50 value of 455 and 71 µg/mL for DPPH and ABTS radicals scavenging activities, respectively. This sample was composed mainly of small peptides (MW < 3 kDa), in which the antioxidant properties increased after fractionation by ultrafiltration. Gel electrophoresis analysis showed protein hydrolysates composed mainly of polypeptide chains with a mass of less than 14 kDa. Finally, the enzymatic treatment proved to be an efficient process to improve the antioxidant properties of black cricket proteins, increasing the possibility of applying these hydrolysates as bioactive ingredients in food or nutraceutical products.Practical ApplicationInsects represent an alternative source of proteins. Their modification through hydrolysis allows for the acquisition of compounds with great potential in industrial applications, such as functional ingredients or for nutraceutical purposes. The use of our experimental design proved to be an adequate tool for defining the best process conditions required for increasing the attainment of biologically active compounds.

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Section: Resultsmentioning

confidence: 77%

“…According to Sousa et al. (2020), the antioxidant properties of peptides are associated with their amino acid composition. Hydrophobic amino acids, such as alanine, valine, isoleucine, leucine, proline, and methionine, have electrons that can be donated to eliminate free radicals.…”

Section: Resultsmentioning

confidence: 99%

Enzymatic hydrolysis of black cricket (Gryllus assimilis) proteins positively affects their antioxidant properties

Matos

Novelli

Castro

2021

Journal of Food Science

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“…Enzymatic hydrolysis was realized using alcalase enzyme according to Sousa et al [35] with modifications. The enzyme/substrate (E:S) ratio was fixed at 1:10 (w/w) and the reaction was done under agitation 100 rpm at 55 • C, pH 8.0, for 180 min.…”

Section: Enzymatic Hydrolysis and Combined Treatmentsmentioning

confidence: 99%

Effect of Physical and Enzymatic Pre-Treatment on the Nutritional and Functional Properties of Fermented Beverages Enriched with Cricket Proteins

Dridi¹,

Millette

Aguilar

et al. 2021

Foods

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The aim of this study was to evaluate the effects of γ-irradiation (IR), ultrasound (US), and combined treatments of ultrasound followed by γ-irradiation (US-IR), ultrasound followed by enzymatic hydrolysis with and without centrifugation (US-E and US-EWC, respectively), and ultrasound followed by γ-irradiation and enzymatic hydrolysis (US-IRE), on the digestibility and the nutritional value of fermented beverages containing probiotics. Results showed that US (20 min), IR (3 kGy) and US-IR (tUS = 20 min, dose = 3 kGy) treatments raised protein solubility from 11.5 to 21.5, 24.3 and 29.9%, respectively. According to our results, these treatments were accompanied by the increased amount of total sulfhydryl groups, surface hydrophobicity and changes to the secondary structure of the proteins measured by Fourier-transform infrared spectroscopy (FTIR). Fermented probiotic beverages, non-enriched (C) and enriched with untreated (Cr) or treated cricket protein with combined treatments were also evaluated for their in vitro protein digestibility. Results showed that the soluble fraction of US-IRE fermented beverage had the highest digestibility (94%) as compared to the whole fermented tested beverages. The peptides profile demonstrated that US-IRE had a low proportion of high molecular weight (MW) peptides (0.7%) and the highest proportion of low MW peptides by over 80% as compared to the other treatments.

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“…Investigations on techno-functional properties including solubility, water- and oil-binding capacity, foaming capacity, surface hydrophobicity, gelling properties, coagulation properties, and the emulsifying ability of various insect powders, and their protein extracts have already shown promising outcomes [ 29 , 30 , 31 , 32 , 33 , 34 , 35 ]. In addition, enzymatic hydrolysis of the protein extracts could efficiently enhance their functionalities and obtain bioactive peptides with antioxidative, antihypertensive, antidiabetic, and antimicrobial properties [ 36 , 37 , 38 , 39 , 40 , 41 , 42 ]. Regarding studies in emulsions stabilized with insect proteins, Wang et al [ 43 ] reported a superior performance of black soldier fly ( Hermetia illucens ) protein concentrate on emulsifying a high fraction (40 wt%) of lemon oil compared to whey protein isolate (WPI), and Gould and Wolf [ 44 ] found that sunflower oil emulsions stabilized with mealworm protein displayed smaller droplet size and a lower protein concentration was required compared to WPI; in addition, the produced emulsion also showed great stability under wide environmental stresses (temperature at −20 °C and 60–90 °C, pH 3–8 and ionic strength 80–330 mM).…”

Section: Introductionmentioning

confidence: 99%

Polyphenol Loaded W1/O/W2 Emulsions Stabilized with Lesser Mealworm (Alphitobius diaperinus) Protein Concentrate Produced by Membrane Emulsification: Stability under Simulated Storage, Process, and Digestion Conditions

Wang

Ballon

Schroën

et al. 2021

Foods

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Water-in-oil-in-water (W1/O/W2) emulsions are complex delivery systems for polyphenols amongst other bio-actives. To stabilize the oil–water interphase, dairy proteins are commonly employed, which are ideally replaced by other, more sustainable sources, such as insect proteins. In this study, lesser mealworm (Alphitobius diaperinus) protein concentrate (LMPC) is assessed and compared to whey protein (WPI) and pea protein (PPI), to stabilize W1/O/W2 emulsions and encapsulate a commercial polyphenol. The results show that LMPC is able to stabilize W1/O/W2 emulsions comparably to whey protein and pea protein when using a low-energy membrane emulsification system. The final droplet size (d4,3) is 7.4 μm and encapsulation efficiency is between 72 and 74%, regardless of the protein used. Under acidic conditions, the LMPC shows a similar performance to whey protein and outperforms pea protein. Under alkaline conditions, the three proteins perform similarly, while the LMPC-stabilized emulsions are less able to withstand osmotic pressure differences. The LMPC stabilized emulsions are also more prone to droplet coalescence after a freeze–thaw cycle than the WPI-stabilized ones, but they are the most stable when exposed to the highest temperatures tested (90 °C). The results show LMPC’s ability to stabilize multiple emulsions and encapsulate a polyphenol, which opens the door for application in foods.

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Enzymatic hydrolysis of insectAlphitobius diaperinustowards the development of bioactive peptide hydrolysates

Abstract: Edible insects are a promising protein source for the future generation, due to their nutritional composition, sustainability and low environmental impact.

Cited by 42 publications

References 54 publications

Enzymatic hydrolysis of black cricket (Gryllus assimilis) proteins positively affects their antioxidant properties

Enzymatic hydrolysis of black cricket (Gryllus assimilis) proteins positively affects their antioxidant properties

Effect of Physical and Enzymatic Pre-Treatment on the Nutritional and Functional Properties of Fermented Beverages Enriched with Cricket Proteins

Polyphenol Loaded W1/O/W2 Emulsions Stabilized with Lesser Mealworm (Alphitobius diaperinus) Protein Concentrate Produced by Membrane Emulsification: Stability under Simulated Storage, Process, and Digestion Conditions

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