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This present study aimed to investigate the effects of various cooking times (1 h, 1.5 h, 2 h, 2.5 h, named as JHBP-1, JHBP-1.5, JHBP-2, JHBP-2.5) on the antioxidant activity and peptide profile of Jinhua ham broth peptides (JHBP). The peptides extracted from uncooked ham were used as an uncooked group with the name of JHBP-0. The results revealed that the antioxidant efficacy in the four cooked groups changed dramatically compared to JHBP-0. After cooking, the DPPH radical scavenging activity, hydroxyl radical scavenging activity and superoxide anion radical scavenging activity decreased, except for the Fe2+ chelation and ABTS+ scavenging capacity which increased significantly. However, the cooked groups still showed a strong antioxidant capacity. In particular, the superoxide anion radical scavenging ability and the Fe2+ chelation action were significantly stronger compared to glutathione (GSH) and butylated hydroxytoluene (BHT) (p < 0.05). JHBP-1.5 also displayed stronger antioxidant capacity than the other three cooked groups, and its secondary structure and mass distribution changed significantly after cooking, specifically with an increased proportion of helix and

Submitted by Vitor Silverio Rodrigues (vitorsrodrigues@reitoria.unesp.br) on 2014-05-27T11:26:23Z No. of bitstreams: 0Bitstream added on 2014-05-27T14:36:39Z : No. of bitstreams: 1 2-s2.0-80052965793.pdf: 391722 bytes, checksum: 7166ab85cd1951015d9af5e904320054 (MD5) Submitted by Vitor Silverio Rodrigues (vitorsrodrigues@reitoria.unesp.br) on 2014-05-27T11:26:23Z No. of bitstreams: 0Bitstream added on 2014-05-27T14:36:39Z : No. of bitstreams: 1 2-s2.0-80052965793.pdf: 391722 bytes, checksum: 7166ab85cd1951015d9af5e904320054 (MD5) Made available in DSpace on 2014-05-27T11:26:23Z (GMT). No. of bitstreams: 0 Previous issue date: 2012-02-15 Submitted by Vitor Silverio Rodrigues (vitorsrodrigues@reitoria.unesp.br) on 2014-05-27T11:26:23Z No. of bitstreams: 0Bitstream added on 2014-05-27T14:36:39Z : No. of bitstreams: 1 2-s2.0-80052965793.pdf: 391722 bytes, checksum: 7166ab85cd1951015d9af5e904320054 (MD5) Made available in DSpace on 2014-05-27T11:26:23Z (GMT). No. of bitstreams: 0 Previous issue date: 2012-02-15 Made available in DSpace on 2014-05-27T11:26:23Z (GMT). No. of bitstreams: 0 Previous issue date: 2012-02-15 Made available in DSpace on 2014-05-27T11:26:23Z (GMT). No. of bitstreams: 0 Previous issue date: 2012-02-15 Prato cheeses were manufactured using coagulant from Thermomucor indicae-seudaticae N31 or a commercial coagulant. Cheeses were characterised using the following analysis: yield; fat; acidity; moisture; ash; salt; pH; total nitrogen; total protein; NS-pH 4.6/NT100; NS-TCA 12%/NT100; casein electrophoresis; and RP-HPLC. The results were statistically analysed and revealed that the proteolytic indices were not significantly different throughout the 60 days of ripening of cheeses made with either coagulant. Even though there were some quantitative differences in the peptide profile of cheeses, the enzyme from T. indicae-seudaticae N31 was used in the production of good quality Prato cheese without having to change the established technological parameters of the process. © 2011 Elsevier Ltd. All rights reserved. Laboratory of Biochemistry and Applied Microbiology IBILCE UNESP, Rua Cristóvão Colombo 2265, Sao Jose do Rio Preto, Sao Paulo, CEP 15054-000 Laboratory of Milk and Milk Products IBILCE UNESP, Rua Cristóvão Colombo 2265, Sao Jose do Rio Preto, Sao Paulo, CEP 15054-000 Laboratory of Biochemistry and Applied Microbiology IBILCE UNESP, Rua Cristóvão Colombo 2265, Sao Jose do Rio Preto, Sao Paulo, CEP 15054-000 Laboratory of Milk and Milk Products IBILCE UNESP, Rua Cristóvão Colombo 2265, Sao Jose do Rio Preto, Sao Paulo, CEP 15054-000

Background Recent development of novel technologies paved the way for quantitative proteomics. One of the most important among them is iTRAQ, employing isobaric tags for relative or absolute quantitation. Despite large progress in technology development, still many challenges remain for derivation and interpretation of quantitative results. One of these challenges is the consistent assignment of peptides to proteins. Results We have developed Peptide Profiling Guided Identification of Proteins (PPINGUIN), a statistical analysis workflow for iTRAQ data addressing the problem of ambiguous peptide quantitations. Motivated by the assumption that peptides uniquely derived from the same protein are correlated, our method employs clustering as a very early step in data processing prior to protein inference. Our method increases experimental reproducibility and decreases variability of quantitations of peptides assigned to the same protein. Giving further support to our method, application to a type 2 diabetes dataset identifies a list of protein candidates that is in very good agreement with previously performed transcriptomics meta analysis. Making use of quantitative properties of signal patterns identified, PPINGUIN can reveal new isoform candidates. Conclusions Regarding the increasing importance of quantitative proteomics we think that this method will be useful in practical applications like model fitting or functional enrichment analysis. We recommend to use this method if quantitation is a major objective of research., BMC Bioinformatics, 13, ISSN:1471-2105