Recovery of value‐added glycopeptides from edible bird's nest (EBN) co‐products: enzymatic hydrolysis, physicochemical characteristics and bioactivity

BACKGROUND Processing of edible bird's nest (EBN) requires extensive washing to remove impurities and produces huge amounts of EBN co‐products, which contain mainly feathers with glycoproteins attached, which are usually discarded. This study was conducted to recover the valuable EBN glycoprote...

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Veröffentlicht in:Journal of the science of food and agriculture 2020-10, Vol.100 (13), p.4714-4722
Hauptverfasser: Ling, Jin Wei Alvin, Chang, Lee Sin, Babji, Abdul Salam, Lim, Seng Joe
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creator Ling, Jin Wei Alvin
Chang, Lee Sin
Babji, Abdul Salam
Lim, Seng Joe
description BACKGROUND Processing of edible bird's nest (EBN) requires extensive washing to remove impurities and produces huge amounts of EBN co‐products, which contain mainly feathers with glycoproteins attached, which are usually discarded. This study was conducted to recover the valuable EBN glycoproteins from the waste material. Enzymatic hydrolysis was applied to recover EBN glycopeptides from EBN co‐products (EBNcoP) and processed cleaned EBN (EBNclean) was used as control, which were then freeze‐dried into EBN hydrolysates (EBNhcoP and EBNhclean, respectively). RESULTS The recovery yield for EBNhclean and EBNhcoP were 89.09 ± 0.01% and 47.64 ± 0.26%, respectively, indicating nearly 50% of glycopeptide can be recovered from the waste material. Meanwhile, N‐acetylneuraminic acid, a major acid sugar in EBN glycoproteins, of EBNhcoP increased by 229% from 58.6 ± 3.9 to 192.9 ± 3.1 g kg−1, indicating the enzymatic hydrolysis removed impurities and thus enhanced the N‐acetylneuraminic acid content. Total soluble protein was more than 330 g kg−1 for all the samples. Colour parameter showed that hydrolysate samples have greater L* (lightness) values. Chroma result indicates the intensity of all the samples were low (
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This study was conducted to recover the valuable EBN glycoproteins from the waste material. Enzymatic hydrolysis was applied to recover EBN glycopeptides from EBN co‐products (EBNcoP) and processed cleaned EBN (EBNclean) was used as control, which were then freeze‐dried into EBN hydrolysates (EBNhcoP and EBNhclean, respectively). RESULTS The recovery yield for EBNhclean and EBNhcoP were 89.09 ± 0.01% and 47.64 ± 0.26%, respectively, indicating nearly 50% of glycopeptide can be recovered from the waste material. Meanwhile, N‐acetylneuraminic acid, a major acid sugar in EBN glycoproteins, of EBNhcoP increased by 229% from 58.6 ± 3.9 to 192.9 ± 3.1 g kg−1, indicating the enzymatic hydrolysis removed impurities and thus enhanced the N‐acetylneuraminic acid content. Total soluble protein was more than 330 g kg−1 for all the samples. Colour parameter showed that hydrolysate samples have greater L* (lightness) values. Chroma result indicates the intensity of all the samples were low (&lt; 11). Fourier‐transform infrared (FTIR) spectrum displayed that the EBNhcoP exhibited similar functional groups with EBNhclean, indicating that the EBNcoP has similar functionality as EBNclean. Significantly higher (P ≤ 0.05) 1,1‐diphenyl‐2‐picrylhydrazyl (DPPH) and ferric reducing antioxidant power (FRAP) activities were reported in EBNhcoP after the enzymatic reaction. CONCLUSION EBNhcoP were successfully recovered from low value EBNcoP with enhanced antioxidant activities. The findings of this work are beneficial for the EBN industry to reduce wastage and enhance economic values of EBN co‐products, both economically and nutritionally. © 2020 Society of Chemical Industry</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.10530</identifier><identifier>PMID: 32468613</identifier><language>eng</language><publisher>Chichester, UK: John Wiley &amp; Sons, Ltd</publisher><subject>Animals ; Antibiotics ; Antioxidants ; Antioxidants - chemistry ; Antioxidants - isolation &amp; purification ; Biocatalysis ; Biological activity ; Biological Products - chemistry ; Biological Products - isolation &amp; purification ; Birds ; Economic conditions ; edible bird's nest ; Enzymes - chemistry ; Feathers - chemistry ; Food Handling - methods ; FTIR ; Functional groups ; glycopeptide ; Glycopeptides ; Glycopeptides - chemistry ; Glycopeptides - isolation &amp; purification ; Glycoproteins ; Hydrolysates ; Hydrolysis ; Impurities ; Infrared radiation ; N‐acetylneuraminic acid ; Recovery ; Saliva - chemistry ; Waste materials</subject><ispartof>Journal of the science of food and agriculture, 2020-10, Vol.100 (13), p.4714-4722</ispartof><rights>2020 Society of Chemical Industry</rights><rights>2020 Society of Chemical Industry.</rights><rights>Copyright © 2020 Society of Chemical Industry</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3570-4449179438dabd5443a54d632c0f7a75260e3801d2c0ff775a3ac171978ca47d3</citedby><cites>FETCH-LOGICAL-c3570-4449179438dabd5443a54d632c0f7a75260e3801d2c0ff775a3ac171978ca47d3</cites><orcidid>0000-0002-9460-5136 ; 0000-0002-5694-3943</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjsfa.10530$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.10530$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32468613$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ling, Jin Wei Alvin</creatorcontrib><creatorcontrib>Chang, Lee Sin</creatorcontrib><creatorcontrib>Babji, Abdul Salam</creatorcontrib><creatorcontrib>Lim, Seng Joe</creatorcontrib><title>Recovery of value‐added glycopeptides from edible bird's nest (EBN) co‐products: enzymatic hydrolysis, physicochemical characteristics and bioactivity</title><title>Journal of the science of food and agriculture</title><addtitle>J Sci Food Agric</addtitle><description>BACKGROUND Processing of edible bird's nest (EBN) requires extensive washing to remove impurities and produces huge amounts of EBN co‐products, which contain mainly feathers with glycoproteins attached, which are usually discarded. This study was conducted to recover the valuable EBN glycoproteins from the waste material. Enzymatic hydrolysis was applied to recover EBN glycopeptides from EBN co‐products (EBNcoP) and processed cleaned EBN (EBNclean) was used as control, which were then freeze‐dried into EBN hydrolysates (EBNhcoP and EBNhclean, respectively). RESULTS The recovery yield for EBNhclean and EBNhcoP were 89.09 ± 0.01% and 47.64 ± 0.26%, respectively, indicating nearly 50% of glycopeptide can be recovered from the waste material. Meanwhile, N‐acetylneuraminic acid, a major acid sugar in EBN glycoproteins, of EBNhcoP increased by 229% from 58.6 ± 3.9 to 192.9 ± 3.1 g kg−1, indicating the enzymatic hydrolysis removed impurities and thus enhanced the N‐acetylneuraminic acid content. Total soluble protein was more than 330 g kg−1 for all the samples. Colour parameter showed that hydrolysate samples have greater L* (lightness) values. Chroma result indicates the intensity of all the samples were low (&lt; 11). Fourier‐transform infrared (FTIR) spectrum displayed that the EBNhcoP exhibited similar functional groups with EBNhclean, indicating that the EBNcoP has similar functionality as EBNclean. Significantly higher (P ≤ 0.05) 1,1‐diphenyl‐2‐picrylhydrazyl (DPPH) and ferric reducing antioxidant power (FRAP) activities were reported in EBNhcoP after the enzymatic reaction. CONCLUSION EBNhcoP were successfully recovered from low value EBNcoP with enhanced antioxidant activities. 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This study was conducted to recover the valuable EBN glycoproteins from the waste material. Enzymatic hydrolysis was applied to recover EBN glycopeptides from EBN co‐products (EBNcoP) and processed cleaned EBN (EBNclean) was used as control, which were then freeze‐dried into EBN hydrolysates (EBNhcoP and EBNhclean, respectively). RESULTS The recovery yield for EBNhclean and EBNhcoP were 89.09 ± 0.01% and 47.64 ± 0.26%, respectively, indicating nearly 50% of glycopeptide can be recovered from the waste material. Meanwhile, N‐acetylneuraminic acid, a major acid sugar in EBN glycoproteins, of EBNhcoP increased by 229% from 58.6 ± 3.9 to 192.9 ± 3.1 g kg−1, indicating the enzymatic hydrolysis removed impurities and thus enhanced the N‐acetylneuraminic acid content. Total soluble protein was more than 330 g kg−1 for all the samples. Colour parameter showed that hydrolysate samples have greater L* (lightness) values. Chroma result indicates the intensity of all the samples were low (&lt; 11). Fourier‐transform infrared (FTIR) spectrum displayed that the EBNhcoP exhibited similar functional groups with EBNhclean, indicating that the EBNcoP has similar functionality as EBNclean. Significantly higher (P ≤ 0.05) 1,1‐diphenyl‐2‐picrylhydrazyl (DPPH) and ferric reducing antioxidant power (FRAP) activities were reported in EBNhcoP after the enzymatic reaction. CONCLUSION EBNhcoP were successfully recovered from low value EBNcoP with enhanced antioxidant activities. The findings of this work are beneficial for the EBN industry to reduce wastage and enhance economic values of EBN co‐products, both economically and nutritionally. © 2020 Society of Chemical Industry</abstract><cop>Chichester, UK</cop><pub>John Wiley &amp; Sons, Ltd</pub><pmid>32468613</pmid><doi>10.1002/jsfa.10530</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-9460-5136</orcidid><orcidid>https://orcid.org/0000-0002-5694-3943</orcidid></addata></record>
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source MEDLINE; Wiley Online Library Journals Frontfile Complete
subjects Animals
Antibiotics
Antioxidants
Antioxidants - chemistry
Antioxidants - isolation & purification
Biocatalysis
Biological activity
Biological Products - chemistry
Biological Products - isolation & purification
Birds
Economic conditions
edible bird's nest
Enzymes - chemistry
Feathers - chemistry
Food Handling - methods
FTIR
Functional groups
glycopeptide
Glycopeptides
Glycopeptides - chemistry
Glycopeptides - isolation & purification
Glycoproteins
Hydrolysates
Hydrolysis
Impurities
Infrared radiation
N‐acetylneuraminic acid
Recovery
Saliva - chemistry
Waste materials
title Recovery of value‐added glycopeptides from edible bird's nest (EBN) co‐products: enzymatic hydrolysis, physicochemical characteristics and bioactivity
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