Probing the Antioxidant Activity of Functional Proteins and Bioactive Peptides in Hermetia Illucens Larvae Fed with Food Wastes

Abstract Food waste is becoming more prevalent, and managing it is one of the most important issues in terms of food safety. In this study, functional proteins and bioactive peptides produced from the enzymatic digestion of Black soldier fly (Hermetia illucens L., BSF) fed with food wastes were characterized and quantified using proteomics-based analysis.The results revealed approximately 78 peptides and 57 proteins, including 40S ribosomal protein S4, 60S ribosomal protein L8, ATP synthase subunit alpha, ribosomal protein S3, Histone H2A, NADP- glutamate dehydrogenase, Fumarate hydratase, RNA helicase, Chitin binding Peritrophin-A, Lectin C-type protein, etc. were found in BSF. Furthermore, functional analysis of the proteins revealed that the 60S ribosomal protein L5 (RpL5) in BSF interacted with a variety of ribosomal proteins and played a key role in the glycolytic process (AT14039p). Higher antioxidant activity was found in peptide sequences such as GYGFGGGAGCLSMDTGAHLNR, VVPSANRAMVGIVAGGGRIDKPILK, AGLQFPVGR, GFKDQIQDVFK, and GFKDQIQDVFK. It was concluded that the bioconversion of food wastes by Hermetia illucens broght about the generation of variety of functional proteins and bioactive peptides with strong antioxidant activity. However, more studies are required for exploiting potential of Hermetia illucens in value addition of food wastes.

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Interaction of Hsp90 with Ribosomal Proteins Protects from Ubiquitination and Proteasome-dependent Degradation

Molecular Biology of the Cell ◽

10.1091/mbc.e05-08-0713 ◽

2006 ◽

Vol 17 (2) ◽

pp. 824-833 ◽

Cited By ~ 74

Author(s):

Tae-Sung Kim ◽

Chang-Young Jang ◽

Hag Dong Kim ◽

Jae Yung Lee ◽

Byung-Yoon Ahn ◽

...

Keyword(s):

Ribosomal Protein ◽

Molecular Chaperone ◽

Ribosomal Proteins ◽

Heat Shock Protein 90 ◽

Small Subunit ◽

Hsp90 Inhibitors ◽

Ribosomal Protein S6 ◽

Hsp90 Activity ◽

Ribosomal Protein S3 ◽

The Stability

Heat-shock protein 90 (Hsp90) is a molecular chaperone that plays a key role in the conformational maturation of various transcription factors and protein kinases in signal transduction. Multifunctional ribosomal protein S3 (rpS3), a component of the ribosomal small subunit, is involved in DNA repair and apoptosis. Our data show that Hsp90 binds directly to rpS3 and the functional consequence of Hsp90-rpS3 interaction results in the prevention of the ubiquitination and the proteasome-dependent degradation of rpS3, subsequently retaining the function and the biogenesis of the ribosome. Interference of Hsp90 activity by Hsp90 inhibitors appears to dissociate rpS3 from Hsp90, associate the protein with Hsp70, and induce the degradation of free forms of rpS3. Furthermore, ribosomal protein S6 (rpS6) also interacted with Hsp90 and exhibited a similar effect upon treatment with Hsp90 inhibitors. Therefore, we conclude that Hsp90 regulates the function of ribosomes by maintaining the stability of 40S ribosomal proteins such as rpS3 and rpS6.

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Drosophila ribosomal protein S3 contains an activity that cleaves DNA at apurinic/apyrimidinic sites.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)47256-0 ◽

1994 ◽

Vol 269 (41) ◽

pp. 25359-25364

Author(s):

D M Wilson ◽

W A Deutsch ◽

M R Kelley

Keyword(s):

Ribosomal Protein ◽

Ribosomal Protein S3

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Generation of bioactive peptides from lentil protein: degree of hydrolysis, antioxidant activity, phenol content, ACE-inhibitory activity, molecular weight, sensory, and functional properties

Journal of Food Measurement & Characterization ◽

10.1007/s11694-021-01077-4 ◽

2021 ◽

Author(s):

Amir Rezvankhah ◽

Mohammad Saeid Yarmand ◽

Babak Ghanbarzadeh ◽

Homaira Mirzaee

Keyword(s):

Molecular Weight ◽

Antioxidant Activity ◽

Functional Properties ◽

Inhibitory Activity ◽

Bioactive Peptides ◽

Degree Of Hydrolysis ◽

Phenol Content ◽

Ace Inhibitory Activity ◽

Ace Inhibitory

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Assessment of In Vitro Bioaccessibility of Polyphenols from Annurca, Limoncella, Red Delicious, and Golden Delicious Apples Using a Sequential Enzymatic Digestion Model

Antioxidants ◽

10.3390/antiox10040541 ◽

2021 ◽

Vol 10 (4) ◽

pp. 541

Author(s):

Giulia Graziani ◽

Anna Gaspari ◽

Claudio Di Vaio ◽

Aurora Cirillo ◽

Carolina Liana Ronca ◽

...

Keyword(s):

Antioxidant Activity ◽

Antioxidant Activities ◽

In Vitro Digestion ◽

Enzymatic Digestion ◽

Beneficial Effects ◽

Golden Delicious ◽

In Vitro Bioaccessibility ◽

Inflammatory Processes ◽

Great Relevance

Four different varieties of apples have been considered (Limoncella, Annurca, Red Delicious, and Golden Delicious) to estimate the extent of colon polyphenolics release after in vitro sequential enzyme digestion. Since several studies report a positive effect of apple polyphenols in colonic damage, we found of interest to investigate the colon release of polyphenols in different varieties of apples in order to assess their prevention of colonic damage. UHPLC-HRMS analysis and antioxidant activity (ABTS, DPPH, and FRAP assays) were carried out on the apple extracts (peel, flesh, and whole fruit) obtained from not digested samples and on bioaccessible fractions (duodenal and colon bioaccessible fractions) after in vitro digestion. Polyphenolic content and antioxidant activities were found to vary significantly among the tested cultivars with Limoncella showing the highest polyphenol content accompanied by an excellent antioxidant activity in both flesh and whole fruit. The overall trend of soluble antioxidant capacity from the soluble duodenal phase (SDP) and soluble colonic phase (SCP) followed the concentrations of flavanols, procyandinis, and hydroxycinnamic acids under the same digestive steps. Our results highlighted that on average 64.2% of the total soluble antioxidant activity was released in the SCP with Limoncella exhibiting the highest values (82.31, 70.05, and 65.5%, respectively for whole fruit, flesh, and peel). This result suggested that enzymatic treatment with pronase E and viscozyme L, to reproduce biochemical conditions occurring in the colon, is effective for breaking the dietary fiber-polyphenols interactions and for the release of polyphenols which can exercise their beneficial effects in the colon. The beneficial effects related to the Limoncella consumption could thus be of potential great relevance to counteract the adverse effects of pro-oxidant and inflammatory processes on intestinal cells.

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The N-terminal Sequence of Ribosomal Protein L10 from the ArchaebacteriumHalobacterium marismortuiand its Relationship to Eubacterial Protein L6 and Other Ribosomal Proteins

Biological Chemistry Hoppe-Seyler ◽

10.1515/bchm3.1987.368.2.921 ◽

1987 ◽

Vol 368 (2) ◽

pp. 921-926 ◽

Cited By ~ 3

Author(s):

Jan DIJK ◽

Rudolf VAN DEN BROEK ◽

Georgios NASIULAS ◽

Alfred BECK ◽

Richard REINHARDT ◽

...

Keyword(s):

Ribosomal Protein ◽

Ribosomal Proteins ◽

Terminal Sequence

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Halobacterium cutirubrum ribosomes. Properties of the ribosomal proteins and ribonucleic acid

Biochemical Journal ◽

10.1042/bj1300103 ◽

1972 ◽

Vol 130 (1) ◽

pp. 103-110 ◽

Cited By ~ 51

Author(s):

L. P. Visentin ◽

C. Chow ◽

A. T. Matheson ◽

M. Yaguchi ◽

F. Rollin

Keyword(s):

Ribosomal Protein ◽

Ribosomal Proteins ◽

Soluble Fraction ◽

Ribosomal Subunit ◽

23S Rrna ◽

Core Particle ◽

Fractionation Procedure ◽

Additional Protein ◽

70S Ribosome ◽

Low Ionic Strength

1. The 30S ribosomal subunit of the extreme halophile Halobacterium cutirubrum is unstable and loses 75% of its ribosomal protein when the 70S ribosome is dissociated into the two subunits. A stable 30S subunit is obtained if the dissociation of the 70S particle is carried out in the presence of the soluble fraction. 2. A fractionation procedure was developed for the selective removal of groups of proteins from the 30S and 50S subunits. When the ribosomes, which are stable in 4m-K+ and 0.1m-Mg2+, were extracted with low-ionic-strength buffer 75–80% of the 30S proteins and 60–65% of the 50S proteins as well as the 5S rRNA were released. The proteins in this fraction are the most acidic of the H. cutirubrum ribosomal proteins. Further extraction with Li+–EDTA releases additional protein, leaving a core particle containing either 16S rRNA or 23S rRNA and about 5% of the total ribosomal protein. The amino acid composition, mobility on polyacrylamide gels at pH4.5 and 8.7, and the molecular-weight distribution of the various protein fractions were determined. 3. The s values of the rRNA are 5S, 16S and 23S. The C+G contents of the 16S and 23S rRNA were 56.1 and 58.8% respectively and these are higher than C+G contents of the corresponding Escherichia coli rRNA (53.8 and 54.1%).

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An intergenic G-rich region in Leishmania tarentolae kinetoplast maxicircle DNA is a pan-edited cryptogene encoding ribosomal protein S12

Molecular and Cellular Biology ◽

10.1128/mcb.12.1.56-67.1992 ◽

1992 ◽

Vol 12 (1) ◽

pp. 56-67

Author(s):

D A Maslov ◽

N R Sturm ◽

B M Niner ◽

E S Gruszynski ◽

M Peris ◽

...

Keyword(s):

Amino Acid ◽

Ribosomal Protein ◽

Ribosomal Proteins ◽

Sequence Similarity ◽

Rich Region ◽

Leishmania Tarentolae ◽

Significant Sequence Similarity ◽

The Family ◽

Intergenic Regions ◽

Ribosomal Protein S12

Six short G-rich intergenic regions in the maxicircle of Leishmania tarentolae are conserved in location and polarity in two other kinetoplastid species. We show here that G-rich region 6 (G6) represents a pan-edited cryptogene which contains at least two domains edited independently in a 3'-to-5' manner connected by short unedited regions. In the completely edited RNA, 117 uridines are added at 49 sites and 32 uridines are deleted at 13 sites, creating a translated 85-amino-acid polypeptide. Similar polypeptides are probably encoded by pan-edited G6 transcripts in two other species. The G6 polypeptide has significant sequence similarity to the family of S12 ribosomal proteins. A minicircle-encoded gRNA overlaps 12 editing sites in G6 mRNA, and chimeric gRNA/mRNA molecules were shown to exist, in agreement with the transesterification model for editing.

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Mild temperature shock alters the transcription of a discrete class of Saccharomyces cerevisiae genes

Molecular and Cellular Biology ◽

10.1128/mcb.3.3.457-465.1983 ◽

1983 ◽

Vol 3 (3) ◽

pp. 457-465

Author(s):

C H Kim ◽

J R Warner

Keyword(s):

Saccharomyces Cerevisiae ◽

Ribosomal Protein ◽

Ribosomal Proteins ◽

Temperature Shift ◽

Restrictive Temperature ◽

Ribosomal Protein Genes ◽

Wild Type ◽

Temperature Shock ◽

Mild Temperature ◽

Mutant Cells

In Saccharomyces cerevisiae the synthesis of ribosomal proteins declines temporarily after a culture has been subjected to a mild temperature shock, i.e., a shift from 23 to 36 degrees C, each of which support growth. Using cloned genes for several S. cerevisiae ribosomal proteins, we found that the changes in the synthesis of ribosomal proteins parallel the changes in the concentration of mRNA of each. The disappearance and reappearance of the mRNA is due to a brief but severe inhibition of the transcription of each of the ribosomal protein genes, although the total transcription of mRNA in the cells is relatively unaffected by the temperature shock. The precisely coordinated response of these genes, which are scattered throughout the genome, suggests that either they or the enzyme which transcribes them has unique properties. In certain S. cerevisiae mutants, the synthesis of ribosomal proteins never recovers from a temperature shift. Yet both the decline and the resumption of transcription of these genes during the 30 min after the temperature shift are indistinguishable from those in wild-type cells. The failure of the mutant cells to grow at the restrictive temperature appears to be due to their inability to process the RNA transcribed from genes which have introns (Rosbash et al., Cell 24:679-686, 1981), a large proportion of which appear to be ribosomal protein genes.

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Ribosomal protein S14 is altered by two-step emetine resistance mutations in Chinese hamster cells

Molecular and Cellular Biology ◽

10.1128/mcb.3.2.190-197.1983 ◽

1983 ◽

Vol 3 (2) ◽

pp. 190-197

Author(s):

J J Madjar ◽

M Frahm ◽

S McGill ◽

D J Roufa

Keyword(s):

Ribosomal Protein ◽

Ribosomal Proteins ◽

Ribosomal Subunit ◽

Chinese Hamster ◽

Complementation Group ◽

Resistance Mutations ◽

Cho Cell ◽

Ribosomal Subunits ◽

40S Ribosomal Subunit ◽

One Step

Four two-dimensional polyacrylamide gel electrophoresis systems were used to identify 78 Chinese hamster cell ribosomal proteins by the uniform nomenclature based on rat liver ribosomal proteins. The 40S ribosomal subunit protein affected by Chinese hamster ovary (CHO) cell one-step emetine resistance mutations is designated S14 in the standard nomenclature. To seek unambiguous genetic evidence for a cause and effect relationship between CHO cell emetine resistance and mutations in the S14 gene, we mutagenized a one-step CHO cell mutant and isolated second-step mutant clones resistant to 10-fold-higher concentrations of emetine. All of the highly resistant, two-step CHO cell mutants obtained displayed additional alterations in ribosomal protein S14. Hybridization complementation tests revealed that the two-step CHO cell emetine resistance mutants were members of the same complementation group defined by one-step CHO cell mutants, EmtB. Two-step mutants obtained from a Chinese hamster lung cell emetine-resistant clone belong to the EmtA complementation group. The two-step and EmtB mutants elaborated 40S ribosomal subunits, which dissociated to 32S and 40S core particles in buffers containing 0.5 M KCl at 4 degrees C. In contrast, 40S ribosomal subunits purified from all EmtA, one-step EmtB EmtC mutants, and wild-type CHO and lung cells were stable at this temperature in buffers containing substantially higher concentrations of salt. Thus, two-step emtB mutations affect the structure of S14 protein directly and the stability of the 40S ribosomal subunit indirectly.

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