Antioxidant activity of queen bee larvae processed by enzymatic hydrolysis

Abstract

Queen bee larvae (QBL), by‐products of royal jelly processing, was enzymatically hydrolyzed to produce bioactive peptides. Five enzymes were firstly used to obtain hydrolysates which were evaluated for their antioxidative performances. QBL hydrolyzed by pepsin, showing the highest antioxidant resistance, were prepared and isolated by ultrafiltration using different molecular weight cutoffs of <1, 1–5, 5–10, and >10 kDa. Then, hydrolysate III (MW 1–5 kDa) with the highest activity was purified through continuous chromatography. Antioxidant capacities of active peak 3 (P3) to DPPH, hydroxyl, superoxide, ABTS, oxygen radical absorbance capacity radicals assay were 74.31%, 82.44%, 74.53%, 78.81%, and 1,074 μM TE/g, respectively. Finally, the most potent antioxidant hydrolysate was determined through a high‐speed amino acid analyzer. The results of the QBLH for in vitro antioxidant assays have indicated that P3 is a good antioxidative peptide due to its high percentage of hydrophobic amino acids and has vast prospects for future development and application. Practical applications QBL has been used as a traditional medicine for several millennia in China due to its rich nutrition and potent effect in improving human immunity, however, the utilization of QBL resources industry is rather low. This article evaluated the antioxidant activities of queen bee larvae using DPPH, hydroxyl, superoxide, ABTS, ORAC radicals assay, respectively. This article indicates that high antioxidant amino acid residues can be obtained from QBL through simple processing methods (enzymatic hydrolyzing and membrane isolating). Our study could arouse a great interest among researchers to develop a new series of QBL products with high efficient antioxidant properties.

Preparation, antioxidant activity evaluation, and identification of antioxidant peptide from black soldier fly ( Hermetia illucens L.) larvae

“…The BLPHs‐I possessed high content of hydrophobic amino acids, which may contribute to the higher superoxide scavenging activity. It was consistent with a previous study of Dong et al (2017) who demonstrated that the strong superoxide radical scavenging capabilities may be owing to hydrophobic amino acids. The sequence and amino acid composition make a lot of contributions to the antioxidant capabilities.…”

“…The commercial enzymes are used to promote the hydrolysis of protein improve its bioactivity by converting it into peptides while retaining its nutritive value (Moure, Domínguez, & Parajó, 2006). Numerous studies over the recent years have demonstrated the antioxidant properties of hydrolyzed proteins from multiple insects species, such as weaver ant ( Oecophylla smaragdina ) (Pattarayingsakul et al, 2017), male silkmoth (Liu, Wan, Liu, Zou, & Liao, 2017), and queen bee (Dong, Dong, Liu, Lu, & Yu, 2017). However, studies on the antioxidant activity of the BLP hydrolysates (BLPHs) are rarely reported, and few antioxidant sequences of BSF have been reported before.…”

Supplementation with Queen Bee Larva Powder Extended the Longevity of Caenorhabditis elegans

“…Queen bee larva (QBL) is an important edible insect that is harvested for use as by-product of royal jelly production [ 6 ]. In contrast to worker larva, which is fed royal jelly for the first 3 days after hatching, QBL are exclusively fed royal jelly [ 7 ].…”

Characterization of protein hydrolysate from silkworm pupae (Bombyx mori)

“…However, the increasing rate of activity was slightly improved and was constant when the concentration of Alcalase and Flavourzyme hydrolyses was increased to 20–40 mg/ml (Klompong et al, ). In the case of queen bee larvae that had been treated using five enzymes (Trypsin, α‐Chymotrypsin, Pepsin, Papain, and Neutrase), Pepsin showed the best performance of hydrolysis, due to it having the highest antioxidant activity of DPPH (40.42%), hydroxyl (46.82%), superoxide (59.80%), 2,2‐azinobis (3‐ethylbenzothiazoline‐6‐sulfonate) (63.4%), and peroxyl (987 μM Trolox equivalent/g) (Dong, Dong, Liu, Lu, & Yu, ). The antioxidant activity could be affected by the type of protease enzyme, DH (Gibbs, Zougman, Masse, & Mulligan, ), proportion of amino acid (Yang, Yang, Li, Li, & Jiang, ), molecular weight of the peptide (Klompong et al, ), and structure of the peptide (Saito et al, ).…”