Preparation of Angiotensin Converting Enzyme (ACE) Inhibitory Peptide from Abalone<i>(Haliotis discus hannai)</i> Mantle Membrane by Serine Protease in Shrimp<i>(Litopenaeus vannamei)</i> Digestive Gland

JI Mengya; WAN Chujun; WENG Ling; MA Ting; ZHANG Lingjing; ZHANG Qian; CAO Minjie

doi:10.13386/j.issn1002-0306.2021080046

Volume 43 Issue 10

May 2022

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Science and Technology of Food Industry > 2022 > 43(10): 73-79. > DOI: 10.13386/j.issn1002-0306.2021080046

JI Mengya, WAN Chujun, WENG Ling, et al. Preparation of Angiotensin Converting Enzyme (ACE) Inhibitory Peptide from Abalone(Haliotis discus hannai) Mantle Membrane by Serine Protease in Shrimp(Litopenaeus vannamei) Digestive Gland[J]. Science and Technology of Food Industry, 2022, 43(10): 73−79. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2021080046.

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Preparation of Angiotensin Converting Enzyme (ACE) Inhibitory Peptide from Abalone(Haliotis discus hannai) Mantle Membrane by Serine Protease in Shrimp(Litopenaeus vannamei) Digestive Gland

College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China

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Received Date: August 04, 2021
Available Online: April 11, 2022

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Abstract

Abstract

The abalone (Haliotis discus hannai) mantle processing by-products was used to prepare biologically active peptides with inhibiting the activity of angiotensin converting enzyme (ACE), which provided a new idea for the high-value utilization of abalone processing by-products. The serine protease prepared from the digestive glands of Litopenaeus vannamei was used to enzymatically hydrolyze the mantle proteins of Haliotis discus hannai. The ACE inhibitory activity of the enzymatic hydrolysate was used as the evaluation index to optimize the digestion conditions. After the enzymatic hydrolysis solution passed through the 3 kDa ultrafiltration membrane, the active components were separated and purified by Superdex peptide 10/300 GL gel filtration column and reversed-phase high performance liquid chromatography (RP-HPLC). Liquid chromatography tandem mass spectrometry (LC-MS/MS) was used to identify the amino acid sequence of the purified peptide. The results showed that the ACE inhibition rate of the enzymatic hydrolysate was 13.42%. After preliminary separation by the 3 kDa ultrafiltration membrane, the ACE inhibition rate of the fractions less than 3 kDa at the same concentration was 53.25%. After further purification by gel filtration column and RP-HPLC, five peptides were identified from the peak with the highest ACE inhibitory activity. The sequences were LGDSFYYGK, LVNEVTEFAK, VDEVGGEALGR, MFLSFPTTK, VATVSLPR, indicating that the active peak was a mixture of peptides. Preparation of ACE inhibitory peptides using abalone mantle could provide a theoretical reference for the high-value utilization of the processing by-products of abalone and prawn.
- Haliotis discus hannai,
- mantle,
- serine proteinase,
- (ACE) inhibitory peptides

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