A comparative study on the functional properties of mealworm (Tenebrio molitor) larvae and soybean protein isolates and hydrolysates

Oh E., . and Yu X., . and Kim Y., . A comparative study on the functional properties of mealworm (Tenebrio molitor) larvae and soybean protein isolates and hydrolysates. pp. 816-826. ISSN 22317546

The present work aimed to compare the functional and antioxidant properties of mealworm larvae and soybean proteins at different processing steps. The mealworm larvae protein isolate (MPI) was hydrolysed with 2 alcalase at pH 8 and 60C for 3 h to produce mealworm protein hydrolysate (MPH). The content of amino acids were higher in MPI than in soybean protein isolates (SPI) except for those of threonine arginine glutamic acid and serine. MPI contained a higher amount of hydrophobic amino acids (941.4 mol/L) than hydrophilic amino acids (697.1 mol/L). The emulsifying activity stability and fat absorption capacity of MPI were higher than those of SPI whereas their water absorption and holding capacities were similar. Alcalase hydrolysis increased MPI solubility. MPI showed lower solubility at pH 3 - 9 than that of SPI whereas MPH had higher solubility than that of soy protein hydrolysate (SPH). The foam expansion capacity and foam stability of MPI were lower than those of SPI but hydrolysis improved those of MPI. MPI formed a gel at pH 5 7 and 9 at 15 concentration or at pH 7 and 9 at 10 concentration. However MPH showed no gel formation under any conditions. The total phenolic content and antioxidant capacity of MPI were higher than those of SPI. The DPPH activity of MPH (70) was higher than that of MPI (18) SPI (12) or SPH (34). MPI can be used as an alternative to SPI. Alcalase hydrolysis can increase the antioxidant effect digestibility and functionality of MPI as a sustainable ingredient in high value-added products.

Full text available from: Official URL: http://www.ifrj.upm.edu.my/28%20(04)%202021/DONE%2...

Abstract

The present work aimed to compare the functional and antioxidant properties of mealworm larvae and soybean proteins at different processing steps. The mealworm larvae protein isolate (MPI) was hydrolysed with 2 alcalase at pH 8 and 60C for 3 h to produce mealworm protein hydrolysate (MPH). The content of amino acids were higher in MPI than in soybean protein isolates (SPI) except for those of threonine arginine glutamic acid and serine. MPI contained a higher amount of hydrophobic amino acids (941.4 mol/L) than hydrophilic amino acids (697.1 mol/L). The emulsifying activity stability and fat absorption capacity of MPI were higher than those of SPI whereas their water absorption and holding capacities were similar. Alcalase hydrolysis increased MPI solubility. MPI showed lower solubility at pH 3 - 9 than that of SPI whereas MPH had higher solubility than that of soy protein hydrolysate (SPH). The foam expansion capacity and foam stability of MPI were lower than those of SPI but hydrolysis improved those of MPI. MPI formed a gel at pH 5 7 and 9 at 15 concentration or at pH 7 and 9 at 10 concentration. However MPH showed no gel formation under any conditions. The total phenolic content and antioxidant capacity of MPI were higher than those of SPI. The DPPH activity of MPH (70) was higher than that of MPI (18) SPI (12) or SPH (34). MPI can be used as an alternative to SPI. Alcalase hydrolysis can increase the antioxidant effect digestibility and functionality of MPI as a sustainable ingredient in high value-added products.

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Item Type:	Article
AGROVOC Term:	Tenebrio molitor
AGROVOC Term:	Larvae
AGROVOC Term:	Protein isolates
AGROVOC Term:	Protein hydrolysate
AGROVOC Term:	Sampling
AGROVOC Term:	Kjeldahl method
AGROVOC Term:	Statistical analysis
AGROVOC Term:	Analysis of variance
AGROVOC Term:	Energy production
AGROVOC Term:	Antioxidants
Depositing User:	Mr. AFANDI ABDUL MALEK
Last Modified:	24 Apr 2025 00:55
URI:	http://webagris.upm.edu.my/id/eprint/10004

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