Isolation, Identification, and Biological Activity Analysis of Swim Bladder Polypeptides from <i<Acipenser schrencki</i<

Swim bladder polypeptides (SBPs) of <i<Acipenser schrencki</i< were analyzed for their antioxidant activity and physicochemical properties. The results showed the optimal enzymatic conditions were alkaline protease with a solid-to-liquid ratio of 1:20, an incubation time of 4 h, a temper...
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Autor*in:	Xiao-Yan Zu [verfasserIn] Wen-Bo Liu [verfasserIn] Guang-Quan Xiong [verfasserIn] Tao Liao [verfasserIn] Hai-Lan Li [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	swim bladder polypeptides antioxidant peptides peptide sequence

Übergeordnetes Werk:	In: Foods - MDPI AG, 2013, 12(2023), 10, p 1934
Übergeordnetes Werk:	volume:12 ; year:2023 ; number:10, p 1934

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/foods12101934

Katalog-ID:	DOAJ094382816

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520			\|a Swim bladder polypeptides (SBPs) of <i<Acipenser schrencki</i< were analyzed for their antioxidant activity and physicochemical properties. The results showed the optimal enzymatic conditions were alkaline protease with a solid-to-liquid ratio of 1:20, an incubation time of 4 h, a temperature of 55 °C, and an enzyme dosage of 5000 U/g. Three different molecular weight fractions (F1, F2, and F3) were obtained via ultrafiltration. F3 (912.44–2135.82 Da) showed 77.90%, 72.15%, and 66.25% removal of O<sub<2</sub<•<sup<-</sup<, DPPH•, and •OH, respectively, at 10 mg/mL, which was significantly higher than the F1 and F2 fractions (<i<p</i< < 0.05). F3 contained proline (6.17%), hydroxyproline (5.28%), and hydrophobic amino acids (51.39%). The UV spectrum of F3 showed maximum absorption at 224 nm. Peptide sequence analysis showed that F3 contained antioxidant peptides (MFGF, GPPGPRGPPGL, and GPGPSGERGPPGPM) and exhibited inhibitory activities on angiotensin-converting enzyme and dipeptidyl peptidase III/IV (FRF, FPFL and LPGLF). F3 was considered a good raw material for obtaining bioactive peptides.
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language	English
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callnumber-first	T - Technology
author	Xiao-Yan Zu
spellingShingle	Xiao-Yan Zu misc TP1-1185 misc <i<Acipenser schrencki</i< misc swim bladder polypeptides misc antioxidant peptides misc peptide sequence misc Chemical technology Isolation, Identification, and Biological Activity Analysis of Swim Bladder Polypeptides from <i<Acipenser schrencki</i<
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topic_title	TP1-1185 Isolation, Identification, and Biological Activity Analysis of Swim Bladder Polypeptides from <i<Acipenser schrencki</i< <i<Acipenser schrencki</i< swim bladder polypeptides antioxidant peptides peptide sequence
topic	misc TP1-1185 misc <i<Acipenser schrencki</i< misc swim bladder polypeptides misc antioxidant peptides misc peptide sequence misc Chemical technology
topic_unstemmed	misc TP1-1185 misc <i<Acipenser schrencki</i< misc swim bladder polypeptides misc antioxidant peptides misc peptide sequence misc Chemical technology
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title	Isolation, Identification, and Biological Activity Analysis of Swim Bladder Polypeptides from <i<Acipenser schrencki</i<
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title_full	Isolation, Identification, and Biological Activity Analysis of Swim Bladder Polypeptides from <i<Acipenser schrencki</i<
author_sort	Xiao-Yan Zu
journal	Foods
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author_browse	Xiao-Yan Zu Wen-Bo Liu Guang-Quan Xiong Tao Liao Hai-Lan Li
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doi_str_mv	10.3390/foods12101934
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title_sort	isolation, identification, and biological activity analysis of swim bladder polypeptides from <i<acipenser schrencki</i<
callnumber	TP1-1185
title_auth	Isolation, Identification, and Biological Activity Analysis of Swim Bladder Polypeptides from <i<Acipenser schrencki</i<
abstract	Swim bladder polypeptides (SBPs) of <i<Acipenser schrencki</i< were analyzed for their antioxidant activity and physicochemical properties. The results showed the optimal enzymatic conditions were alkaline protease with a solid-to-liquid ratio of 1:20, an incubation time of 4 h, a temperature of 55 °C, and an enzyme dosage of 5000 U/g. Three different molecular weight fractions (F1, F2, and F3) were obtained via ultrafiltration. F3 (912.44–2135.82 Da) showed 77.90%, 72.15%, and 66.25% removal of O<sub<2</sub<•<sup<-</sup<, DPPH•, and •OH, respectively, at 10 mg/mL, which was significantly higher than the F1 and F2 fractions (<i<p</i< < 0.05). F3 contained proline (6.17%), hydroxyproline (5.28%), and hydrophobic amino acids (51.39%). The UV spectrum of F3 showed maximum absorption at 224 nm. Peptide sequence analysis showed that F3 contained antioxidant peptides (MFGF, GPPGPRGPPGL, and GPGPSGERGPPGPM) and exhibited inhibitory activities on angiotensin-converting enzyme and dipeptidyl peptidase III/IV (FRF, FPFL and LPGLF). F3 was considered a good raw material for obtaining bioactive peptides.
abstractGer	Swim bladder polypeptides (SBPs) of <i<Acipenser schrencki</i< were analyzed for their antioxidant activity and physicochemical properties. The results showed the optimal enzymatic conditions were alkaline protease with a solid-to-liquid ratio of 1:20, an incubation time of 4 h, a temperature of 55 °C, and an enzyme dosage of 5000 U/g. Three different molecular weight fractions (F1, F2, and F3) were obtained via ultrafiltration. F3 (912.44–2135.82 Da) showed 77.90%, 72.15%, and 66.25% removal of O<sub<2</sub<•<sup<-</sup<, DPPH•, and •OH, respectively, at 10 mg/mL, which was significantly higher than the F1 and F2 fractions (<i<p</i< < 0.05). F3 contained proline (6.17%), hydroxyproline (5.28%), and hydrophobic amino acids (51.39%). The UV spectrum of F3 showed maximum absorption at 224 nm. Peptide sequence analysis showed that F3 contained antioxidant peptides (MFGF, GPPGPRGPPGL, and GPGPSGERGPPGPM) and exhibited inhibitory activities on angiotensin-converting enzyme and dipeptidyl peptidase III/IV (FRF, FPFL and LPGLF). F3 was considered a good raw material for obtaining bioactive peptides.
abstract_unstemmed	Swim bladder polypeptides (SBPs) of <i<Acipenser schrencki</i< were analyzed for their antioxidant activity and physicochemical properties. The results showed the optimal enzymatic conditions were alkaline protease with a solid-to-liquid ratio of 1:20, an incubation time of 4 h, a temperature of 55 °C, and an enzyme dosage of 5000 U/g. Three different molecular weight fractions (F1, F2, and F3) were obtained via ultrafiltration. F3 (912.44–2135.82 Da) showed 77.90%, 72.15%, and 66.25% removal of O<sub<2</sub<•<sup<-</sup<, DPPH•, and •OH, respectively, at 10 mg/mL, which was significantly higher than the F1 and F2 fractions (<i<p</i< < 0.05). F3 contained proline (6.17%), hydroxyproline (5.28%), and hydrophobic amino acids (51.39%). The UV spectrum of F3 showed maximum absorption at 224 nm. Peptide sequence analysis showed that F3 contained antioxidant peptides (MFGF, GPPGPRGPPGL, and GPGPSGERGPPGPM) and exhibited inhibitory activities on angiotensin-converting enzyme and dipeptidyl peptidase III/IV (FRF, FPFL and LPGLF). F3 was considered a good raw material for obtaining bioactive peptides.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
container_issue	10, p 1934
title_short	Isolation, Identification, and Biological Activity Analysis of Swim Bladder Polypeptides from <i<Acipenser schrencki</i<
url	https://doi.org/10.3390/foods12101934 https://doaj.org/article/be63290bcead465899a715376491c6eb https://www.mdpi.com/2304-8158/12/10/1934 https://doaj.org/toc/2304-8158
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Isolation, Identification, and Biological Activity Analysis of Swim Bladder Polypeptides from <i<Acipenser schrencki</i<

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