넙치(Paralichthys olivaceus) 알로부터 등전점 가용화/침전공정으로 회수한 분리단백질의 식품기능성에 미치는 pH-shift의 영향
Influence of pH-shift on Food Functionality of Protein Isolates Recovered by Isoelectric Solubilization and Precipitation from Olive Flounder Paralichthys olivaceus Roes
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
We investigated the functional properties and in vitro bioactivity of protein isolates (RPIs) recovered from olive flounder Paralichthys olivaceus roes by isoelectric solubilization/precipitation process, according to pH-shift treatments. The buffer capacity of RPIs was shown to be stronger in alkaline pH than in acidic pH. Water holding capacity of RPIs was in range of 4.5–5.2 g/g protein with no significant differences (P>0.05). The foaming capacity and emulsifying activity index of RPIs did not show any significant differences between RPI-1 (pH 11/4.5) and 3 (pH 12/4.5), however they were superior to RPI-2 (pH 11/5.5) and 4 (pH 12/5.5). The 2,2′-azino-bis-3-ethylbenzo-thiazoline-6-sulfonic acid radical scavenging activity of RPI-3 (2.5 mg protein/mL) was 102.4 μg/mL, and the angiotensin I converting enzyme inhibitory activity was 30.8%. Among the RPIs, RPI-3 was relatively superior in protein functional properties such as buffer capacity, foaming capacity, emulsification, and anti-oxidative activity. Therefore, we suggest that RPI prepared from olive flounder roes could serve as a potential food resource.
Abstract
We investigated the functional properties and in vitro bioactivity of protein isolates (RPIs) recovered from olive flounder Paralichthys olivaceus roes by isoelectric solubilization/precipitation process, according to pH-shift treatments. The buffer capacity of RPIs was shown to be stronger in alkaline pH than in acidic pH. Water holding capacity of RPIs was in range of 4.5–5.2 g/g protein with no significant differences (P>0.05). The foaming capacity and emulsifying activity index of RPIs did not show any significant differences between RPI-1 (pH 11/4.5) and 3 (pH 12/4.5), however they were superior to RPI-2 (pH 11/5.5) and 4 (pH 12/5.5). The 2,2′-azino-bis-3-ethylbenzo-thiazoline-6-sulfonic acid radical scavenging activity of RPI-3 (2.5 mg protein/mL) was 102.4 μg/mL, and the angiotensin I converting enzyme inhibitory activity was 30.8%. Among the RPIs, RPI-3 was relatively superior in protein functional properties such as buffer capacity, foaming capacity, emulsification, and anti-oxidative activity. Therefore, we suggest that RPI prepared from olive flounder roes could serve as a potential food resource.
참고문헌 (54)
- Alvarez C, "Optimised protein recovery from mackerel whole fish by using sequential acid", alkaline isoelectric solubilization precipitation(ISP)extraction assisted by ultrasound, 2018, pp.88, 210~216
- Azadian M, "Comparison of functional properties and SDS-PAGE patterns between fish protein isolate and surimi produced from silver carp", Eur Food Res Technol, 235, pp.83~90 (2012)[DOI]
- Cha JW, "Food functionalities and bioactivities of protein isolates recovered from skipjack tuna roe by isoelectric solubilization and precipitation", Food Sci Nutri, 8, pp.1874~1887 (2020)[DOI]
- Chalamaiah M, "Chemical composition and functional properties of mrigal(Cirrhinus mrigala)egg protein concentrates and their application in pasta", J Food Sci Technol, 50, pp.514~520 (2013)[DOI]
- Chalamaiah M, "Chemical composition, molecular mass distribution and antioxidant capacity of rohu(Labeo rohita)roe(egg)protein hydrolysates prepared by gastrointestinal proteases", Food Res Int, 52, pp.221~229 (2013)[DOI]
- Choi JI, "Physiological properties of tuna cooking drip hydrolysate prepared with gamma irradiation", Process Biochem, 46, pp.1875~1878 (2011)[DOI]
- Choi JS, "Physiological properties of Engraulis japonicus muscle protein hydrolysates prepared by subcritical water hydrolysis", J Eviron Biol, 38, pp.283~289 (2017)[DOI]
- Damodaran S, "Food Proteins and Their Applications", pp.57~110 (1997), Marcel Dekker
- "New Fish Feeds Made from Fish Byproducts" (2010)[URL]
- Galla NR, "Physico-chemical, functional and antioxidant properties of roe protein concentrates from Cyprinus carpio and Epinephelus tauvina", J Food Pharm Sci, 1, pp.81~88 (2013)
- Galla NR, "Chemical and functional characterization of gum karaya(Sterculia urens L. )seed meal", Food Hydrocoll, 24, pp.479~485 (2010)[DOI]
- Galla NR, "Physico-chemical, amino acid composition, functional and antioxidant properties of roe protein concentrates obtained from Channa striatus and Lates calcarifer", Food Chem, 132, pp.1171~1176 (2012)[DOI]
- Galla NR, "Functional properties and in vitro antioxidant activity of roe protein hydrolysates of Channa striatus and Labeo rohita", Food Chem, 135, pp.1479~1484 (2012)[DOI]
- Guerard F, "Recent developments of marine ingredients for food and nutraceutical applications : A review", J Sci Hal Aquat, 2, pp.21~27 (2010)
- Heu MS, "Food component characteristics of skipjack(Katsuwonus pelamis)and yellowfin tuna(Thunnus albacares)roes", J Kor Fish Soc, 39, pp.1~8 (2006)[DOI]
- Himaya SWA, "An active peptide purified from gastrointestinal enzyme hydrolysate of Pacific cod skin gelatin attenuates angiotensin-1 converting enzyme(ACE)activity and cellular oxidative stress", Food Chem, 132, pp.1872~1882 (2012)[DOI]
- Hultin HO, "Process for isolating a protein composition from a muscle source and protein composition. US Patent No. 6,288,216 B1", Advanced Protein Technologies Inc, ~ (2011)
- Intarasirisawat R, "Antioxidative and functional properties of protein hydrolysate from defatted skipjack(Katsuwonous pelamis)roe", Food Chem, 135, pp.3039~3048 (2012)[DOI]
- Intarasirisawat R, "Effects of skipjack roe protein hydrolysate on properties and oxidative stability of fish emulsion sausage", LWT Food Sci Technol, 58, pp.280~286 (2014)[DOI]
- Intarasirisawat R, "Isolation of antioxidative and ACE inhibitory peptides from protein hydrolysate of skipjack(Katsuwana pelamis)roe", J Funct Foods, 5, pp.1854~1862 (2013)[DOI]
- Kadam SU, "Marine foods as functional ingredients in bakery and pasta products", Food Res Int, 43, pp.1975~1980 (2010)[DOI]
- Kang KT, "Food component characteristics of tuna livers", Food Sci Biotechnol, 16, pp.367~373 (2007)
- Kang SI, "Food characteristics of protein isolates recovered from olive flounder Paralichthys olivaceus roe by isoelectric solubilization and precipitation process", Korean J Fish Aquat Sci, 56, pp.162~173 (2023)[DOI]
- Karaca AC, "Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction", Food Res Int, 44, pp.2742~2750 (2011)[DOI]
- Kim JS, "Preparation off calcium powder from cooking skipjack tuna bone and its characteristics", J Korean Fish Soc, 33, pp.158~163 (2000)
- Kim SB, "Antioxidant and angiotensin I-converting enzyme inhibitory activities of northern shrimp(Pandalus borealis)by-products hydrolysate by enzymatic hydrolysis", Fish Aquat Sci, 19, pp.29~ (2016)[DOI]
- Kinsella JE, "Functional properties of proteins in foods : A survey", Crit Rev Food Sci Nutr, 7, pp.219~280 (1976)[DOI]
- Klompong V, "Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally(Selaroides leptolepis)as influenced by the degree of hydrolysis and enzyme type", Food Chem, 102, pp.1317~1327 (2007)[DOI]
- Kristinsson HG, "Fish protein hydrolysates : Production, biochemical and functional properties", Crit Rev Food Sci Nutr, 40, pp.43~81 (2000)[DOI]
- Kristinsson HG, "A comparative study between acid-and alkali-aided processing and surimi processing for the recovery of proteins from channel catfish muscle", J Food Sci, 70, pp.C298~C306 (2005)[DOI]
- Kwon IS, "Food characteristics of olive flounder Paralichthys olivaceus roe concentrates prepared using a cook-dried process", Korean J Fish Aquat Sci, 55, pp.791~801 (2022)[DOI]
- Lee GW, "Functionality and biological activity of isolate processed water generated during protein isolate preparation of fish roes using an isoelectric solubilization and precipitation process", Korean J Fish Aquat Sci, 50, pp.694~706 (2017)[DOI]
- Lee HJ, "Preparation and characterization of protein isolate from yellowfin tuna Thunnus albacares roe by isoelectric solubilization", precipitation process, 2016, pp.19, 14~
- Liu J, "Preparation of skipjack tuna(Katsuwonus pelamis)protein hydrolysate using combined controlled enzymatic hydrolysis and glycation for improved solubility and emulsifying properties", J Food Nutr Res, 3, pp.471~477 (2015)[DOI]
- Lowry OH, "Protein measurement with the Folin phenol reagent", J Biol Chem, 193, pp.265~275 (1951)
- Mahmoud KA, "Characterisation of the lipid fractions obtained by proteolytic and chemical extractions from rainbow trout(Oncorhynchus mykiss)roe", Process Biochem, 43, pp.376~383 (2008)[DOI]
- Mohamed BKF, "Influence of pH shift on functional properties of protein isolated of tilapia(Oreochromis niloticus)muscles and of soy protein isolate", Food Bioprocess Technol, 5, pp.2192~2200 (2012)[DOI]
- Mohan M, "Functional properties of rohu(Labeo rohita)proteins during iced storage", Food Res Int, 39, pp.847~854 (2006)[DOI]
- Mohan M, "Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet(Mugil cephalus)", Process Biochem, 42, pp.1056~1062 (2007)[DOI]
- Mutilangi WAM, "Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate", J Food Sci, 61, pp.270~274 (1996)[DOI]
- Ngo DH, "Active peptides from skate(Okamejei kenojei)skin gelatin diminish angiotensin-I converting enzyme activity and intracellular free radicalmediated oxidation", Food Chem, 143, pp.246~255 (2014)[DOI]
- Park SH, "Protein functionality of concentrates prepared from yellowfin tuna(Thunnus albacares)roe by cook-dried process", Food Sci Biotechnol, 25, pp.1569~1575 (2016)[DOI]
- Pearce KN, "Emulsifying properties of proteins. Evaluation of a turbidimetric technique", J Agric Food Chem, 26, pp.716~723 (1978)[DOI]
- Schurink M, "Novel peptides with tyrosinase inhibitory activity", Peptides, 28, pp.485~495 (2007)[DOI]
- Sikorski ZE, "Modification of technological properties of fish protein concentrates", Crit Rev Food Sci Nutr, 14, pp.201~230 (1981)[DOI]
- Tan ES, "A comparative study of physicochemical characteristics and functionalities of pinto bean protein isolate(PBPI)against the soybean protein isolate(SPI)after the extraction optimisation", Food Chem, 152, pp.447~455 (2014)[DOI]
- Wu HC, "Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel(Scomber austriasicus)", Food Res Int, 36, pp.949~957 (2003)[DOI]
- Yoon IS, "Food functionality and bioactivity of vacuum freeze-dried fish roe concentrates", Korean J Fish Aquat Sci, 53, pp.403~416 (2020)[DOI]
- Yoon IS, "Food functionality of collagenous protein fractions recovered from fish roe by alkaline solubilization", Korean J Fish and Aquat Sci, 51, pp.351~361 (2018)[DOI]
- Yoon IS, "Food functionality and biological activity of processed waters produced during the preparation of fish roe concentrates by cook-dried process", Korean J Fish Aquat Sci, 50, pp.506~519 (2017)[DOI]
- Yoon IS, "Chemical composition and functional properties of roe concentrates from skipjack tuna(Katsuwonus pelamis)by cook-dried process", Food Sci Nutr, 6, pp.1276~1286 (2018)[DOI]
- Yoon IS, "Food functionality of protein isolates extracted from yellowfin tuna(Thunnus albacares)roe using alkaline solubilization and acid precipitation process", Food Sci Nutri, 7, pp.412~424 (2019)[DOI]
- Yoon IS, "Food functionality and in vitro bioactivity of olive flounder Paralichthys olivaceus roe concentrates prepared by cook-dried process", Korean J Fish Aquat Sci, 56, pp.7~20 (2023)[DOI]
- You L, "Purification and identification of antioxidative peptides from loach(Misgurnus anguillicaudatus)protein hydrolysate by consecutive chromatography and electrospray ionization-mass spectrometry", Food Res Int, 43, pp.1167~1173 (2010)[DOI]
