Antibacterial Activity of Trypsin-Hydrolyzed Camel and Cow Whey and Their Fractions

Antibacterial peptides were isolated and purified from whey proteins of camel milk (CaW) and cow milk (CoW) and their antimicrobial activities were studied. The whey proteins were hydrolyzed using trypsin, and the degree of hydrolysis was identified by gel electrophoresis. The whey hydrolysate (WH)...

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Main Authors: Ruixue Wang, Zhihao Han, Rimutu Ji, Yuchen Xiao, Rendalai Si, Fucheng Guo, Jing He, Le Hai, Liang Ming, Li Yi
Format: Article
Language:English
Published: MDPI AG 2020-02-01
Series:Animals
Subjects:
Online Access:https://www.mdpi.com/2076-2615/10/2/337
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spelling doaj-93d7c96e142545d19344dc5331ea1e4a2020-11-24T21:53:48ZengMDPI AGAnimals2076-26152020-02-0110233710.3390/ani10020337ani10020337Antibacterial Activity of Trypsin-Hydrolyzed Camel and Cow Whey and Their FractionsRuixue Wang0Zhihao Han1Rimutu Ji2Yuchen Xiao3Rendalai Si4Fucheng Guo5Jing He6Le Hai7Liang Ming8Li Yi9Key Laboratory of Dairy Biotechnology and Bioengineering, Ministry of Education, College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, Inner Mongolia, ChinaKey Laboratory of Dairy Biotechnology and Bioengineering, Ministry of Education, College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, Inner Mongolia, ChinaKey Laboratory of Dairy Biotechnology and Bioengineering, Ministry of Education, College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, Inner Mongolia, ChinaKey Laboratory of Dairy Biotechnology and Bioengineering, Ministry of Education, College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, Inner Mongolia, ChinaKey Laboratory of Dairy Biotechnology and Bioengineering, Ministry of Education, College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, Inner Mongolia, ChinaKey Laboratory of Dairy Biotechnology and Bioengineering, Ministry of Education, College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, Inner Mongolia, ChinaKey Laboratory of Dairy Biotechnology and Bioengineering, Ministry of Education, College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, Inner Mongolia, ChinaKey Laboratory of Dairy Biotechnology and Bioengineering, Ministry of Education, College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, Inner Mongolia, ChinaKey Laboratory of Dairy Biotechnology and Bioengineering, Ministry of Education, College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, Inner Mongolia, ChinaKey Laboratory of Dairy Biotechnology and Bioengineering, Ministry of Education, College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, Inner Mongolia, ChinaAntibacterial peptides were isolated and purified from whey proteins of camel milk (CaW) and cow milk (CoW) and their antimicrobial activities were studied. The whey proteins were hydrolyzed using trypsin, and the degree of hydrolysis was identified by gel electrophoresis. The whey hydrolysate (WH) was purified using ultrafiltration and Dextran gel chromatography to obtain small peptides with antibacterial activity. The effect of the antimicrobial peptides on the morphology of bacterial strains was investigated using transmission electron microscopy. Their amino acid composition and antimicrobial activities were then determined. Polypeptides CaWH-III (&lt;3 kDa) and CoWH-III (&lt;3 kDa) had the strongest antibacterial activity. Both Fr.A2 (CaWH-Ⅲ&#8217;s fraction 2) and Fr.B1 (CoWH-Ⅲ&#8217;s fraction 1) had antibacterial effects toward <i>Escherichia coli</i> and <i>Staphylococcus aureus</i>, with minimum antimicrobial mass concentrations of 65 mg/mL and 130 mg/mL for Fr.A2, and 130 mg/mL and 130 mg/mL for Fr.B1, respectively. The highly active antimicrobial peptides had high amounts of alkaline amino acids (28.13% in camel milk Fr.A2 and 25.07% in the cow milk Fr.B1) and hydrophobic amino acids. (51.29% in camel milk Fr.A2 and 57.69% in the cow milk Fr.B1). This results showed that hydrolysis of CaW and CoW using trypsin produced a variety of effective antimicrobial peptides against selected pathogens, and the antibacterial activity of camel milk whey was slightly higher than that of cow milk whey.https://www.mdpi.com/2076-2615/10/2/337camel milkcow milkultra-filtrationchromatographyamino acidantimicrobial peptide
collection DOAJ
language English
format Article
sources DOAJ
author Ruixue Wang
Zhihao Han
Rimutu Ji
Yuchen Xiao
Rendalai Si
Fucheng Guo
Jing He
Le Hai
Liang Ming
Li Yi
spellingShingle Ruixue Wang
Zhihao Han
Rimutu Ji
Yuchen Xiao
Rendalai Si
Fucheng Guo
Jing He
Le Hai
Liang Ming
Li Yi
Antibacterial Activity of Trypsin-Hydrolyzed Camel and Cow Whey and Their Fractions
Animals
camel milk
cow milk
ultra-filtration
chromatography
amino acid
antimicrobial peptide
author_facet Ruixue Wang
Zhihao Han
Rimutu Ji
Yuchen Xiao
Rendalai Si
Fucheng Guo
Jing He
Le Hai
Liang Ming
Li Yi
author_sort Ruixue Wang
title Antibacterial Activity of Trypsin-Hydrolyzed Camel and Cow Whey and Their Fractions
title_short Antibacterial Activity of Trypsin-Hydrolyzed Camel and Cow Whey and Their Fractions
title_full Antibacterial Activity of Trypsin-Hydrolyzed Camel and Cow Whey and Their Fractions
title_fullStr Antibacterial Activity of Trypsin-Hydrolyzed Camel and Cow Whey and Their Fractions
title_full_unstemmed Antibacterial Activity of Trypsin-Hydrolyzed Camel and Cow Whey and Their Fractions
title_sort antibacterial activity of trypsin-hydrolyzed camel and cow whey and their fractions
publisher MDPI AG
series Animals
issn 2076-2615
publishDate 2020-02-01
description Antibacterial peptides were isolated and purified from whey proteins of camel milk (CaW) and cow milk (CoW) and their antimicrobial activities were studied. The whey proteins were hydrolyzed using trypsin, and the degree of hydrolysis was identified by gel electrophoresis. The whey hydrolysate (WH) was purified using ultrafiltration and Dextran gel chromatography to obtain small peptides with antibacterial activity. The effect of the antimicrobial peptides on the morphology of bacterial strains was investigated using transmission electron microscopy. Their amino acid composition and antimicrobial activities were then determined. Polypeptides CaWH-III (&lt;3 kDa) and CoWH-III (&lt;3 kDa) had the strongest antibacterial activity. Both Fr.A2 (CaWH-Ⅲ&#8217;s fraction 2) and Fr.B1 (CoWH-Ⅲ&#8217;s fraction 1) had antibacterial effects toward <i>Escherichia coli</i> and <i>Staphylococcus aureus</i>, with minimum antimicrobial mass concentrations of 65 mg/mL and 130 mg/mL for Fr.A2, and 130 mg/mL and 130 mg/mL for Fr.B1, respectively. The highly active antimicrobial peptides had high amounts of alkaline amino acids (28.13% in camel milk Fr.A2 and 25.07% in the cow milk Fr.B1) and hydrophobic amino acids. (51.29% in camel milk Fr.A2 and 57.69% in the cow milk Fr.B1). This results showed that hydrolysis of CaW and CoW using trypsin produced a variety of effective antimicrobial peptides against selected pathogens, and the antibacterial activity of camel milk whey was slightly higher than that of cow milk whey.
topic camel milk
cow milk
ultra-filtration
chromatography
amino acid
antimicrobial peptide
url https://www.mdpi.com/2076-2615/10/2/337
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