Enzymatic Preparation and Sequence Analysis of Antioxidant Peptides from Chicken Lung

YIN Jiaqi; KANG Mingli; HAN Minyi; LI Lingyun; WANG Xiaoming; XU Xinglian

doi:10.13386/j.issn1002-0306.2021090176

Volume 43 Issue 10

May 2022

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Science and Technology of Food Industry > 2022 > 43(10): 112-123. > DOI: 10.13386/j.issn1002-0306.2021090176

YIN Jiaqi, KANG Mingli, HAN Minyi, et al. Enzymatic Preparation and Sequence Analysis of Antioxidant Peptides from Chicken Lung[J]. Science and Technology of Food Industry, 2022, 43(10): 112−123. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2021090176.

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Enzymatic Preparation and Sequence Analysis of Antioxidant Peptides from Chicken Lung

YIN Jiaqi^{1, 2,},
KANG Mingli³,
HAN Minyi^{1, 2, 4, ,},
LI Lingyun⁴,
WANG Xiaoming⁴,
XU Xinglian^{1, 2}

1.
College of Food Technology, Nanjing Agricultural University, Nanjing 210095, China
2.
Key Laboratory of Meat Products Processing, Ministry of Agriculture, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Nanjing 210095, China
3.
College of Food Science and Biology, Hebei University of Science and Technology, Shijiazhuang 050018, China
4.
Wens Food Group Co., Ltd., Yunfu 527400, China

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Received Date: September 13, 2021
Available Online: March 16, 2022

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Abstract

Abstract

Chicken lung is generally utilized as a low-value feed in poultry slaughtering industry. In order to increase the added value of chicken lung, this study determined the proximate chemical composition of chicken lung and prepared antioxidant peptide by enzymatic hydrolysis. Firstly, using 1, 1-diphenyl-2-picrylhydrazyl (DPPH) scavenging rate and crude peptide content as indexes, the effects of the kinds of enzyme, pH, enzyme supplemental levels and hydrolysis time on antioxidant peptide activity were investigated by single factor experiment. Secondly, based on the results, Box-Behnken response surface designed was used to optimize the reaction conditions for enzymatic hydrolysis of chicken lung antioxidant peptide. The main influencing factors were pH, enzyme supplemental levels and hydrolysis time (P<0.05). The optimal conditions were obtained as follows: pH3.60, enzyme supplemental levels 4200 U/g, hydrolysis time 5 h. The DPPH· scavenging rate and crude peptide content in the validation test were 94.96% and 88.42%, respectively. Thirdly, compared with the supernatant of chicken lung homogenate, the free amino acid content of the crude peptide increased significantly (P<0.05). Finally, among the ultrafiltration products, the <3 kDa component had the strongest antioxidant capacity while the proportion of molecular weight <1000 Da was 86.70%. Liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) sequencing revealed that peptides with water residue ratio ≥50% were 60.97%. Meanwhile, Val and Leu accounted for 48.78% of the total N-terminal frequency of occurrence from peptide. The present results could provide theoretical and technical support for the comprehensive utilization of chicken lung.
- antioxidant peptide,
- enzymatic hydrolysis,
- process optimization,
- amino acid composition,
- peptide sequence determination

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References (47)

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