Extraction and physicochemical characterization of Tenebrio molitor proteins

Azagoh, Christiane; Ducept, Fabrice; Garcia, Rebeca; Rakotozafy, Lalatiana; Keller, Séverine; Lewandowski, Richard; Mezdour, Samir

doi:10.1016/j.foodres.2016.06.010

Cited by 109 publications

(91 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…These results are in accordance with studies reporting considerable low solubility of insect protein flours derived from mealworm larvae (3-45%; pH 2-9), black soldier fly larvae (10-35%; pH 2-9), house cricket (12-23%, pH 3-9) and tropical banded cricket (5-25%; pH 3-10), especially at weak acidic conditions [20,23,33]. In contrast, Azagoh et al [22] observed higher protein solubility of flour from mealworm larvae between 40-76% from pH 2-10.…”

Section: Protein Solubilitysupporting

confidence: 91%

“…For mealworm (Tenebrio molitor) and black soldier fly larvae (Hermetia illucens), protein solubilities between 3 and 95% were observed and found to be significantly influenced by the solvent pH, purity of the protein fraction and previous processing [20][21][22]. However, near the isoelectric point (IP) around pH 3 to 7-which reflects the common pH range of many food products-the protein solubility was lowest, especially for non-purified insect flours [20,22,23]. Protein solubility of untreated, defatted and acid-hydrolysed mealworm and silkworm pupae (Bombyx mori) flour were reported to range between 12 and 13% at pH 7.6 [24].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Purschke

Meinlschmidt

Horn

et al. 2017

Eur Food Res Technol

106

View full text Add to dashboard Cite

Enzymatic hydrolysis of migratory locust (Locusta migratoria L.) protein flour (MLPF) was investigated as a method to improve the techno-functional properties. Experiments were conducted under variation of the applied proteases (Alcalase, Neutrase, Flavourzyme, Papain) or combinations thereof, enzyme-substrate ratio (0.05-1.0% w/w), heat pre-treatment (60-80 °C; 15-60 min), and hydrolysis time (0-24 h). Protein degradation was monitored in terms of degree of hydrolysis (DH) and SDS-PAGE. Solubility, emulsifying, foaming and water/oil binding properties of the hydrolysates were determined. In comparison to the control (DH = 5%), hydrolysis resulted in considerably higher DH values up to 42%. SDS-PAGE profiles revealed a steady decrease of bands between 25 and 75 kDa and an increase of low molecular weight bands (10-15 kDa). However, different heat pre-treatments resulted in impaired hydrolytic cleavage as evidenced by lower DH values. Protein solubility of MLPF hydrolysates was improved over a broad pH range from initially 10-22% up to 55% at alkaline conditions. Furthermore, hydrolysis resulted in enhanced emulsifying activity (54%) at pH 7, improved foamability (326%) at pH 3 and advanced oil binding capacity. The results of this study have clearly demonstrated the potential of targeted enzymatic degradation to improve the techno-functionality of migratory locust protein in order to produce tailored insect-based ingredients for the use in food applications.

show abstract

Section: Protein Solubilitysupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Purschke

Meinlschmidt

Horn

et al. 2017

Eur Food Res Technol

106

View full text Add to dashboard Cite

show abstract

“…CP bands, mostly appearing below 35 kDa, did not separate clearly on the gel and suggest the presence of cuticular proteins with molecular weights of 14-30 kDa . For NC, major groups of protein bands were noted at 8-15 kDa, 15-31 kDa, and 31-72 kDa, as previously reported by Yi et al (2013) and Azagoh et al (2016) for protein extracted from whole yellow mealworm. Bands at 8.5-13 kDa are due to anti-freeze, including hemolymph, proteins (12 kDa), those at 14-32 kDa suggest the presence of soluble cuticular proteins in NC, and bands at 32-95 kDa are related to enzymatic and muscle proteins (Yi et al, 2013).…”

Section: In Silico Parameters Of Yellow Mealworm Proteins As Precursupporting

confidence: 83%

“…ducted with proteins extracted from defatted yellow mealworm flour. andAzagoh et al (2016) reported protein contents of 79% and 84%, respectively, for yellow mealworm proteins extracted at alkaline pH at 40 and 45°C. The former is lower than other mealworm protein contents in the literature Zhao, Vázquez-Gutiérrez, Johansson, Landberg, and Langton (2016).…”

mentioning

confidence: 99%

Bioinformatics of edible yellow mealworm (Tenebrio molitor) proteome reveal the cuticular proteins as promising precursors of dipeptidyl peptidase‐IV inhibitors

et al. 2019

View full text Add to dashboard Cite

Bioinformatics was applied for strategic processing of yellow mealworm (Tenebrio molitor) proteins to produce dipeptidyl peptidase (DPP)-IV inhibiting peptides. In silico analysis of 384 mealworm proteins revealed structural proteins as better precursors of DPP-IV inhibiting peptides, compared with other protein types, after pepsin and papain hydrolysis. This was associated with the higher hydropathicity and amounts of residues associated with DPP-IV inhibition in the structural (cuticular) proteins. In silico, the peptides were mostly released with pepsin than papain. Cuticular (CP) and non-cuticular proteins (NC) were extracted from yellow mealworm and hydrolyzed with pepsin and papain in vitro to validate the virtual findings. CP hydrolysate with papain inhibited DPP-IV the most compared to CP hydrolysate with pepsin, whereas NC hydrolysates were mostly inactive. CP had higher hydrophobic-hydrophilic amino acid ratios and contents of the activity-associated residues than NC. The findings demonstrate the application of bioinformatics in processing proteins for bioactive peptide production. S U PP O RTI N G I N FO R M ATI O NAdditional supporting information may be found online in the Supporting Information section.How to cite this article: Dávalos Terán I, Imai K, Lacroix IME, Fogliano V, Udenigwe CC. Bioinformatics of edible yellow mealworm (Tenebrio molitor) proteome reveal the cuticular proteins as promising precursors of dipeptidyl peptidase-IV inhibitors. J Food Biochem. 2020;44:e13121. https ://doi.

show abstract

“…e surface hydrophobicity of WSPC and WSPP was found to be 22.59 ± 0.22 and 15.92 ± 0.21, respectively ( Table 1). From the result, surface hydrophobicity of both insect proteins was lower than the previous report of Azagoh et al [29]. ey reported that surface hydrophobicity of T. molitor larvae meal was 102.5.…”

Section: Surface Hydrophobicity and Sulfhydryl Contentcontrasting

confidence: 54%

Characteristics, Functional Properties, and Antioxidant Activities of Water-Soluble Proteins Extracted from Grasshoppers,Patanga succinctaandChondracris roseapbrunner

Chatsuwan

Nalinanon

Puechkamut

et al. 2018

Journal of Chemistry

View full text Add to dashboard Cite

Water-soluble proteins extracted from two species of grasshoppers, Patanga succincta (WSPP) and Chondracris roseapbrunner (WSPC), were characterized as well as their functional properties and antioxidant activities were investigated. e extraction yield, on a wet weight basis, was 7.35% and 7.46% for WSPP and WSPC, respectively. e most abundant amino acid in both proteins was glutamic acid, followed by aspartic, alanine, and leucine, in that order. e electrophoretic study revealed that proteins with MW of 29, 42, 50, 69, and 146 kDa were the major protein components in WSPP and WSPC. FTIR analysis showed that those proteins remained their structural integrity. e surface hydrophobicity at pH 7 of WSPC was higher than WSPP, but the sulfhydryl group content did not show significant difference between the proteins from two species. Both grasshopper proteins were mostly soluble in strong acidic and alkaline aqueous solutions with a minimum value at pH 4. ose proteins exhibited poor emulsifying properties and foaming capacity, but they had greater foaming stability compared with bovine serum albumin (BSA) (p < 0.05). WSPC showed greater DPPH • and ABTS •+ scavenging activities and ferric-reducing antioxidant power (FRAP) than did WSPP (p < 0.05). erefore, based on characteristics and functional properties, water-soluble proteins from both edible grasshoppers can be used as an ingredient in food applications.

show abstract

Extraction and physicochemical characterization of Tenebrio molitor proteins

Cited by 109 publications

References 33 publications

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Bioinformatics of edible yellow mealworm (Tenebrio molitor) proteome reveal the cuticular proteins as promising precursors of dipeptidyl peptidase‐IV inhibitors

Characteristics, Functional Properties, and Antioxidant Activities of Water-Soluble Proteins Extracted from Grasshoppers,Patanga succinctaandChondracris roseapbrunner

Contact Info

Product

Resources

About