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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.)

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 & Fermentation Industries is the property of Food & Fermentation Industries 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 & Fermentation Industries is the property of Food & Fermentation Industries 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.)

Food taste-modulating peptides mainly interact with salt taste receptor ENaC, TRPV1 or TMC4, umami receptor T1R1/T1R3, sweet receptor T1R2/T1R3, bitter receptor T2R and kokumi receptor CaSR to induce PLCβ2/IP3 or cAMP/PKA pathway to achieve taste transduction. Computer aided analysis techniques such as molecular docking, dynamic simulation, virtual screening and deep learning can efficiently, accurately and widely identify and develop novel taste-modulating peptides, which can effectively promote the high-quality development of nutrition and health food industry. This paper aims to present the latest research progress in the field of taste-modulating peptides, including the human taste perception mechanism, the taste mechanism of food taste-modulating peptides, as well as computer aided analysis techniques. This provides ideas for cost reduction, efficiency enhancement, and subsequent in-depth research in the era of Big Compute and development of new taste-modulating peptide products in the field of food taste-modulating peptides development. [ABSTRACT FROM AUTHOR]

Most of the active proteins and industrial enzymes commonly used in industry, agriculture and medicine are obtained through heterologous expression systems. Pichia pastoris is one of the excellent hosts for expressing heterologous proteins. This expression system has the advantages including good genetic stability, high protein expression and secretory level, post-translational modification system, and low cost etc. However, excessive aggregation of heterologous proteins usually leads to incorrect fold and ineffective secretion of the target proteins, thus decling protein expression level. This paper reviewed the progress in the study on exogenous protein expression in Pichia pastoris by engineering the secretion and folding pathways such as signal peptide optimization, chaperone optimization and fusion protein expression. [ABSTRACT FROM AUTHOR]

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.)

The purpose of the paper was to explore the effect of adding different levels of soybean active peptides to the diet on the growth performance, carcass traits, serum biochemical indexes and intestinal microorganisms of finishing pigs. A total of 120 finishing pigs with a weight of (72.40±1.10) kg were randomly divided into four groups, with three replicates in each group and 10 pigs in each replicate. The finishing pigs in the control group were fed a basic diet, and group A, group B and group C added 0.2%, 0.4% and 0.6% soybean active peptides in the basic diet, respectively. The experiment lasted for 42 days. The results showed that the average daily gain of the finishing pigs was significantly increased by adding soybean active peptide (P<0.05). Compared with the control group, the feed-to-weight ratio of the group B was significantly reduced (P<0.05), and the feed-to-weight ratio and average back fat thickness of the group C were significantly reduced ( P<0.05). Adding soybean active peptide could improve the meat color and significantly reduce the dripping loss of the finishing pigs in the group B and group C (P<0.05). Compared with the control group, the content of serum MDA in the experimental groups decreased significantly (P<0.05), the content of serum BUN in the group B and group C decreased significantly (P<0.05), the content of IgM and T-AOC increased significantly (P<0.05). The activity of serum AST and GSH-Px in the group C decreased significantly, and the content of IgG increased significantly (P<0.05). The flora with a relative abundance of more than 1% at the phylum level in each experimental group included Firmicutes, Proteobacterium and Bacteroides, and the relative abundance of Proteobacterium in the group C was significantly lower than that in the control group (P<0.05). The flora with a relative abundance over 1% at the genus level included Actinomycetes, Coprococcus, Clostridium and Enterobacter, and there was no significant difference in the relative abundance of each genus compared with the control group (P>0.05). The study indicates that adding 0.4%~0.6% soybean active peptide to the diet can improve the growth performance, modify carcass traits, adjust serum biochemical indexes, and affect the intestinal microbial composition of finishing pigs. [ABSTRACT FROM AUTHOR]

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 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.)

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]

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 Cereals, Oils & Foods is the property of Science & Technology of Cereals, Oils & Foods 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.)

Copyright of Feed Research is the property of Editorial Board of Feed Research 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 Bioinformatics is the property of Bioinformatics 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 Tea Science is the property of Journal of Tea Science 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 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 Chinese Journal of Applied Chemistry is the property of Chinese Journal of Applied Chemistry 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 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.)

Copyright of Journal of Shenyang Pharmaceutical University is the property of Shenyang Pharmaceutical University 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.)

Sea cucumber has high nutritional and medicinal value, is characterized by a marine echinoderm with high protein and low lipid. In recent years, a growing number of sea cucumber peptides with bioactive functions have been discovered, including antioxidant, anti-aging, learning and memory improvement, anti-fatigue, anti-hypertensive, antimicrobial, antitumor, immune-regulating, hypoglycemic, as well as anti-inflammatory activities, and regulate the physiological function through multiple ways. This paper aimed to review biological functions of sea cucumber peptides and their potential regulatory mechanisms. Furthermore, main application fields and research directions are presented, which will provide a theoretical basis for the development and utilization of sea cucumber peptides in the future. [ABSTRACT FROM AUTHOR]

Objective: The main purpose of this paper was to prepare the immunoactive peptides from Meretrix meretrix Linnaeus (MLIP) by enzymatic hydrolysis, optimize the enzymolysis conditions of MLIP, and studied its immune activity. Method: MLIP was used as raw material, and five commonly used proteases were chosen to hydrolyze. The proliferation rate of RAW264.7 cells was selected as an indicator to screen the most suitable protease for enzymolysis solution. Then, the single factor test was carried out, and three factors with significant impact were selected to optimize the enzymolysis conditions by response surface method, and MLIP was prepared with the optimized process parameters. In addition, this research also studied the effects of different concentrations of MLIP on the relative proliferation rate, cell morphology and NO release of RAW264.7 cells. Results: The proliferation rate results showed that complex protease was the most suitable enzyme to prepare MLIP. The optimal enzymatic parameters obtained by response surface optimization were: pH 6.8, solid-liquid ratio 1:6.2, enzyme dosage 3 493 U/g, enzymolysis at 45 °C for 3 hours. The relative proliferation rate of RAW264.7 cells was predicted to be 71.40%, which were basically the same with the results obtained by verification experiment. In addition, RAW264.7 cells showed the best proliferation promoting effect when the concentration of MLIP was 0.4 mg/mL. All dose of MLIP caused differentiation to varying degrees of cell differentiation and had a certain promoting effect on the release of NO of RAW264.7 cells. Conclusion: The results indicated that the MLIP exhibit desirable immune activity, which might provide reference for the preparation and further study of the MLIP. [ABSTRACT FROM AUTHOR]

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 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 International Obstetrics & Gynecology is the property of TianJin Medical Information Center 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 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.)

Proteins are the carriers of biological structure and function, which are involved in almost all the physiological processes in organisms. The qualitative and quantitative analysis of proteins can not only help us understand the mechanisms of life activities, but also screen for the proteins with abnormal expression compared to healthy controls as biomarkers of diseases as well as environmental exposure to harmful substances, thus facilitating to unravel the mechanisms of disease generation and development. Tandem mass spectrometry (MS/MS) is currently the main tool for high-throughput proteomics analysis. It can characterize the proteins by determining the molecular mass of digestion products, locating modification sites, and obtaining sequence information. However, acidic amino acid residues often have a significant impact on the cleavage process of peptides, limiting the performance of MS/MS. For example, for the phosphopeptides containing abundance of negatively charged carboxyl and phosphoryl groups, their ionization is not efficient in the positive mode, and neutral loss is easy to occur during the cleavage process, resulting in a low coverage of product ions in the MS/MS spectra. In this paper, the carboxyl groups from the R group of aspartic acid and glutamic acid as well as the C-terminus of peptide were neutralized using dimethylamine derivatization under mild condition. Accordingly, the fragmentation features of peptides with altered charge properties were studied in collision-induced dissociation (CID) mode. Further, the peptides were labeled using light and heavy isotopic dimethylamine, respectively, thus enabling to verify the features based on the same ion with different labels. The results showed that the precursor ion signal from the derivatized peptide was significantly enhanced compared to that of the native peptide. And, the derived peptides could yield a variety of a, b, y, and z ions, and some reported ions in MS/MS analysis, such as the ion at m/z 129.10/135.14 produced by the peptides with glutamic acid or lysine residue at C-terminus, which facilitating to determine the C-terminal amino acid of protein. While, the peptides proned to lose the derivative groups located at the C-terminus, yielding a series of ions at m/z ［yn-45.06］ or ［yn-73.05] In addition, the neutralization of carboxyl groups could suppress the loss of phosphoryl groups in phosphopeptides to a certain extent, thus improving the resolution efficiency of the MS/MS spectra. Overall, the derivatization method based on carboxyamidation can provide abundant information for the sequence determination and quantitative analysis of peptides due to the altered fragmentation features in CID mode. [ABSTRACT FROM AUTHOR]

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 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.)

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.)

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 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 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 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.)

The extraction and composition analysis of peptides (FNPs) from fermentation Nannochloropsis sp., as well as their anti-aging effects on Drosophila melanogaster in vivo were investigated. Compared with the non-fermentation group, the number of peptide in FNPs increases by about 100, and the oxidation sites in the peptides also increase. The maximum absorption intensity of FNPs is observed at 258 nm with a dose-dependent relationship. Compared with the control group, 5 μg/mL FNPs extends the mean life span of the the natural aging Drosophila melanogaster for 13 days. Additionally, for 70-90 days old, the deterioration of oxidative stress indicators such as MDA, SOD, and CAT caused by age are significantly restored and increased to the level of positive group by FNPs at 0.5 and 5 μg/mL. These results indicate that FNPs have potential as a promising nutritional component for alleviating human health problems induced by aging. It can also be used as a new antioxidant ingredient for functional food development or cosmeceutical applications from a resource rich and easily obtainable raw material Nannochloropsis sp. [ABSTRACT FROM AUTHOR]

【Objective】The present paper aimed to explore the molecular mechanism of Apocheima cinerarius response to stress and explore the main associated genes about low temperature and starvation. 【Method】This study cloned and obtained the chitinase gene of A. cinerarius, named AcinCht10（GenBank accession No. : OK504624）, the molecular characteristics and basic physicochemical properties of amino acids of this gene were analyzed, sequence alignment was carried out and phylogenetic tree was constructed. And the expression profile of this gene under stress（low temperature and starvation） was analyzed. 【Result】The predicted molecular formula of AcinCht10 gene was C5017H7689N1349O1490S39, the length of coding protein region was 2967 bp, encoding a total of 988 amino acids, the predicted molecular weight of AcinCht10 was 111. 99 kDa, and the predicted isoelectric point was 6. 25. The hydrophilic coefficient of the protein was-0. 547, and the predicted instability coefficient was 37. 19, indicating that it was stable hydrophilic protein. One signal peptide was found, but no transmembrane structure was found. Two catalytic regions and one chitin binding domain were found. There were 48 serine, 43 threonine and 14 tyrosine phosphoric acid sites, no glycosylation sites were detected. Four phosphoric acid sites were detected. Sequence alignment results showed that the consistency of chitinase gene between AcinCht10 and other Lepidopteran insects was higher than 91%. Phylogenetic results showed that the chitinase genes were grouped into 8 groups（type I-VIII）. AcinCht10 was grouped with Manduca sexta Cht10, Trichoplusia ni Cht10, and Ostrinia furnacalis Cht10, which were also lepidoptera. The results of gene expression analysis showed that AcinCht10 gene expression decreased with the increase of starvation treatment time, and there was no significant difference between adjacent treatments. The expression of AcinCht10 gene was the highest under 25 ℃, while the expression of AcinCht10 gene was at a low level under other temperature stresses with no significant difference. 【Conclusion】AcinCht10 gene was closely related to the response to low temperature and starvation stress. The results are helpful to reveal the molecular function of chitinase gene of A. cinerarius under stress, and lay a foundation for further revealing the molecular mechanism of A. cinerarius response to stress. [ABSTRACT FROM AUTHOR]

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.)

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.)

Post-translational modification of proteins is complex and diverse, with the phosphorylation regulated by kinases and phosphatases being one of the most widespread and important modifications. Dynamic change of quantitative analysis of phosphorylated proteins is helpful to clarify the mechanism of phosphorylation regulating life activities and understand its role in achieving biological functions. Mass spectrometry is the most commonly used strategy for the quantitative analysis of post-translational modification, involving label-free quantification, internal standard absolute quantification, and chemical labeling, etc. In this paper, a chemical labeling approach which has been used for protein glycosylation profiling was applied to the relative quantitative analysis of phosphopeptides. Using the method, carboxyl groups were located on the side chain of aspartic acid and glutamic acid residues, and the C-terminus of peptide were allowed to react with dimethylamine (d0-DMA)/deuterated dimethylamine (d6-DMA). As a result, the carboxyl groups were neutralized, and all enzymatic peptides were labeled with light/heavy tags. After the samples with different tags were mixed, the phosphopeptides were enriched using TiO2 magnetic particles and then analyzed qualitatively and relatively quantitatively by liquid chromatography-mass spectrometry (LC-MS). Amidation could shield the negatively charged carboxyl groups of non-phosphorylated and phosphorylated peptides, so that the peptides with phosphate groups mainly exhibited negative charge property, thus improving the enrichment specificity of TiO2 for phosphopeptides as well as its detection sensitivity in LC-MS analysis. Using 0.2 mg casein as a standard, 8 phosphopeptides were detected in the derivatized samples. A high abundance of b and y ions indicated that the amidation by dimethylamine was highly specific and usually occurs only at the carboxyl group without a significant effect on the phosphate group of peptides. A series of molar ratios (5∶1, 2∶1, 1∶1, 1∶2, 1∶5) of samples were derivatized using d0-DMA and d6-DMA, respectively. The results showed that the error was less than 20% for each ratio, indicating that the method possessed good relative quantitative range and accuracy. However, too many derivative sites in the peptides could result in incomplete derivatization, and the C-terminal lysine residues might self-condense to form lactam during the derivatization process. By selecting some individualized proteases during protein digestion, such as GluC, the number of derivative sites might be in an appropriate range and lysine residue could be avoided at the terminal of peptides, which should be useful for improving identification efficiency and quantitative accuracy of phosphopeptides. In summary, the chemical labeling method based on dimethylamine derivatization presents advantages for high-throughput relative quantitative analysis of phosphopeptides and it is expected to be a powerful tool for protein phosphorylation profiling in biological tissues. [ABSTRACT FROM AUTHOR]

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 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.)

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.)

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.)