Correction: Involvement of phenoloxidase in browning during grinding of Tenebrio molitor larvae.
Ontology highlight
ABSTRACT:
SUBMITTER: Janssen RH
PROVIDER: S-EPMC5785002 | biostudies-literature | 2018
REPOSITORIES: biostudies-literature
Publications
Correction: Involvement of phenoloxidase in browning during grinding of Tenebrio molitor larvae.
Janssen Renske H RH Lakemond Catriona M M CMM Fogliano Vincenzo V Renzone Giovanni G Scaloni Andrea A Vincken Jean-Paul JP
PloS one 20180125 1
[This corrects the article DOI: 10.1371/journal.pone.0189685.]. ...[more]
Similar Datasets
Project description:Insects are investigated as alternative protein source to meet the increasing demand for proteins in the future. Enzymatic browning occurring during grinding of insect and subsequent extraction of proteins can influence the proteins' properties, but it is unclear which enzymes are responsible for this phenomenon. This study was performed on larvae of three commonly used insect species, namely Tenebrio molitor, Alphitobius diaperinus and Hermetia illucens. Oxygen consumption measurements on protein extracts showed activity on L-tyrosine, L-3,4-di-hydroxy-phenylalanine (L-DOPA) and L-dopamine, indicating phenoloxidase as a key player in browning. Furthermore, no reaction on 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) was observed, ruling out an important contribution of laccase to browning. The browning reaction was most prominent at pH 6 for T. molitor and A. diaperinus, and 7 for H. illucens. As the enzyme activity of H. illucens was the lowest with the darkest color formation, this was likely caused by another factor. The activity of phenoloxidase was confirmed for T. molitor and A. diaperinus by activity measurements after fractionation by anion-exchange chromatography. Color measurements showed the presence of activity on both L-DOPA and L-tyrosine in the same fractions. Both substrates were converted into dopachrome after incubation with enzyme-enriched fractions. No DOPA-decarboxylase, tyrosine hydroxylase and peroxidase activities were observed. By using native PAGE with L-DOPA as staining-solution, active T. molitor protein bands were resolved and characterized, identifying a tyrosinase/phenoloxidase as the active enzyme species. All together, these data confirmed that tyrosinase is an important enzyme in causing enzymatic browning in T. molitor and likely in A. diaperinus.
| S-EPMC5731683 | biostudies-literature
Project description:The hypothesis tested was that dietary inclusion of insect meal (IM) causes an alteration in the cecal microbiota composition and its fermentation activity of growing pigs. Five-week-old male crossbred pigs were randomly assigned to three groups of 10 pigs each, and fed isonitrogenous diets either without (CON) or with 5% IM (IM5) or 10% IM (IM10) from Tenebrio molitor larvae for four weeks. The relative abundance of the phylum Bacteroidetes was lower in group IM10 than in group CON (p < 0.05), whereas the relative abundance of Firmicutes and the Firmicutes:Bacteroidetes-ratio tended to be higher in groups IM10 and IM5 than in group CON (p < 0.1). The relative abundance of the Proteobacteria tended to be higher in group IM10 than in groups CON and IM5 (p < 0.1). The concentrations of the total short-chain fatty acids in the cecal digesta did not differ between the three groups, but the concentrations of the branched-chain fatty acids in the cecal digesta were higher in group IM5 and IM10 than in group CON (p < 0.05). The present study shows for the first time that the replacement of soybean meal by Tenebrio molitor larvae meal causes a shift of the cecal microbial community and its fermentation activity in growing pigs.
| S-EPMC7401588 | biostudies-literature
Project description:proteome obtained from Tenebrio molitor larvae were collected and analysis
2021-10-14 | PXD029111 |
Project description:Edible insects have recently attracted research attention due to their nutritional value and low environmental footprint. Tenebrio molitor larva was the first insect species to be classified by European Food Safety Authority (EFSA) as safe for human consumption. However, it is thought that the incorporation of edible insect as an ingredient in a food product would be more appealing to consumers than being visible. The aim of the present study was to determine the physicochemical properties of the larvae meal and protein concentrates. Different methods to extract and recover proteins from defatted (DF) Tenebrio molitor larvae were applied; i.e., alkaline extraction (DF-ASP); isoelectric precipitation after alkaline extraction (DF-AIP); and NaCl treatment (DF-SSP), and the obtained protein fractions were characterized. The DF-ASP exhibited the highest protein extraction/recovery efficiency (>60%), while it was the most effective in decreasing the interfacial tension at the oil/water (o/w) interface. The DF-AIP had the highest protein content (75.1%) and absolute values of ζ-potential and the best ability to retain water (10.54 g/g) and stabilize emulsions at pH 3.0. The DF-SSP protein preparation had the highest oil binding capacity (8.62%) and solubility (~88%) at acidic pHs and the highest emulsifying activity (~86 m2/g). Electrophoresis of the protein preparations revealed proteins with different molecular weights, while the protein secondary structure was dominated by β-structures and α-helix. Protein concentrates with different properties were able to be recovered from Tenebrio molitor larvae, that could affect their interactions with other food ingredients and their behavior during processing or storage. These findings would be valuable guidance for the technological exploitation of larvae protein preparations in the development of food formulations.
| S-EPMC9737764 | biostudies-literature
Project description:The amylase from Tenebrio molitor L. larvae (yellow mealworm) was characterized according to a number of its molecular and catalytic properties. The insect amylase is a single polypeptide chain with mol.wt. 68000, an isoelectric point of 4.0 and a very low content of sulphur-containing amino acids. The enzyme is a Ca2+-protein and behaves as an alpha-amylase. Removal of Ca2+ by exhaustive dialysis against water causes the irreversible inactivation of the enzyme. Moreover, the enzyme is activated by the presence in the assay mixture of Cl-, or some other inorganic anions that are less effective than Cl-, and is inhibited by F-. Optimal conditions of pH and temperature for the enzymic activity are 5.8 and 37 degrees C. The insect amylase exhibits an identical kinetic behaviour toward starch, amylose and amylopectin; the enzyme hydrolyses glycogen with a higher affinity constant. Compared with the non-insect alpha-amylases described in the literature, Tenebrio molitor amylase has a lower affinity for starch.
| S-EPMC1172630 | biostudies-other
Project description:The industrial production of Tenebrio molitor L. requires optimized rearing and processing conditions to generate insect biomass with high nutritional value in large quantities. One of the problems arising from processing is a tremendous loss in mineral accessibility, affecting, amongst others, the essential trace element Zn. As a feasible strategy this study investigates Zn-enrichment of mealworms during rearing to meet the nutritional requirements for humans and animals. Following feeding ZnSO4-spiked wheat bran substrates late instar mealworm larvae were evaluated for essential micronutrients and human/animal toxic elements. In addition, growth rate and viability were assessed to select optimal conditions for future mass-rearing. Zn-feeding dose-dependently raised the total Zn content, yet the Znlarvae/Znwheat bran ratio decreased inversely related to its concentration, indicating an active Zn homeostasis within the mealworms. The Cu status remained stable, suggesting that, in contrast to mammals, the intestinal Cu absorption in mealworm larvae is not affected by Zn. Zn biofortification led to a moderate Fe and Mn reduction in mealworms, a problem that certainly can be overcome by Fe/Mn co-supplementation during rearing. Most importantly, Zn feeding massively reduced the levels of the human/animal toxicant Cd within the mealworm larvae, a technological novelty of outstanding importance to be implemented in the future production process to ensure the consumer safety of this edible insect species.
| S-EPMC7674442 | biostudies-literature
Project description:Bacillus thuringiensis (Bt) crystal (Cry) proteins are effective against a select number of insect pests, but improvements are needed to increase efficacy and decrease time to mortality for coleopteran pests. To gain insight into the Bt intoxication process in Coleoptera, we performed RNA-Seq on cDNA generated from the guts of Tenebrio molitor larvae that consumed either a control diet or a diet containing Cry3Aa protoxin. Approximately 134,090 and 124,287 sequence reads from the control and Cry3Aa-treated groups were assembled into 1,318 and 1,140 contigs, respectively. Enrichment analyses indicated that functions associated with mitochondrial respiration, signalling, maintenance of cell structure, membrane integrity, protein recycling/synthesis, and glycosyl hydrolases were significantly increased in Cry3Aa-treated larvae, whereas functions associated with many metabolic processes were reduced, especially glycolysis, tricarboxylic acid cycle, and fatty acid synthesis. Microarray analysis was used to evaluate temporal changes in gene expression after 6, 12 or 24 h of Cry3Aa exposure. Overall, microarray analysis indicated that transcripts related to allergens, chitin-binding proteins, glycosyl hydrolases, and tubulins were induced, and those related to immunity and metabolism were repressed in Cry3Aa-intoxicated larvae. The 24 h microarray data validated most of the RNA-Seq data. Of the three intoxication intervals, larvae demonstrated more differential expression of transcripts after 12 h exposure to Cry3Aa. Gene expression examined by three different methods in control vs. Cry3Aa-treated larvae at the 24 h time point indicated that transcripts encoding proteins with chitin-binding domain 3 were the most differentially expressed in Cry3Aa-intoxicated larvae. Overall, the data suggest that T. molitor larvae mount a complex response to Cry3Aa during the initial 24 h of intoxication. Data from this study represent the largest genetic sequence dataset for T. molitor to date. Furthermore, the methods in this study are useful for comparative analyses in organisms lacking a sequenced genome.
| S-EPMC3338813 | biostudies-literature
Project description:Tenebrio molitor Genome sequencing and assembly
| PRJNA763039 | ENA
Project description:Tenebrio molitor Central Nervous System Transcriptome
| PRJNA608239 | ENA
Project description:Tenebrio molitor Transcriptome or Gene expression
| PRJNA265941 | ENA