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A comparative study of fermented buffalo and camel milk with anti-inflammatory, ace-inhibitory and anti-diabetic properties and release of bio active peptides with molecular interactions: In vitro, in silico and molecular study

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Food Bioscience 2023年第2期52卷 687-721页

作者： Ruchita Khakhariya Amar A.Sakure Ruchika Maurya Mahendra Bishnoi Kanthi Kiran Kondepudi Srichandan Padhi Amit Kumar Rai Zhenbin Liu G.B.Patil Maunil Mankad Subrota Hati Dept.of Dairy Microbiology SMC College of Dairy ScienceKamdhenu UniversityAnand388110GujaratIndia Dept.of Agriculture Biotechnology Anand Agricultural UniversityAnand388110GujaratIndia Regional Center for Biotechnology FaridabadHaryana121001India Healthy Gut Research Group Food&Nutritional Biotechnology DivisionNational Agri-Food Biotechnology InstituteKnowledge CitySector 81SAS NagarPunjab140306India Institute of Bioresources and Sustainable Development Regional CentreTadong737102SikkimIndia School of Food and Biological Engineering Shaanxi University of Science and TechnologyXi’an710021China Dept.of Tissue Culture Anand Agricultural UniversityAnand388110GujaratIndia

The aim of this study is to compare ace inhibitory,anti-diabetic and Anti-inflammatory activity of buffalo and camel milk using Lacticaseibacillus paracasei(M11)in combination with yeast Saccharomyces cerevisiae(WBS2A)and to release peptides with antihypertensive and anti-diabetic *** buffalo and camel milk were considered for the evaluation of Angiotensin-converting enzyme(ace)inhibitory and anti-diabetic activities at specific time intervals(12,24,36 and 48 h)at 37℃.For the growth condition optimization,proteolytic activity was evaluated with specific inoculation rates(1.5%,2.0%,and 2.5%)and at specific incubation periods(12,24,36,and 48 h).The highest peptides were produced at 2.5%inoculation rate and at 48 h of incubation in both buffalo and camel milk at 37℃.Further,camel and buffalo milk fermented with M11+WBS2A significantly lower the overproduction of TNF-α,IL-6,IL-1βand Nitric oxide(NO),that was induced by lipopolysaccharide(LPS)stimulation in RAW 267.4 *** protein purification,2D gel electrophoresis and SDS-PAGE were *** and buffalo milk that had not been fermented displayed protein bands between 10 and 100 kDa and 10 and 75 kDa respectively,whereas all the fermented samples showed bands between 10 and 75 *** SDS-PAGE,in permeates,there were no apparent protein *** fermented buffalo and camel milk were electrophoresed in 2D gel,a total of 26 and 25 protein spots were *** 2D gel electrophoresis,protein spots had sizes between 10 and 37 *** RP-HPLC,water-soluble extracts(WSEs)of ultra-filtered fractions were used to distinguish different fractions of a *** software was used to characterize the LC/MS *** transform-infrared spectroscopy(FTIR)was used to evaluate various functional groups of fermented *** molecular docking study,the peptide sequences identified from the fermented buffalo milk(FBM)and camel milk(FCM)were examined for their binding affinity against the binding sites of

关键词： ace inhibitory Anti-diabetic activity Buffalo milk Camel milk SDS FTIR RP-HPLC LC/MS Molecular docking

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In vitro and in silico analysis of dual-function peptides derived from casein hydrolysate

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Food Science and Human Wellness 2021年第1期10卷 32-37页

作者： Maolin Tu Xinyu Qiao Cong Wang Hanxiong Liu Shuzhen Cheng Zhe Xu Ming Du School of Food Science and Technology National Engineering Research Center of SeafoodCollaborative Innovation Center of Seafood Deep ProcessingDalian Polytechnic UniversityDalian 116034China

There is no study on food-derived peptide with both anticoagulant and angiotensin I-converting enzyme inhibitory (aceI) activities yet. In this work, the anticoagulant and aceI activities of the casein hydrolysates released by pepsin digestion were evaluated for the first time to the best of our knowledge. Results indicated that the casein hydrolysate exhibited potent anticoagulant activity by prolonging the thrombin time (TT) and the activated partial thromboplastin time (APTT). Compared with control samples, at 10 mg/mL, the TT and APTT of casein hydrolysate were 186.0 % ± 6.6 % and 163.5 % ± 7.4 %, respectively. The casein hydrolysate also showed a strong aceI activity with an IC50 value of 1.775 mg/mL. The components of the bioactive casein hydrolysate were analyzed by nanoscale liquid chromatography quadrupole time-of-flight tandem mass spectrometry (NanoLC-Q-TOF-MS/MS). Total of 115 peptides were identified, among which 34, 9, 55 and 17 peptides were derived from α_(s1-), α_(s2-), β-, and κ-casein, respectively. The results of PeptideRanker and PepSite 2 analysis showed that 6 peptides (FRQFYQL, NENLLRF, NPWDQVKR, PVVVPPFLQ, PVRGPFPIIV, and ARHPHPHLSF) have both aceI and anticoagulant activities by binding to the active sites of ace and thrombin. This study indicated that casein is a potential functional food supplement that can be used for medical purposes.

关键词： Casein Anticoagulant ace inhibitory Dual-function NanoLC-Q-TOF-MS/MS

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