Gotowa bibliografia na temat „Pea protein hydrolysates”
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Artykuły w czasopismach na temat "Pea protein hydrolysates"
Ratnayani, Ketut, Indriani Wisnu Susanto Panjaitan i Ni Made Puspawati. "SCREENING POTENTIAL ANTIOXIDANT AND ANTIBACTERIAL ACTIVITIES OF PROTEIN HYDROLYSATES DERIVED FROM GERMINATED LABLAB BEAN, PIGEON PEA AND KIDNEY BEAN". Journal of Health Sciences and Medicine 1, nr 1 (1.02.2017): 24. http://dx.doi.org/10.24843/jhsm.2017.v01.i01.p07.
Pełny tekst źródłaRuiz, Raquel, Raquel Olías, Alfonso Clemente i Luis A. Rubio. "A Pea (Pisum sativum L.) Seed Vicilins Hydrolysate Exhibits PPARγ Ligand Activity and Modulates Adipocyte Differentiation in a 3T3-L1 Cell Culture Model". Foods 9, nr 6 (16.06.2020): 793. http://dx.doi.org/10.3390/foods9060793.
Pełny tekst źródłaAwosika, Temitola, i Rotimi E. Aluko. "Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors". Foods 8, nr 6 (10.06.2019): 200. http://dx.doi.org/10.3390/foods8060200.
Pełny tekst źródłaSiriporn, B., P. Thongkorn, S. Waraporn, S. Wiriyaporn, S. Sinee, A. Chiramet i E. A. Rotimi. "Antioxidant polypeptides derived from pigeon pea (Cajanus cajan (L) Mill sp.) by enzymatic hydrolysis". Food Research 8, Supplementary 2 (26.04.2024): 182–89. http://dx.doi.org/10.26656/fr.2017.8(s2).146.
Pełny tekst źródłaHidayat, Meilinah, Sijani Prahastuti, TeresaLiliana Wargasetia, Vincentius Ferdinand, Roro Wahyudianingsih, AndreanusAndaja Soemardji, SitiFarah Rahmawati, Nova Suliska i Khomaini Hasan. "Role of pea protein hydrolysates as antinephrotoxicity". Journal of Reports in Pharmaceutical Sciences 8, nr 1 (2019): 55. http://dx.doi.org/10.4103/jrptps.jrptps_14_17.
Pełny tekst źródłaSoral-Śmietana, M., A. Świgoń, R. Amarowicz i L. Sijtsma. "The solubility of trypsin pea protein hydrolysates". Nahrung / Food 42, nr 03-04 (sierpień 1998): 217–18. http://dx.doi.org/10.1002/(sici)1521-3803(199808)42:03/04<217::aid-food217>3.3.co;2-u.
Pełny tekst źródłaKrasnoshtanova, Alla Al'bertovna, i Leonid Viktorovich Shul'ts. "PREPARATION AND EVALUATION OF THE FUNCTIONAL PROPERTIES OF PROTEIN ISOLATES AND HY-DROLYSATES FROM PLANT RAW MATERIALS". chemistry of plant raw material, nr 4 (15.12.2022): 299–309. http://dx.doi.org/10.14258/jcprm.20220410952.
Pełny tekst źródłaStanisavljevic, Nemanja, Goran Vukotic, Ferenc Pastor, Desanka Suznjevic, Zivko Jovanovic, Ivana Strahinic, Djordje Fira i Svetlana Radovic. "Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria". Archives of Biological Sciences 67, nr 3 (2015): 1033–42. http://dx.doi.org/10.2298/abs150130066s.
Pełny tekst źródłaMoreno, Cecilia, Luis Mojica, Elvira González de Mejía, Rosa María Camacho Ruiz i Diego A. Luna-Vital. "Combinations of Legume Protein Hydrolysates Synergistically Inhibit Biological Markers Associated with Adipogenesis". Foods 9, nr 11 (17.11.2020): 1678. http://dx.doi.org/10.3390/foods9111678.
Pełny tekst źródłaHumiski, L. M., i R. E. Aluko. "Physicochemical and Bitterness Properties of Enzymatic Pea Protein Hydrolysates". Journal of Food Science 72, nr 8 (październik 2007): S605—S611. http://dx.doi.org/10.1111/j.1750-3841.2007.00475.x.
Pełny tekst źródłaRozprawy doktorskie na temat "Pea protein hydrolysates"
Irankunda, Rachel. "Nickel Chelating Peptides & Chromatography : From Peptides Separation Simulation up to their Antioxidant Activities - related Applications". Electronic Thesis or Diss., Université de Lorraine, 2023. http://www.theses.fr/2023LORR0213.
Pełny tekst źródłaMetal-Chelating Peptides (MCPs), from protein hydrolysates, present various applications in nutrition, pharmacy, cosmetic etc. Yet, the empirical approach generally used to discover bioactive peptides from hydrolysates is time consuming and expensive due to many steps of fractionation, separation and biological activities evaluation. Thus, this PhD aimed to develop a novel approach for MCPs separation prediction using chromatography modelling and simulation based on the analogy between Immobilized Metal ion Affinity Chromatography (IMAC) and Surface Plasmon Resonance (SPR). For the first time, the SPR-IMAC analogy was experimentally investigated on 22 peptides and 70% of them validated this analogy, since peptides well retained in IMAC were also endowed with a good affinity for Ni2+ in SPR. In the second time, peptides with high affinity for Ni2+ (i.e low dissociation constant KD in SPR and a high retention time in IMAC) were used to study the modelling and simulation of peptide concentration profiles at the column outlet in IMAC. Since knowledge of adsorption isotherms was required to perform simulation, it was necessary to develop a methodology for predicting Langmuir isotherm parameters in IMAC from SPR data. The validity of simulation was evaluated by comparing experimental and simulated retention times that should be close for reliable prediction. Therefore, several approaches were evaluated to determine Langmuir sorption parameters, the most interesting one introduces a correction factor on the maximum adsorption capacity qmax alone, assuming that the affinity of peptides for immobilized Ni2+ did not change depending on the technology used (SPR vs. IMAC), thus affinity constant KA was not modified. Meanwhile, industrial application of MCPs and hydrolysates were studied. First, pea protein hydrolysates were produced by either Alcalase® followed by Flavourzyme® (Alc+Flav≤1kDa) or Protamex® followed by Flavourzyme® (Prot+Flav≤1kDa). SwitchSENSE® technology evidences the presence of Ni2+ chelating peptides and antioxidants tests showed that Prot+Flav≤1kDa has higher radical scavenging and reducing power, related to its higher degree of hydrolysis and small-size peptides quantity. Secondly, pea hydrolysates and MCPs were investigated for their ability to inhibit the lipid oxidation in emulsions. They slowed down lipid oxidation through chelation of prooxidant (metals such as Fe2+) reducing primary and secondary oxidation products responsible of deterioration of lipid containing products. Thus, pea hydrolysates and MCPs could be used as antioxidants in food and cosmetic products, as alternative to chemicals such as EDTA, BHT and TBHQ
Chao, Dongfang. "Effects of thermal and high pressure treatments on structural and functional properties of pea seed (Pisum sativum L.) proteins and enzymatic protein hydrolysates". 2012. http://hdl.handle.net/1993/8103.
Pełny tekst źródłaTang, Chung-Yu, i 鄧頌瑜. "To investigate the potential of xanthine oxidase inhibition from corn by-products extracts and yellow field pea protein hydrolysates". Thesis, 2018. http://ndltd.ncl.edu.tw/handle/dwexn4.
Pełny tekst źródłaPrairie, Natalie Paula. "The cardio-renal effect of pea protein hydrolysate in a chronic kidney disease rat model". 2012. http://hdl.handle.net/1993/5015.
Pełny tekst źródłaPownall, Trisha. "Effects of molecular charge and hydrophobicity on the antioxidative properties of pea (Pisum sativum L.) protein hydrolysate fractions". 2009. http://hdl.handle.net/1993/21596.
Pełny tekst źródłaStreszczenia konferencji na temat "Pea protein hydrolysates"
Asen, Nancy, i Rotimi Aluko. "Functional Properties of Enzymatic Pea Protein Hydrolysates That Inhibit in vitro Activities of Acetylcholinesterase and Butyrylcholinesterase". W 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/ktht4252.
Pełny tekst źródłaVarela, D., R. O’Hara i A. C. Neves. "BY-PRODUCTS OF THE WHELK PROCESSING INDUSTRY AS VALUABLE SOURCE OF ANTIOXIDANT PEPTIDES". W World Conference on Waste Management. The International Institute of Knowledge Management, 2021. http://dx.doi.org/10.17501/26510251.2021.1103.
Pełny tekst źródłaReinoso, Zain Sanchez, Jacinthe Thibodeau, Laila Ben Said, Ismail Fliss, Laurent Bazinet i Sergey Mikhaylin. "Bioactive Peptide Production from Slaughterhouse Blood Proteins: Impact of Pulsed Electric Fields and Ph on Enzyme Inactivation, Antimicrobial and Antioxidant Activities of Peptic Hydrolysates from Bovine and Porcine Hemoglobins". W 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/fsht2150.
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