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Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Science & Technology of Food Industry is the property of Science & Technology of Food Industry Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Acta Edulis Fungi is the property of Acta Edulis Fungi and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Expansin(EXP)plays an important role in plant response to environmental stress by regulating cell wall relaxation. To explore the role of EXP genes in soybean response to abiotic stress, two soybean EXP genes (GmEXPB5 and GmEXPB7) and their protein sequences were analyzed by bioinformatics, and their expression levels were detected by real-time fluorescent quantitative PCR(qRT-PCR). The results were as follows: (1)The GmEXPB5 and GmEXPB7 were located on chromosomes 10 and 12 of soybean, and encoded proteins containing 272 and 267 amino acids, respectively. The molecular weight of GmEXPB5 protein was 29.07 kD and the theoretical isoelectric point was 7.51. The molecular weight of GmEXPB7 protein was 29.09 kD and the theoretical isoelectric point was 8.66. Both GmEXPB5 and GmEXPB7 were stable hydrophilic proteins, and localized in the cell wall. Both GmEXPB5 and GmEXPB7 proteins contained a signal peptide sequence and a conserved DPBB_1 structural domain. (2)GmEXPB5 protein had the closest affinity with CaEXPB15 protein of Cicer arietinum, and GmEXPB7 protein was closely related to EXPB3 proteins of Spatholobus suberectus, Vigna angularis and V. unguiculata. (3)GmEXPB5 and GmEXPB7 were expressed in root, stem and leaf of soybean, and their expression levels in root and leaf were significantly higher than those in stem. (4)GmEXPB5 and GmEXPB7 could respond to salt, drought and cold stresses in soybean seedlings. (5)The promoter region of GmEXPB5 contained two types of stress-related cis-elements(ABRE and ARE). The promoter region of GmEXPB7 contained five types of stress-related cis-elements(ABRE, ARE, CGTCA-motif, TC-rich repeats and MBS). In conclusion, these results indicate that GmEXPB5 and GmEXPB7 can participate in the response of soybean to abiotic stress. [ABSTRACT FROM AUTHOR]

Objective To screen and identify new human sperm specific antigen epitopes from candidate sperm-specific antigen epitope peptides using phage display random peptide library technolog and bioinformatics methods. Methods Candidate sperm-specific epitope peptide monomers and trimers were synthesized by solid phase polypeptide synthesis. Dot immunoblotting and enzyme-linked immunosorbent assay (ELISA) were used to detect the immune reaction of the peptides with anti-sperm antibody (ASA) positive serum. ELISA was used to detect antibody titers against candidate sperm-specific epitope peptides in serum of immunized mice. The effects of the sera of the mice immunized with the candidate sperm-specific epitope peptide on human spermatozoa were examined by computer aided sperm analysis. Results High performance liquid chromatography and mass spectrometry showed that the purity and structure of the synthesized candidate sperm-specific epitope peptide were in accordance with the design. Blot and ELISA results indicated that the sperm-specific epitope peptide with the amino acid sequence n-TRRIHRHMTIRR-c and its trimers displayed strong immune response to 17 of 35 ASA positive sera. The serum from mice immunized with the peptide and its trimers significantly attenuated the sperm motility parameters compared with serum from the control group (P < 0. 05), with trimeric-induced decrease in motility parameters being particularly significant. (P<0.01). Conclusion The dodecapeptide with amino acid sequence n-TRRIHRHMTIRR-c is a novel human sperm-specific epitope peptide. [ABSTRACT FROM AUTHOR]

Copyright of Journal of Chinese Institute of Food Science & Technology is the property of Journal of Chinese Institute of Food Science & Technology Periodical Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Acta Edulis Fungi is the property of Acta Edulis Fungi and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Chinese Journal of Preventive Veterinary Medicine / Zhongguo Yufang Shouyi Xuebao is the property of Chinese Journal of Preventive Veterinary Medicine Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Chinese Journal of Preventive Veterinary Medicine / Zhongguo Yufang Shouyi Xuebao is the property of Chinese Journal of Preventive Veterinary Medicine Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Chinese Journal of Preventive Veterinary Medicine / Zhongguo Yufang Shouyi Xuebao is the property of Chinese Journal of Preventive Veterinary Medicine Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Coxsackievirus A10 (CV-A10) is one of the most common pathogens causing hand, foot and mouth disease (HFMD). The 39 candidate epitope peptides covering the amino acid sequence of the VP1 region of CV-A10 were screened by using the overlapping peptide method and verified by indirect enzyme linked immunosorbent assay (ELISA) and microneutralization inhibition assays. It has been found that candidate epitope P6 (amino acid 39~53 in VP1 region of CV-A10) showed high reactivity with CV-A10 virus serum, and still showed neutralizing inhibition effect at 3.91 μg/mL dilution mass concentration, which was a potential neutralizing epitope. P6 antiserum was prepared by immunizing mice with P6 peptide, and microneutralization test was used to verify its protective effect. The results showed a 1:8.97 geometric mean neutralizing titer for P6 antiserum, which identified P6 as the neutralizing epitope of CV-A10. In order to understand the conservativeness of P6 sequence in CV-A10, the amino acid sequence of the P6 was compared with the representative strains of CV-A10 genotype, and the results showed that P6 was highly conserved in CV-A10. It indicated that P6 is a conserved linear neutralization epitope of CV-A10, which has the potential to resist the infection of various genotypes of CV-A10, and can be used as a target for the development of CV-A10 epitope vaccine. This study aimed to screen and identify linearly neutralizing epitopes on the CV-A10 VP1 protein and to lay a foundation for the development of CV-A10 epitope vaccine and HFMD prevention. [ABSTRACT FROM AUTHOR]

Plant-derived peptides have been the high-quality resources of plant protein, because of their natural availability, unique nutritional and physiological functions, particularly without any toxic or side effects. The high protein content can also be balanced in the composition of amino acids. Among them, rapeseed/canola meal is one of the by-products in the extraction of rapeseed oil, while commonly used as animal feed, resulting in low economic benefit. Rapeseed protein hydrolysates have been proven to process antioxidant activity. High-value use of rapeseed protein source is very necessary. Enzymatic hydrolysis can be preferred to produce the bioactive peptides, due to the high specificity, mild conditions, and no by-products. However, the preparation of rapeseed active peptides usually requires the rapeseed protein prior to enzymatic hydrolysis, which is relatively complicated and consumed. Our previous study found that the rapeseed meals with superfine grinding effectively increased their protein dissolution rate. In this study, more attempts were made to directly prepare the active peptides by enzymatic approaches. The raw material was taken as the rapeseed meal powder that was treated with superfine grinding. A comparison was made on the molecular weight distribution and antioxidant activity of the products after rapeseed meal enzymatic hydrolysis by different enzymes. Furthermore, the high-purity antioxidant peptides were purified from the enzymatically hydrolyzed products by membrane separation and Sephadex G-15 column chromatography. The antioxidant activity was evaluated by DPPH (2,2-Diphenyl-1-picrylhydrazyl) radical scavenging capacity, ABTS (2,2’-Azino-bis (3- ethylbenzothiazoline-6-sulfonic acid) radical scavenging capacity, and total antioxidant activity(T-AOC). Finally, the amino acid sequence of the peptide was determined by LC-MS/MS. The results showed that the proteolytic products of rapeseed/canola meal with the higher peptide content were obtained by direct proteolytic hydrolysis of the rapeseed/canola mean ultrafine powder using alkaline protease and flavourzyme. Both hydrolytic products showed better ABTS free radical scavenging and total antioxidant at 1 mg/mL, but the lower DPPH free radical scavenging. Moreover, the hydrolytic products of flavourzyme were mainly composed of small peptides with a molecular weight of less than 1 kDa. The alkaline protease hydrolysis was dominated by peptides from 5 to 10 kDa fractions. The antioxidant activities of peptides were related to their molecular weight distribution. Specifically, the low molecular weight fraction of alkaline protease hydrolysis (＜ 1 kDa) showed better ABTS free radical scavenging at (89.73±0.33)% and total antioxidant activity at (2 669.5±2.82) μmol/g at 1 mg/mL. Furthermore, the active peptide fraction(J3) was achieved using Sephadex G-15 gel filtration chromatography. The peptide content of the J3 fraction was about 32.5%. Five peptides were selected, namely RF, LPF, PAGPF, VF, and LATPF. All five peptides showed a content of over 50% hydrophobic amino acids with phenylalanine as the N-terminal. Specially, RAGPF, VF, and LATPF were newly identified. In summary, the rapeseed meal can be used as a source of prepared antioxidant peptides, which would broaden their applicability. This finding can provide a theoretical reference to further develop the rapeseed/canola meal protein resources through direct enzymatic hydrolysis of rapeseed meal ultra-fine powder. [ABSTRACT FROM AUTHOR]

To investigate the inhibitory mechanism of small peptides on carbohydrate digestion, α-amylase and α-glucosidase inhibitory fractions from the water extract and the gastropancreatic digest of dry-cured ham muscle of Wanzhe spotted pigs were separated, purified, identified, and screened for peptide sequences. And the quantum chemical calculation was used to calculate structural and charge parameters including the distribution and energy of the frontier orbitals, electrostatic charge distribution and bond length, in order to speculate the active sites. It was found that the particle size of ham muscle decreased and its hypoglycemic activity increased after proteolysis. Two (S-I and S-II) and three fractions (WY-I, WY-II and WY-III) were obtained from the water extract and the digest after Sephadex column chromatography, respectively. Using mass spectrometry, 104 peptide sequences consisting of 8–24 amino acids were identified from fraction WY-II and five sequences with Peptide Ranker scores greater than 0.7 were selected. The highest occupied orbitals of the five sequences were mainly distributed in the guanidine groups of arginine and the groups close to the amino-terminal end, while the lowest unoccupied orbitals were in the carboxyl terminals and nearby groups. Sequences with lower ΔEL-H values, GPMGPSGPR, LGFGGPSGPNAGR and APAPAPAPAPPK, might be more active. According to Coulomb’s law, the active sites of these three peptides were located at –C106H108 of arginine, –C10H12 of leucine and –C176H177 of lysine, respectively. This study could provide theoretical support for understanding the blood glucose-regulating mechanism of peptides and the nutritional value of local pig breeds. [ABSTRACT FROM AUTHOR]

[Objective] In this study, previously identified nce-miR-11248 in Nosema ceranae was expressed and verified, its target gene was projected and analyzed, and their expression patterns during the Nosema ceranae infection to Apis mellifera ligustica workers were assessed, aiming to provide references or further exploration of the mechanism underlying N. ceranae infection regulated by nce-miR-11248. [Method] Stem-loop RT-PCR and Sanger sequencing were used to prove the authenticity of nce-miR-1248. Related bioinformatic software were employed to predict its target gene and analyze molecular chaacteristics of the encoded protein. MEME and TBtools were utilized to predict conserved motifs and strutural domains in the encode protein. Multiple alignment of amino acid sequences was conducted by Mega 1.0 software, followed by construction of phylogenetic tree with the neighbor-joining method. The midgut issues of A.m. ligustica workers at 1, 2, 4, 6 and 8 d post N. ceranae infestation were collected. RT-qPCR was used to determine expression profiles of nce-miR-11248 and the target gene. [Result] It was proved hat nce-miR-11248 was truly existed in N. ceranae spores, and the sequence length was 25 bp. The target gene of nce-miR-11248 was SGT1. The molecular formula of SGT1 was C765 H1213N195 O241 S4 with molecular weight of approximately 17.10 ku, its lipolysis coefficient, isoelectric point and hydrophilic coefficient were 82.67, 5.50 and -0.709, respectively. There was no classical signal peptide and transmembrane domain in SGT1, and it simultaneously located in nucleus, mitochondrion and peroxisome. Additionally, SGT1 proeins in N. ceranae, Nosema bombycis, Pancytospora, Encephalitozoon intestinalis and Encephalitozoon romaleae contained four conserved motifs of Motif 1, Motif 2, Motif 3 and Motif 4 and one structural domain of SGT1 superfamily. Furthermore, SGT1 proteins in N. ceranae, N. bombycis, E. intestinalis and E. romaleae were grouped into one cladcand N. ceranae SGT1 and N. bombycis SGT1 had the closest evolutionary distance. As compared to 1 day post N. ceranae inoculation, the expression level of nce-miR-11248 was significantly down-regulated at 2, 4, 6 and 8 days post inoculation (P<0.05), the expression level of SGT1 was down-regulated at 2, 4, 6 and 8 days post inoculation, and the differences in expression level at 4, 6 and 8 days post inoculation reached significant levels (P<0.05). [Conclusion] This study showed that nce-miR-11248 was truly existed in N. ceranae spores. N. ceranae SGT1 and N. bombycis SGT1 had the closest genetic distance. Both nce-miR-11248 and target gene SGT1 presented continuous decreases during the N. ceranae infection to A. m. ligustica workers, and nce-miR-11 248 and SGT1 were poential factors involved in modulation of the microsporidian infection process. [ABSTRACT FROM AUTHOR]

[Objective] The structure and function of yak heart fatty acid binding protein 3 (FABP3) gene were analyzed and its expression levels in adult and fetal yak were detected to provide references for xploring biological functions of the gene in yak breeding. [Method] The FABP3 gene was amplified by PCR from heart tissue of Meiren yak, and bioinformatics analysis was carried out after the CDS region was obtained. The expression levels of FABP3 in heart, liver, spleen, lung, kidney, and muscle tissues of adult and fetal yak were detected by real-time quantitative PCR (RT-qPCR). [Result] The length of the coding egion of FABP3 was 402 bp, encoding 133 amino acids. The advanced structure of the protein included mainly β-turn and extended chain. There was no transmembrane region or signal peptide on yak FABP3 protein, indicating it was a stable protein with certain hydrophilicity. Homology analysis of the nucleotide and amino acid sequences of the CDS region showed that the FABP3 gene was conserved in cattle. Accordng to the phylogenetic tree, yak had the closest genetic relationship with wild yak and zebu, and the farhest genetic relationship with chicken. RT-qPCR results showed that the FABP3 gene was expressed in heart, liver, spleen, lung, kidney, and muscle tissues of adult and fetal yak. The expression in liver, spleen, kidney, and muscle of fetal cattle was significantly or extremely significantly higher than that of adult yak, and the expression level in lung of adult yak was significantly higher than that of fetal yak. [Conclusion] The FABP3 gene of yak was cloned, and its tissue expression pattern was explored. This study provided asic data for further study on the role of FABP3 in fat deposition. [ABSTRACT FROM AUTHOR]

The paper was to explore the biological function of the antimicrobial peptide Caerin 2.1, and to analyze the characteristics of the antimicrobial peptide Caerin 2.1 by the online bioinformatics software. The results showed that Caerin 2.1, an antimicrobial peptide derived from bombesin, was composed of 25 amino acids and was a cationic polypeptide. Its secondary structure mainly contained an α -helix, a few β structures and irregular curls. Its theoretical isoelectric point was 9.99, and its net charge was +2. It was stable, hydrophobic, expressed intracellularly and had three phosphorylation sites. The study indicates that the prediction analysis of Caerin 2.1 can provide information basis for modification of natural antimicrobial peptides to obtain stable and safe alternatives to antibiotics. [ABSTRACT FROM AUTHOR]

[Objective] This study investigated molecular structure, expression characteristics and function of the HTRA gene in Takifugu fasciatus and explored the correlation between HTRA gene and puffer growth. [Method] The 3 UTR, 5 UTR and intermediate fragments of HTRA gene were separately amplified by segmental cloning, the full-length cDNA sequence was obtained after splicing, and bioinformatics analysis was performed. The expression pattern of the HTRA gene in 10 tissues including brain, kidney, liver, spleen, heart, ovary, midgut, gill, skin and muscle and 8 tissues of ovary at 5 different developmental stages (I -V)including brain, kidney, liver, spleen, heart, midgut, gill and muscle was analyzed by quantitative real-time PCR technology. Finally, Sanger sequencing was used to screen the SNP loci related to growth traits in the coding region of HTRA. [Result] The cDNA full-length sequence of HTRA gene in largemouth bass was 2 302 bp in length with a 1 170 bp open reading frame encoding 389 amino acids and 5 exons. The amino acid sequence alignment and phylogenetic tree analysis showed that T. fasciatus had the highest identity (99.53%) with Takifugu rubripes. Spatial structure of HTRi protein showed that it was conserved in fish. The HTRA gene was expressed in 10 different tissues. The highest expression level was in brain, followed by midgut, and the lowest expression was in muscle tissue. The HTRA gene was expressed in 8 different tissues of the ovary at five different developmental periods, with the highest expression in the IV period of ovarian development. A synonymous mutant SNP locus (c.1202 C>G) at 1 202 bp in exon A of the HTRA gene of T. fasciatus was screened and association analysis showed that the SNP loci had significant correlation (P< 0.05) with fatness in T. fasciatus. Individuals with CC genotype had higher fatness than others. [Conclusion] The HTRA gene played important roles in the growth and development of T. fasciatus. It can be used as a candidate gene and molecular maker for selection of new varieties. [ABSTRACT FROM AUTHOR]

Copyright of Science & Technology of Food Industry is the property of Science & Technology of Food Industry Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Bioinformatics software was used to predict the potential antigenic epitopes of G3 subunit A1b acidic polypeptide chain in glycinin. Three pairs of primers were designed and synthesized according to the overlapping amino acid sequence of A1b polypeptide chain, and the cloning vector of the target fragment was constructed. The target protein was expressed by phage display technology, and the heat-processed antibody was prepared and the destroyed antigenic epitopes were identified by ELISA. The results showed that G3A1b may contain 7 linear epitopes: 27QQN29,39LKPDNRIE46,58NNK60,114PQQKGQSSRP123,134R, 174QMPR177,184NQEQEF189. The size of the target gene matched expectations,the cloning vector was successfully constructed and the phage was successfully assembled. G3A1b-3 fragment had high antigenicity and was most obviously destroyed in the process. The results provide theoretical support for the precise positioning of the key amino acids in glycinin G3A1b. [ABSTRACT FROM AUTHOR]

Histones are the basic structural proteins that make up chromatin. The amino acid sequence of histone H3 is highly conserved, and it plays an important role in maintaining chromatin stability, regulating plant growth and development, and responding to environmental changes. In order to explore the structure and function of the histone H3 gene family in foxtail millet, and lay a theoretical foundation for further research on the biological function of histone H3 in foxtail millet, in this study, 15 histone H3 genes from the xiaomi and Yugu 1(YG1) genomes were identified, and named sequentially as SiH3.1-SiH3.15. Furthermore, comparative and analytical studies were conducted using bioinformatics techniques to investigate the distribution on chromosomes, phylogenetic relationships, gene structure, conserved motifs, conserved domains, promoter cis-acting elements, subcellular localization, and tissue expression patterns of SiH3 genes. The results showed that, except for SiH3.2 and SiH3.13 in xiaomi, and SiH3.10.1 and SiH3.11.1 in YG1, the other genes were located in corresponding positions on chromosomes. Phylogenetic analysis revealed that SiH3 genes could be classified into four categories, with 6, 1, 6, and 2 genes in each category for xiaomi, and 4, 2, 7, and 2 genes in each category for YG1. Genes within the same subgroup in the two varieties exhibited similar gene structure, conserved motifs, and domains. They were localized in the cell nucleus according to subcellular localization. Promoter cis-acting elements were mainly associated with plant growth and development regulation and stress responses. Expression pattern analysis showed that SiH3.7 and SiH3.15, belonging to the H3.3 subgroup, exhibited constitutive high expression in different tissues, with significantly higher expression levels in the spike than in other tissues, indicating their important role in foxtail millet throughout its growth, especially at reproductive stages, and suggesting their significant potential applications in foxtail millet production. [ABSTRACT FROM AUTHOR]

Wall-associated kinases(WAKs) are a unique class of receptor like kinases(RLKs), they play a key role in disease resistance response of host plant. In order to analyze the characteristics and potential functions of WAK gene family in foxtail millet, in this study, WAK gene family was identified in the whole genome of xiaomi by homologous sequence alignment based on the published WAK protein sequences of arabidopsis and rice. The physicochemical properties, gene localization, phylogenetic evolution, conserved domain, and cis-acting elements of WAK genes in foxtail millet were analyzed by TBtools and MEGA. The results showed that a total of 41 WAK family members were identified, they were distributed on chromosomes 1-9 of foxtail millet and encoded 590-1 131 amino acids. The molecular weight of the protein ranged from 65.62 ku to 123.36 ku, and the isoelectric point ranged from 5.18 to 8.49. The proteins of Si3g36660, Si7g23280, and Si8g19780 were hydrophobic, while the others were hydrophilic. Subcellular localization prediction showed that 28 genes were located in the plasma membrane, 6 genes were located in chloroplasts, and the rest of the genes were located in Golgi apparatus, vacuoles, endoplasmic reticulum, and extracellular matrix, respectively. The phylogenetic analysis showed that WAK gene family in foxtail millet, arabidopsis, and rice could be divided into 5 categories, among which Si1g24650 and Os01g26174, Si1g12300 and Os02g02120 had the closest homologous relationship. Among the 8 motifs of foxtail millet WAK gene family, Motif 3, Motif 1, Motif 6, Motif 4, and Motif 5 were conserved. Si1g25040, Si3g10590, Si3g32650, Si4g01670, Si4g02770, Si4g02780, Si5g09950, Si7g06570 and Si7g08090 contained defense and stress response elements. It was suggested that these 9 WAK genes in foxtail millet played an important role in host disease resistance. Based on the analysis of transcriptome data of early infection interaction of Sclerospora graminicola, the expression levels of three genes, Si6g20040, Si7g08090 and Si8g19780, were higher in the resistant variety Jingu 20 than that in the susceptible variety Jingu 21 at the early infection stage of Sclerospora graminicola. At 48 h, the relative expression levels in Jingu 20 and Jingu 21 were significantly different, and the difference ratios were 4.99, 10.46 and 2.04, respectively. The study above indicated that the three genes might play an important role in response to the infection of Sclerospora graminicola. [ABSTRACT FROM AUTHOR]

Broomcorn millet is a gramineous herb with drought resistance, saline-alkali tolerance, barren tolerance, and short growth period. In order to provide candidate genes for stress resistance molecular breeding for broomcorn millet, in this study, on the basis of the previous transcriptome sequencing annotation genes, the NAC protein domain annotated on the chromosome 16 of the broomcorn millet genome was aligned to obtain the gDNA sequence of the PmNAC1 gene. The nucleotide sequence of the broomcorn millet was obtained by PCR amplification and gene cloning. The online software ORF Finder Blast were used to conduct bioinformatics analysis of the physical and chemical properties and structure of the protein encoded by broomcorn millet NAC. The results showed that the full length of the PmNAC1 gene was 1 634 bp, encoding 423 amino acids, without signal peptide and transmembrane structure. The amino acids in the secondary structure were mainly composed of 8 α-helix chains and 14 β-sheet chains, which were hydrophilic proteins. The conserved sites were 73-211 amino acids, and there were 59 phosphorylation sites. The glycosylation site exceeded the horizontal line of 0.5. The phylogenetic tree of NAC amino acid sequence of broomcorn millet transcription factor was constructed. The genetic relationship between PmNAC1 protein and switchgrass CUC2 was the closest, and the genetic variation coefficient of the two was 0.06. [ABSTRACT FROM AUTHOR]

Sorghum glutelin is a storage protein, presenting in the grain of rice, corn, and other cereal crops, it is the general term of the proteins insoluble in pure water, neutral salt solution or alcohol, but soluble in dilute alkali or dilute acid. In order to provide a basis for further study on the function of sorghum glutelin and improvement of grain quality, in this study, the DNA and amino acid sequence data of sorghum glutelin were obtained through the BLAST Phytozome database, and the SbGLUA1(Sobic. 001G143700), SbGLUA2(Sobic. 009G017600), and SbGLUB4(Sobic. 009G007100) genes were identified by bioinformatics methods, and the information of glutelin gene family, gene structure, phylogenetic tree, the expression of glutelin in different genotypes and tissues, as well as the physicochemical properties, transmembrane, secondary and tertiary structure, and protein interaction of glutelin proteins were analyzed. The results showed that most of the glutelin proteins were not secretory proteins, and were hydrophilic proteins with poor fluidity, the secondary structure of SbGLUB4 was mainly random coil and α -helix. The gene domain analysis of glutelin showed that most proteins were conserved. Sorghum glutelin had high homology with wheat gluten. SbGLUB4 was expressed specifically in seeds and increased with seed maturity. There were differences between varieties, that of IS22204 was slightly higher than that of Laohanye; SbGLUA2 was expressed in seeds, spikes, and other organs. The STRING prediction interaction protein showed that SbGLUB4 interacted with several seed storage protein result genes and regulatory genes(such as MYB and bHLH), while SbGLUA2 interacted with DNA helicase and recombinase enzyme, inferring that the function changed. [ABSTRACT FROM AUTHOR]

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Copyright of Modern Food Science & Technology is the property of Editorial Office of Modern Food Science & Technology and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Northwest A & F University - Natural Science Edition is the property of Editorial Department of Journal of Northwest A&F University (Natural Science Edition) and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Xinyang Normal University Natural Science Edition is the property of Journal of Xinyang Normal University Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

WRKY transcription factors(TFs), as plant-specific transcription factors, play significant roles in various biological and abiotic stress. In this study, based on RNA-seq analyses, many differentially expressed grapes WRKY genes with unknown function were found during the process of SO2 fumigation combined with low temperature preservation. Through amino acid sequence homology comparison, VvWRKY70 which had the highest similarity to the amino acid sequence of AtWRKY70 was selected for bioinformatics and expression characteristics analysis. The results of bioinformatics analysis showed that the promoter region of VvWRKY70 gene contained W-box element and the response elements to the hormones such as methyl jasmonate and salicylic acid. VvWRKY70 encoding protein was composed of 322 amino acids with a molecular weight about 36.57 ku and hydrophilic, rich in serine/threonine. The secondary structure was mainly composed of random coil and α -helix. The N-terminal contained a highly conserved WRKY domain, and the C-terminal was a C2HC zinc finger structure, belonging to the third WRKY subfamily. Predictions also showed that VvWRKY70 protein was mainly located in the nucleus and conserved in evolution. Analysis of qRT-PCR showed that the VvWRKY70 expressed in Muscat root, stem, leaf, bud, and fruit. The expression of VvWRKY70 in fruit was up-regulated by SO2 and Botrytis cinerea, and down-regulated by low temperature. These results revealed that VvWRKY70 was probably involved in regulation of the process of plant physiology and fruit development, played a role in the process of SO2 preservation of fruits after harvest, and regulated the biotic and abiotic stress responses during fruit storage. [ABSTRACT FROM AUTHOR]

In this study, the complete cDNA sequence of argininosuccinate synthetase was cloned in the saltwater clam Meretrix meretrix using the rapid amplification of cDNA ends (RACE) approach. The complete MmASS cDNA measures 1588 bp in length with an open reading frame encoding 415 amino acids. The molecular weight of MmASS was 46.81 kD and the theoretical isoelectric point was 5.51. The deduced MmASS protein comprises six conserved sequences, containing the substrate-binding residues for ATP, aspartate and citrulline. The results of the multiple amino acid alignment and the phylogenetic analysis showed that MmASS exhibited high amino acid sequence identity with other species. MmASS also had a close phylogenetic relationship with Sinonovacula constricta. Overall, similar functions might exist in M. meretrix and other species. Predicted subcellular localization suggested that MmASS is a cytosolic enzyme. The expression levels of MmASS were distributed in all of the examined tissues. MmASS was most highly expressed in the gill (P<0.05), followed by the hepatopancreas. These results indicated that MmASS was involved in various physiological activities of different tissues and may play an important role in the immune mechanisms. [ABSTRACT FROM AUTHOR]

In this paper, we propose a new fast alignment-free method for protein sequence similarity and evolution analysis. First, 10 groups of physicochemical properties of amino acids are reduced to 6 principal components using principal component analysis, and the number of amino acids in each protein sequence is used as weights to the scores of the principal components. Then, the amino acid position information is fused to form a 26-dimension feature vector for each protein sequence. Finally, the Euclidean distance is used to measure the similarity and evolutionary distance between protein sequences. The test on three datasets shows that our method can cluster each protein sequence accurately, which illustrates the validity of our method. [ABSTRACT FROM AUTHOR]

Copyright of Journal of Northwest A & F University - Natural Science Edition is the property of Editorial Department of Journal of Northwest A&F University (Natural Science Edition) and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Henan Agricultural Sciences is the property of Editorial Board of Journal of Henan Agricultural Sciences and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Chinese Institute of Food Science & Technology is the property of Journal of Chinese Institute of Food Science & Technology Periodical Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Computer Engineering & Applications is the property of Beijing Journal of Computer Engineering & Applications Journal Co Ltd. and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

To further explore the structure and function of the promoter and protein of human SIRT1 gene, our research used bioinformatic methods to analyze 5′-end promoter, promoter Motif, transcription factor binding sites, CpG island, single-nucleotide polymorphism, phylogenetic homology, physicochemical properties, hydrophilicity/hydrophobicity, secondary/tertiary structure, conserved domain, mutation site, N-glycosylation and phosphorylation sites, interacted proteins and biological function. The number of promoters predicted by TSSW and Neural Network Promoter Prediction database was 3 and 2 respectively. There were 3 Motifs found in the promoter region by using MEME database. The CpG islands were clustered in the 1 600～2 200 bp, which were found by using EMBOSS, MethPrimer and CpG Finder database. PROMO and AliBaba2.1 database showed that there were 22 transcription factors in their promoter regions. And there were 6 transcription factors found that bind to the positive and negative chains by using JASPAR software. Besides, there were differences found in allele frequencies between different ethnic groups by using SNP Function Prediction database. Human SIRT1 gene is located at chromosome 10q21.3 and widely distributed in different tissues, which is a hydrophilic and unstable protein with a high conservation among different species. The domain is located at the 254～489 amino acid sequence, belonging to the SIR2 superfamily, mainly located in the nucleus and mitochondria. The secondary structure of the protein mainly contains α-helices and irregular coiling. Compared with AlphaFold2, the tertiary structure model constructed by SWISS-MODEL database was reliable. SIRT1 contained 106 mutation sites, 1 N-glycosylation and 61 phosphorylation sites, which interacted with EP300, TP53 and other proteins. It also participated in circadian rhythm process, steroid hormone response, and intracellular receptor signaling etc., which were associated with longevity regulation pathway, AMPK signaling pathway, and FoxO signaling pathway etc. This study can provide a theoretical basis for further studying the effects on inflammatory reaction and other diseases of human SIRT1 gene. [ABSTRACT FROM AUTHOR]

Alfalfa(Medicago sativa L.) contains various nutrients such as protein and vitamins, and is also an important forage widely planted worldwide. However, the infection of alfalfa leaf curl virus(ALCV) seriously affects the quality and yield of alfalfa. In this study, in order to provide some insights for antiviral breeding in the alfalfa industry, and also provide a theoretical basis for the prevention and control of alfalfa virus diseases. ALCV infection in alfalfa samples with leaf curling and shrinking symptoms in the Botanical Garden of Shanxi Agricultural University, Taigu district, Jinzhong city, Shanxi province was detected, by using the geminivirus universal primer(SPG1/SPG2), and the complete sequence of coat protein(CP) gene of ALCV-Taigu was further cloned and compared by PCR technology. The results showed that the nucleotide homology and amino acid homology of the ALCV-Taigu CP gene with other strains of ALCV were 82.7%–96.6% and 82.4%–97.1%, respectively. The phylogenetic analysis of the amino acid sequence of ALCV-Taigu CP showed that it was far from ALCV isolates from the European countries such as France, Spain, Italy, and the Middle Eastern countries such as Lebanon and Iran, and had a distant genetic relationship. ALCV-Taigu was relatively closed to ALCV isolates from China and Argentina, clustered into a large branch, and had a close genetic relationship. ALCV-Taigu isolate and Chinese alfalfa of ALCV-Helinger/N1 isolate were closely related and clustered together. This was the first time that ALCV had been detected on alfalfa in Shanxi. This study helped to gain a deeper understanding of the molecular evolution of ALCV. [ABSTRACT FROM AUTHOR]

【Objective】 The pathogenicity and genomic differences between two Ralstonia solanacearum strains were compared to analyze the key genes leading to the differences, and help the control of tobacco bacterial wilt disease in the future.【Method】 Different R. solanacearum strains were isolated and purified from tobacco plants infected with bacterial wilt disease. The infestation tests were conducted to compare pathogenicity differences and the genomes of two strains were obtained by high-throughput sequencing technique to analyze the sequence difference, to explore the key genes affecting the pathogenicity of the strains. 【Result】 Two strains RsTP2 and RsTY2 were isolated from diseased tobacco plants in Guangchang county and Nanfeng county of Fuzhou, Jiangxi Province. egl gene sequencing results revealed that both strains were sequevar 13 belonged to Asian phylotype I. The infestation test results indicated that strain RsTP2 was more aggressive to Yunyan87 tobacco plants, in contrast to less pathogenicity of strain RsTY2. Draft genome maps of strains RsTP2 and RsTY2 (5.43 MB and 5.23 MB, respectively) were obtained by high-throughput sequencing technique. Then, the gene and protein sequences were compared with relevant databases to obtain gene function and species annotation information. Through analysis, it was found that 52 proteins of RsTY2 and 44 proteins of RsTP2 were different in the alignment with similarity between 50% and 99.88%. Most of the differential proteins were lectin-like protein, followed by cytolysin secretory activator protein and perforin family protein. 【Conclusion】 By comparing the genomic sequences of strains RsTP2 and RsTY2 with different pathogenicity, it was found that there were significant differences in the coding sequences of lectin-like protein, cytolysin secretory activator protein and perforin family protein. These proteins mainly participated in bacterial adhesion, membrane lysis and penetration, and other functions, which were closely related to the ability of bacteria to invade host cells. The differences in these types of coding proteins are speculated to be one of the important factors leading to the differences in pathogenicity in strains RsTP2 and RsTY2. [ABSTRACT FROM AUTHOR]

Copyright of South China Fisheries Science is the property of South China Fisheries Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of China Brewing is the property of China Brewing Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

BACKGROUND: Collagen peptide is a low molecular active peptide obtained by hydrolysis of collagen. It can be digested and absorbed, and participate in protein synthesis and metabolism in the human body. It has a positive effect on skin health. However, the absorption and delivery mechanism of collagen peptides is not completely clear, and another problem is its low bioavailability. OBJECTIVE: To explore the potential measures to increase the bioavailability of collagen peptides for promoting skin health. METHODS: The articles related to the preparation, composition, digestion and bioavailability of collagen peptide, skin structure, photoaging and natural aging, transport mechanism of collagen peptide by oral in vivo, transdermal absorption mechanism of collagen peptide, and synergistic absorption of collagen peptide with other substances, were searched on ScienceDirect, PubMed, CNKI, Sci-Hub, and Baidu Academic Database from January 2009 to March 2022. The main keywords used were “collagen, collagen peptide, preparation of collagen peptide, photoaging, percutaneous absorption of collagen peptide” in Chinese and “collagen, collagen peptide, preparation of collagen peptide, photoaging, oral absorption” in English. Finally, 82 articles were included for review. RESULTS AND CONCLUSION: (1) Photoaging and natural aging cause skin tissue damage. Collagen peptides can be transported to the skin through the blood after oral gastrointestinal digestion, and build skin tissue through internal molecular mechanisms, and can also be absorbed through the skin surface to have a positive effect on the dermis. (2) At present, the bioavailability of oral collagen peptide is low, and its delivery mechanism is mainly concentrated in the gastrointestinal stage, and there is also the problem of excessive epidermal resistance in percutaneous absorption. (3) The source, amino acid composition, peptide sequence, molecular weight and dosage of collagen peptide and synergistic absorption with different substances or enzyme cofactors should be paid more attention, looking for more high-quality delivery carriers to improve the bioavailability of collagen peptides. (4) For percutaneous absorption, advanced technology or improved physical and chemical methods should be applied to reduce skin physical resistance or improve molecular penetration efficiency. (5) In future, both oral and percutaneous absorption of collagen peptide could be used to recover skin tissue problems caused by photoaging and natural aging more quickly and effectively. [ABSTRACT FROM AUTHOR]

【Objective】Doublesex, a member of the DMRT gene family, plays a key role in controlling sex-specific differentiation. To clone the Open Reading Frame (ORF) of Macrobrachium rosenbergii Doublesex (MrDsx) gene, construct the recombinant plasmid and induce its expression, purify and obtain the recombinant protein MrDsx, will provides basic information for further study of MrDsx function. 【Method】Based on the ORF sequence of MrDsx, the recombinant plasmid pET-32a-MrDsx was obtained by ligating the specific PCR product with the expression vector pET-32a (+). The recombinant plasmid pET-32a-MrDsx was transformed into the competent cells of Escherichia coli BL21 (DE3) to construct the prokaryotic expression cells of MrDsx. The isopropyl-beta-D-thiogalactoside (IPTG) was used to induce the expression of positive transformed cells, and the induced recombinant protein was detected by SDS-PAGE, Western blot and mass spectrometry analysis.【Result】Using the gonad cDNA as template, a single DNA band with the size of about 660 bp was obtained by the specific PCR primers of MrDsx. And the MrDsx ORF sequence was confirmed by sequencing. The recombinant protein MrDsx could be obtained from the transformed competent cells after induction by IPTG at 37℃ for 4 h. When the final concentration of IPTG was 0.1-0.5 mmol/L, the expression level of recombinant protein MrDsx reached its peak. Soluble analysis showed that the recombinant protein MrDsx was mainly expressed in the form of inclusion bodies. After solubilization with 8 mol/L urea, Ni purification, and dialysis renaturation, a single band was detected at the relative molecular weight of 55 kD by SDS-PAGE and Western blot, indicating that the recombinant protein MrDsx could be specifically recognized by His-tag mouse monoclonal antibody. The results of mass spectrometry analysis showed that the fragmented peptide was consistent with the theoretical amino acid sequence, and the matching degree was 100%. 【Conclusion】The recombinant plasmid pET-32a-MrDsx was successfully obtained by prokaryotic expression of MrDsx. High purity active MrDsx protein can be obtained by the dissolution, purification and renaturation. This study provides a preliminary basis for the subsequent study of MrDsx gene function, screening of interacting proteins and elucidation of sex regulation mechanisms in M. rosenbergii. [ABSTRACT FROM AUTHOR]

Copyright of Journal of Chongqing University of Technology (Natural Science) is the property of Chongqing University of Technology and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Acta Agriculturae Zhejiangensis is the property of Acta Agriculturae Zhejiangensis Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Given that wet experimental methods were no longer adequate for the rapid identification of bitter peptides, this paper presented Bitter-Fus, a novel predictive deep learning method incorporating traditional manual features and pre-trained deep features. Firstly, the method automatically extracted deep learning features from peptide sequences using a pre-trained protein sequence language model, then fed the deep learning features into a long short-term memory (LSTM) network for dimensionality reduction to retain the most relevant features. Finally, the reduced-dimensional deep features were fused with the manual features composed of traditional amino acids composition (AAC) method and passed into the feedforward neural network to construct a prediction model. The validation experimental results showed that the prediction method Bitter-Fus obtained an accuracy precision value of 0. 902 and a Mathews correlation coefficient value of 0. 805 in a 10-fold cross-validation, and an accuracy precision value of 0. 930 and a Mathews correlation coefficient value of 0. 862 in the independent dataset test, which significantly outperformed the current state-of-the-art bitter peptide prediction methods BERT4Bitter and iBitter-SCM. [ABSTRACT FROM AUTHOR]

To investigate whether the expression of the chloroplast gene Iborf56 in sweet potato is induced by salt stress and its effect on growth and development, and provide a reference for sweet potato breeding, in this study, the sweet potato variety, Chestnut Fragrance, was used as the research material to clone the Iborf56 gene. The protein sequence features, subcellular localization prediction, phylogenetic analysis, regulatory element analysis, expression patterns under different tissues and salt stress were analyzed using bioinformatics methods, and qPCR was used to validate the expression level of Iborf56. The results showed that Iborf56 had a 99.28% similarity with known sequences from NCBI and an open reading frame length of 929 bp, encoding 60 amino acids with 8 phosphorylation sites. The Iborf56 protein lacked signal peptides and transmembrane regions and did not possess the characteristics of secreted proteins. It was mainly composed of α-helices and its subcellular localization was in the chloroplast stroma. Phylogenetic tree analysis showed that Iborf56 had the closest genetic distance to Ipomoea trifida and Ipomoea triloba. Promoter element analysis revealed that the promoter region of this gene contained functional elements such as light response, stress response, and hormone response. Transcriptome and qRT-PCR quantitative analysis showed that the expression level of Iborf56 was the highest in sweet potato leaves and increased significantly with growth time, inferring that this gene may be involved in the growth and development of sweet potatoes. In addition, the expression level of the Iborf56 gene showed an upward trend first and then a downward trend with increasing salt stress time, and the critical value was reached after 12 h under salt stress, indicating that it may be involved in the salt stress response of sweet potatoes. [ABSTRACT FROM AUTHOR]