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Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes.

Korean journal for food science of animal resources

Jeewanthi RK, Kim MH, Lee NK, Yoon YC, Paik HD.
PMID: 28316472
Korean J Food Sci Anim Resour. 2017;37(1):62-70. doi: 10.5851/kosfa.2017.37.1.62. Epub 2017 Feb 28.

The aim of this study was identifying a suitable food grade enzymes to hydrolyze whey protein concentrates (WPCs), to give the highest bioactivity. WPCs from ultrafiltration retentate were adjusted to 35% protein (WPC-35) and hydrolyzed by enzymes, alcalase, α-chymotrypsin,...

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Jeewanthi RK, Kim MH, Lee NK, et al. Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes. Korean J Food Sci Anim Resour. 2017;37(1):62-70doi: 10.5851/kosfa.2017.37.1.62.
Jeewanthi, R. K., Kim, M. H., Lee, N. K., Yoon, Y. C., & Paik, H. D. (2017). Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes. Korean journal for food science of animal resources, 37(1), 62-70. https://doi.org/10.5851/kosfa.2017.37.1.62
Jeewanthi, Renda Kankanamge Chaturika, et al. "Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes." Korean journal for food science of animal resources vol. 37,1 (2017): 62-70. doi: https://doi.org/10.5851/kosfa.2017.37.1.62
Jeewanthi RK, Kim MH, Lee NK, Yoon YC, Paik HD. Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes. Korean J Food Sci Anim Resour. 2017;37(1):62-70. doi: 10.5851/kosfa.2017.37.1.62. Epub 2017 Feb 28. PMID: 28316472; PMCID: PMC5355585.
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In vitro Characterization of Bacteriocin Produced by Lactic Acid Bacteria Isolated from Nem Chua, a Traditional Vietnamese Fermented Pork.

Korean journal for food science of animal resources

Pilasombut K, Rumjuankiat K, Ngamyeesoon N, Duy le ND.
PMID: 26761868
Korean J Food Sci Anim Resour. 2015;35(4):473-8. doi: 10.5851/kosfa.2015.35.4.473. Epub 2015 Aug 31.

The aim of this study was to screen and In vitro characterize the properties of bacteriocin produced by lactic acid bacteria isolated from Vietnamese fermented pork (Nem chua). One hundred and fifty LAB were isolated from ten samples of...

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Pilasombut K, Rumjuankiat K, Ngamyeesoon N, et al. In vitro Characterization of Bacteriocin Produced by Lactic Acid Bacteria Isolated from Nem Chua, a Traditional Vietnamese Fermented Pork. Korean J Food Sci Anim Resour. 2015;35(4):473-8doi: 10.5851/kosfa.2015.35.4.473.
Pilasombut, K., Rumjuankiat, K., Ngamyeesoon, N., & Duy, l. e. . N. D. (2015). In vitro Characterization of Bacteriocin Produced by Lactic Acid Bacteria Isolated from Nem Chua, a Traditional Vietnamese Fermented Pork. Korean journal for food science of animal resources, 35(4), 473-8. https://doi.org/10.5851/kosfa.2015.35.4.473
Pilasombut, Komkhae, et al. "In vitro Characterization of Bacteriocin Produced by Lactic Acid Bacteria Isolated from Nem Chua, a Traditional Vietnamese Fermented Pork." Korean journal for food science of animal resources vol. 35,4 (2015): 473-8. doi: https://doi.org/10.5851/kosfa.2015.35.4.473
Pilasombut K, Rumjuankiat K, Ngamyeesoon N, Duy le ND. In vitro Characterization of Bacteriocin Produced by Lactic Acid Bacteria Isolated from Nem Chua, a Traditional Vietnamese Fermented Pork. Korean J Food Sci Anim Resour. 2015;35(4):473-8. doi: 10.5851/kosfa.2015.35.4.473. Epub 2015 Aug 31. PMID: 26761868; PMCID: PMC4662129.
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Comparison the effect of three commercial enzymes for enzymatic hydrolysis of two substrates (rice bran protein concentrate and soy-been protein) with SDS-PAGE.

Journal of food science and technology

Ahmadifard N, Murueta JH, Abedian-Kenari A, Motamedzadegan A, Jamali H.
PMID: 27162408
J Food Sci Technol. 2016 Feb;53(2):1279-84. doi: 10.1007/s13197-015-2087-6. Epub 2015 Nov 09.

In this research enzymatic hydrolysis of rice bran protein concentrate (RBPC) and soybean Protein (SBP) as control were studied with 3 commercial enzymes (Alcalase®, Papain and acommercial 3-enzyme cocktail containing of 1.6 mg ml(-1) Trypsin, 3.1 mg ml(-1) Chymotrypsin,...

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Ahmadifard N, Murueta JH, Abedian-Kenari A, et al. Comparison the effect of three commercial enzymes for enzymatic hydrolysis of two substrates (rice bran protein concentrate and soy-been protein) with SDS-PAGE. J Food Sci Technol. 2015;53(2):1279-84doi: 10.1007/s13197-015-2087-6.
Ahmadifard, N., Murueta, J. H., Abedian-Kenari, A., Motamedzadegan, A., & Jamali, H. (2016). Comparison the effect of three commercial enzymes for enzymatic hydrolysis of two substrates (rice bran protein concentrate and soy-been protein) with SDS-PAGE. Journal of food science and technology, 53(2), 1279-84. https://doi.org/10.1007/s13197-015-2087-6
Ahmadifard, Nasrollah, et al. "Comparison the effect of three commercial enzymes for enzymatic hydrolysis of two substrates (rice bran protein concentrate and soy-been protein) with SDS-PAGE." Journal of food science and technology vol. 53,2 (2016): 1279-84. doi: https://doi.org/10.1007/s13197-015-2087-6
Ahmadifard N, Murueta JH, Abedian-Kenari A, Motamedzadegan A, Jamali H. Comparison the effect of three commercial enzymes for enzymatic hydrolysis of two substrates (rice bran protein concentrate and soy-been protein) with SDS-PAGE. J Food Sci Technol. 2016 Feb;53(2):1279-84. doi: 10.1007/s13197-015-2087-6. Epub 2015 Nov 09. PMID: 27162408; PMCID: PMC4837727.
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Methodological Considerations and Comparisons of Measurement Results for Extracellular Proteolytic Enzyme Activities in Seawater.

Frontiers in microbiology

Obayashi Y, Wei Bong C, Suzuki S.
PMID: 29067013
Front Microbiol. 2017 Oct 10;8:1952. doi: 10.3389/fmicb.2017.01952. eCollection 2017.

Microbial extracellular hydrolytic enzymes that degrade organic matter in aquatic ecosystems play key roles in the biogeochemical carbon cycle. To provide linkages between hydrolytic enzyme activities and genomic or metabolomic studies in aquatic environments, reliable measurements are required for...

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Obayashi Y, Wei Bong C, Suzuki S. Methodological Considerations and Comparisons of Measurement Results for Extracellular Proteolytic Enzyme Activities in Seawater. Front Microbiol. 2017;8:1952doi: 10.3389/fmicb.2017.01952.
Obayashi, Y., Wei Bong, C., & Suzuki, S. (2017). Methodological Considerations and Comparisons of Measurement Results for Extracellular Proteolytic Enzyme Activities in Seawater. Frontiers in microbiology, 81952. https://doi.org/10.3389/fmicb.2017.01952
Obayashi, Yumiko, et al. "Methodological Considerations and Comparisons of Measurement Results for Extracellular Proteolytic Enzyme Activities in Seawater." Frontiers in microbiology vol. 8 (2017): 1952. doi: https://doi.org/10.3389/fmicb.2017.01952
Obayashi Y, Wei Bong C, Suzuki S. Methodological Considerations and Comparisons of Measurement Results for Extracellular Proteolytic Enzyme Activities in Seawater. Front Microbiol. 2017 Oct 10;8:1952. doi: 10.3389/fmicb.2017.01952. eCollection 2017. PMID: 29067013; PMCID: PMC5641328.
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Potent anti-tumor activity of a syringolin analog in multiple myeloma: a dual inhibitor of proteasome activity targeting β2 and β5 subunits.

Oncotarget

Yoshida T, Ri M, Kanamori T, Aoki S, Ashour R, Kinoshita S, Narita T, Totani H, Masaki A, Ito A, Kusumoto S, Ishida T, Komatsu H, Kitahata S, Chiba T, Ichikawa S, Iida S.
PMID: 29515784
Oncotarget. 2018 Jan 11;9(11):9975-9991. doi: 10.18632/oncotarget.24160. eCollection 2018 Feb 09.

Proteasome inhibitors (PI), mainly targeting the β5 subunit of the 20S proteasome, are widely used in the treatment of multiple myeloma (MM). However, PI resistance remains an unresolved problem in the therapy of relapsed and refractory MM. To develop...

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Yoshida T, Ri M, Kanamori T, et al. Potent anti-tumor activity of a syringolin analog in multiple myeloma: a dual inhibitor of proteasome activity targeting β2 and β5 subunits. Oncotarget. 2018;9(11):9975-9991doi: 10.18632/oncotarget.24160.
Yoshida, T., Ri, M., Kanamori, T., Aoki, S., Ashour, R., Kinoshita, S., Narita, T., Totani, H., Masaki, A., Ito, A., Kusumoto, S., Ishida, T., Komatsu, H., Kitahata, S., Chiba, T., Ichikawa, S., & Iida, S. (2018). Potent anti-tumor activity of a syringolin analog in multiple myeloma: a dual inhibitor of proteasome activity targeting β2 and β5 subunits. Oncotarget, 9(11), 9975-9991. https://doi.org/10.18632/oncotarget.24160
Yoshida, Takashi, et al. "Potent anti-tumor activity of a syringolin analog in multiple myeloma: a dual inhibitor of proteasome activity targeting β2 and β5 subunits." Oncotarget vol. 9,11 (2018): 9975-9991. doi: https://doi.org/10.18632/oncotarget.24160
Yoshida T, Ri M, Kanamori T, Aoki S, Ashour R, Kinoshita S, Narita T, Totani H, Masaki A, Ito A, Kusumoto S, Ishida T, Komatsu H, Kitahata S, Chiba T, Ichikawa S, Iida S. Potent anti-tumor activity of a syringolin analog in multiple myeloma: a dual inhibitor of proteasome activity targeting β2 and β5 subunits. Oncotarget. 2018 Jan 11;9(11):9975-9991. doi: 10.18632/oncotarget.24160. eCollection 2018 Feb 09. PMID: 29515784; PMCID: PMC5839415.
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A new concept for molecular engineering of artificial enzymes: a multiscale simulation.

Soft matter

Komarov PV, Khalatur PG, Khokhlov AR.
PMID: 26539842
Soft Matter. 2016 Jan 21;12(3):689-704. doi: 10.1039/c5sm02428e. Epub 2015 Nov 05.

We propose a new concept for the design of artificial enzymes from synthetic protein-like copolymers and non-natural functional monomers which in terms of their affinity for water can be divided into two categories: hydrophobic and hydrophilic. Hydrophilic monomers comprise...

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Komarov PV, Khalatur PG, Khokhlov AR. A new concept for molecular engineering of artificial enzymes: a multiscale simulation. Soft Matter. 2015;12(3):689-704doi: 10.1039/c5sm02428e.
Komarov, P. V., Khalatur, P. G., & Khokhlov, A. R. (2016). A new concept for molecular engineering of artificial enzymes: a multiscale simulation. Soft matter, 12(3), 689-704. https://doi.org/10.1039/c5sm02428e
Komarov, Pavel V, et al. "A new concept for molecular engineering of artificial enzymes: a multiscale simulation." Soft matter vol. 12,3 (2016): 689-704. doi: https://doi.org/10.1039/c5sm02428e
Komarov PV, Khalatur PG, Khokhlov AR. A new concept for molecular engineering of artificial enzymes: a multiscale simulation. Soft Matter. 2016 Jan 21;12(3):689-704. doi: 10.1039/c5sm02428e. Epub 2015 Nov 05. PMID: 26539842.
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Proteasome inhibition slightly improves cardiac function in mice with hypertrophic cardiomyopathy.

Frontiers in physiology

Schlossarek S, Singh SR, Geertz B, Schulz H, Reischmann S, Hübner N, Carrier L.
PMID: 25566086
Front Physiol. 2014 Dec 16;5:484. doi: 10.3389/fphys.2014.00484. eCollection 2014.

A growing line of evidence indicates a dysfunctional ubiquitin-proteasome system (UPS) in cardiac diseases. Anti-hypertrophic effects and improved cardiac function have been reported after treatment with proteasome inhibitors in experimental models of cardiac hypertrophy. Here we tested whether proteasome...

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Schlossarek S, Singh SR, Geertz B, et al. Proteasome inhibition slightly improves cardiac function in mice with hypertrophic cardiomyopathy. Front Physiol. 2014;5:484doi: 10.3389/fphys.2014.00484.
Schlossarek, S., Singh, S. R., Geertz, B., Schulz, H., Reischmann, S., Hübner, N., & Carrier, L. (2014). Proteasome inhibition slightly improves cardiac function in mice with hypertrophic cardiomyopathy. Frontiers in physiology, 5484. https://doi.org/10.3389/fphys.2014.00484
Schlossarek, Saskia, et al. "Proteasome inhibition slightly improves cardiac function in mice with hypertrophic cardiomyopathy." Frontiers in physiology vol. 5 (2014): 484. doi: https://doi.org/10.3389/fphys.2014.00484
Schlossarek S, Singh SR, Geertz B, Schulz H, Reischmann S, Hübner N, Carrier L. Proteasome inhibition slightly improves cardiac function in mice with hypertrophic cardiomyopathy. Front Physiol. 2014 Dec 16;5:484. doi: 10.3389/fphys.2014.00484. eCollection 2014. PMID: 25566086; PMCID: PMC4267180.
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Immunogold localization of chymotrypsin inhibitor-2, a lysine-rich protein, in developing barley endosperm.

Planta

Rasmussen U, Munck L, Ullrich SE.
PMID: 24201956
Planta. 1990 Jan;180(2):272-7. doi: 10.1007/BF00194007.

Chymotrypsin inhibitor-2, a lysine-rich protein in the barley endosperm, has been localized at the ultrastructural level by immunocytochemistry in developing barley endosperm cells 14 days post anthesis. The protein is deposited in the protein bodies. Two morphologically distinct types...

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Rasmussen U, Munck L, Ullrich SE. Immunogold localization of chymotrypsin inhibitor-2, a lysine-rich protein, in developing barley endosperm. Planta. 1990;180(2):272-7doi: 10.1007/BF00194007.
Rasmussen, U., Munck, L., & Ullrich, S. E. (1990). Immunogold localization of chymotrypsin inhibitor-2, a lysine-rich protein, in developing barley endosperm. Planta, 180(2), 272-7. https://doi.org/10.1007/BF00194007
Rasmussen, U, et al. "Immunogold localization of chymotrypsin inhibitor-2, a lysine-rich protein, in developing barley endosperm." Planta vol. 180,2 (1990): 272-7. doi: https://doi.org/10.1007/BF00194007
Rasmussen U, Munck L, Ullrich SE. Immunogold localization of chymotrypsin inhibitor-2, a lysine-rich protein, in developing barley endosperm. Planta. 1990 Jan;180(2):272-7. doi: 10.1007/BF00194007. PMID: 24201956.
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Enzymatic peptide synthesis by new supported biocatalysts.

Amino acids

Rolland-Fulcrand V, May N, Viallefont P, Lazaro R.
PMID: 24189739
Amino Acids. 1994 Oct;6(3):311-4. doi: 10.1007/BF00813751.

It is well known that proteases can be successfully used for peptide synthesis in aqueous medium or in water-containing organic solvents. Copolymerized of acrylated derivatives ofα-chymotrypsin and polyethylene glycol (PEG) have been prepared and used as biocatalysts for the...

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Rolland-Fulcrand V, May N, Viallefont P, et al. Enzymatic peptide synthesis by new supported biocatalysts. Amino Acids. 1994;6(3):311-4doi: 10.1007/BF00813751.
Rolland-Fulcrand, V., May, N., Viallefont, P., & Lazaro, R. (1994). Enzymatic peptide synthesis by new supported biocatalysts. Amino acids, 6(3), 311-4. https://doi.org/10.1007/BF00813751
Rolland-Fulcrand, V, et al. "Enzymatic peptide synthesis by new supported biocatalysts." Amino acids vol. 6,3 (1994): 311-4. doi: https://doi.org/10.1007/BF00813751
Rolland-Fulcrand V, May N, Viallefont P, Lazaro R. Enzymatic peptide synthesis by new supported biocatalysts. Amino Acids. 1994 Oct;6(3):311-4. doi: 10.1007/BF00813751. PMID: 24189739.
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Toward optimized potential functions for protein-protein interactions in aqueous solutions: osmotic second virial coefficient calculations using the MARTINI coarse-grained force field.

Journal of chemical theory and computation

Stark AC, Andrews CT, Elcock AH.
PMID: 24223529
J Chem Theory Comput. 2013 Sep 10;9(9). doi: 10.1021/ct400008p.

Coarse-grained (CG) simulation methods are now widely used to model the structure and dynamics of large biomolecular systems. One important issue for using such methods - especially with regard to using them to model, for example, intracellular environments -...

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Stark AC, Andrews CT, Elcock AH. Toward optimized potential functions for protein-protein interactions in aqueous solutions: osmotic second virial coefficient calculations using the MARTINI coarse-grained force field. J Chem Theory Comput. 2013;9(9)doi: 10.1021/ct400008p.
Stark, A. C., Andrews, C. T., & Elcock, A. H. (2013). Toward optimized potential functions for protein-protein interactions in aqueous solutions: osmotic second virial coefficient calculations using the MARTINI coarse-grained force field. Journal of chemical theory and computation, 9(9), . https://doi.org/10.1021/ct400008p
Stark, Austin C, et al. "Toward optimized potential functions for protein-protein interactions in aqueous solutions: osmotic second virial coefficient calculations using the MARTINI coarse-grained force field." Journal of chemical theory and computation vol. 9,9 (2013). doi: https://doi.org/10.1021/ct400008p
Stark AC, Andrews CT, Elcock AH. Toward optimized potential functions for protein-protein interactions in aqueous solutions: osmotic second virial coefficient calculations using the MARTINI coarse-grained force field. J Chem Theory Comput. 2013 Sep 10;9(9). doi: 10.1021/ct400008p. PMID: 24223529; PMCID: PMC3819042.
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Proteomic analysis of domestic pig pancreas during development using two-dimensional electrophoresis and matrix-assisted laser desorption/ionization-time of flight mass spectrometry.

Laboratory animal research

Ahn JY, Kim IY, Oh SJ, Hwang HS, Yi SS, Kim YN, Shin JH, Yoon YS, Seong JK.
PMID: 24999358
Lab Anim Res. 2014 Jun;30(2):45-53. doi: 10.5625/lar.2014.30.2.45. Epub 2014 Jun 23.

Pig pancreas may be a therapeutic resource for human diabetic patients. However, this potential is hindered by a lack of knowledge of the molecular events of pig pancreas development. In this study, the embryonic day 60, neonate and 6-month...

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Ahn JY, Kim IY, Oh SJ, et al. Proteomic analysis of domestic pig pancreas during development using two-dimensional electrophoresis and matrix-assisted laser desorption/ionization-time of flight mass spectrometry. Lab Anim Res. 2014;30(2):45-53doi: 10.5625/lar.2014.30.2.45.
Ahn, J. Y., Kim, I. Y., Oh, S. J., Hwang, H. S., Yi, S. S., Kim, Y. N., Shin, J. H., Yoon, Y. S., & Seong, J. K. (2014). Proteomic analysis of domestic pig pancreas during development using two-dimensional electrophoresis and matrix-assisted laser desorption/ionization-time of flight mass spectrometry. Laboratory animal research, 30(2), 45-53. https://doi.org/10.5625/lar.2014.30.2.45
Ahn, Ji Ye, et al. "Proteomic analysis of domestic pig pancreas during development using two-dimensional electrophoresis and matrix-assisted laser desorption/ionization-time of flight mass spectrometry." Laboratory animal research vol. 30,2 (2014): 45-53. doi: https://doi.org/10.5625/lar.2014.30.2.45
Ahn JY, Kim IY, Oh SJ, Hwang HS, Yi SS, Kim YN, Shin JH, Yoon YS, Seong JK. Proteomic analysis of domestic pig pancreas during development using two-dimensional electrophoresis and matrix-assisted laser desorption/ionization-time of flight mass spectrometry. Lab Anim Res. 2014 Jun;30(2):45-53. doi: 10.5625/lar.2014.30.2.45. Epub 2014 Jun 23. PMID: 24999358; PMCID: PMC4079831.
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Phase I randomized double-blind placebo-controlled single-dose safety studies of Bowman-Birk inhibitor concentrate.

Oncology letters

Lin LL, Mick R, Ware J, Metz J, Lustig R, Vapiwala N, Rengan R, Kennedy AR.
PMID: 24944684
Oncol Lett. 2014 Apr;7(4):1151-1158. doi: 10.3892/ol.2014.1855. Epub 2014 Feb 05.

In previously performed animal studies and Phase I-II human trials, Bowman-Birk inhibitor concentrate (BBIC) appeared to be a promising cancer chemopreventive agent. The present study describes the results of two phase I randomized double-blind placebo-controlled trials performed in male...

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Lin LL, Mick R, Ware J, et al. Phase I randomized double-blind placebo-controlled single-dose safety studies of Bowman-Birk inhibitor concentrate. Oncol Lett. 2014;7(4):1151-1158doi: 10.3892/ol.2014.1855.
Lin, L. L., Mick, R., Ware, J., Metz, J., Lustig, R., Vapiwala, N., Rengan, R., & Kennedy, A. R. (2014). Phase I randomized double-blind placebo-controlled single-dose safety studies of Bowman-Birk inhibitor concentrate. Oncology letters, 7(4), 1151-1158. https://doi.org/10.3892/ol.2014.1855
Lin, Lilie L, et al. "Phase I randomized double-blind placebo-controlled single-dose safety studies of Bowman-Birk inhibitor concentrate." Oncology letters vol. 7,4 (2014): 1151-1158. doi: https://doi.org/10.3892/ol.2014.1855
Lin LL, Mick R, Ware J, Metz J, Lustig R, Vapiwala N, Rengan R, Kennedy AR. Phase I randomized double-blind placebo-controlled single-dose safety studies of Bowman-Birk inhibitor concentrate. Oncol Lett. 2014 Apr;7(4):1151-1158. doi: 10.3892/ol.2014.1855. Epub 2014 Feb 05. PMID: 24944684; PMCID: PMC3961219.
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Showing 1 to 12 of 753 entries