Separation of Iron-Binding Peptides from Shrimp Processing By-products Hydrolysates

Huang, Guangrong; Ren, Zhang-yan; Jiang, Jiaxin

doi:10.1007/s11947-010-0416-3

Cited by 77 publications

(47 citation statements)

References 45 publications

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“…Lee and Song (2009) isolated an iron-binding nona-peptide, Asp-Leu-Gly-GluGln-Tyr-Phe-Lys-Gly, molecular weight of 1055 Da, from porcine blood plasma protein hydrolysate with Flavourzyme. Huang et al (2012) obtained a hepta-peptide (699 Da) with iron-binding ability from shrimp processing byproducts hydrolysate.…”

Section: Results and Discussion Molecular Weight Distribution Of The mentioning

confidence: 99%

Stability of Mackerel (Trachurus japonicas) Hydrolysate with Iron-Binding Capacity in Simulated Gastrointestinal Fluids

Zhang¹,

Sun²,

Huang³

2015

American J. of Food Technology

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The aim of this study was to investigate the stability of mackerel (Trachurus japonicas) processing byproducts protein hydrolysate with iron-binding capacity in vitro simulated gastrointestinal systems. The changes in molecular weight distribution and iron-binding capacity were used for evaluating the stability of the hydrolysate in simulated gastrointestinal digestion. The molecular weight of mackerel hydrolysate with iron-binding capacity was mostly less than 1300 Da and composted mainly by tripeptides to undepeptides. The hydrolysate was stable in gastric or intestinal digestion separately for 5 h, or two-stage gastrointestinal digestion. The iron-binding capacity did not change significantly during gastrointestinal digestion. The mackerel processing byproducts hydrolysate had potential in iron fortification functional ingredients of food industry.

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Section: Results and Discussion Molecular Weight Distribution Of The mentioning

confidence: 99%

Stability of Mackerel (Trachurus japonicas) Hydrolysate with Iron-Binding Capacity in Simulated Gastrointestinal Fluids

Zhang¹,

Sun²,

Huang³

2015

American J. of Food Technology

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“…With enzymatic hydrolysis, more and more small peptides produced. But many reports showed that the iron or ferrous binding ability of peptides did not show positive or negative relationship with molecular weight of peptides (Wu et al, 2012;Huang et al, 2011;Kim et al, 2014). Therefore, high FAB hydrolysis time might be one of any points during whole hydrolysis process.…”

Section: Effects Of Hydrolysis Time and Enzyme Additive Amountmentioning

confidence: 98%

“…Hence, iron fertilization in food is an effective defending method for iron deficiency. In order to uptake iron absorption rate, there have been many studies about non-heme iron binding bioactive peptides in recent years (Lee and Song, 2009;Huang et al, 2011;Torres-Fuentes et al, 2012;Kim et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Optimization of Enzymatic Hydrolysis for Producing Ferrous Binding Peptides from Horse Mackerel (Trachurus japonicus) Processing Byproducts

Yang¹,

Zhen²,

Song³

et al. 2015

Biotechnology

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A B S T R A C T Marine fish processing byproducts were considered as potential good protein resource for producing bioactive peptides by enzymatic hydrolysis. In this study, hydrolysates with high ferrous binding ability were prepared by enzymatic hydrolysis from mackerel (Trachurus japonicus) processing byproducts. In order to get hydrolysates of high ferrous binding ability and degree of hydrolysis, the enzymatic hydrolysis conditions were optimized, including proteases type, hydrolysis time, temperature, pH and enzyme to substrate ratio. The results showed that the hydrolysate by alcalase had the highest ferrous binding ability and degree of hydrolysis, reaching to 9.8 and 49.0%, respectively. The best hydrolysis conditions of alcalase were optimized using response surface methodology to be: pH 9.0, temperature of 50°C, enzyme substrate ratio of 160 mg/100 mL, hydrolysis time of 100 min. The ferrous binding ability and degree of hydrolysis were reached to 48.0 and 45.4%, respectively, at these optimized hydrolysis conditions.

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“…특히 단백 질에 비해 크기가 작은 생리 활성 펩타이드는 생체내로 쉽게 흡수 될 수 있으며, 다양한 기능적 특성을 갖는다 [10]. 생리활성 팹타이드의 효과로는 미네랄운송 [11,12], 항고혈압 [13], 항균활성 [14] …”

Section: 서론unclassified

Optimization of enzymatic hydrolysis of viscera waste proteins of black body fowl(Yeonsan Ogae) to produce peptides using a commercial protease and it's characters analysis

Choi¹,

Kim²,

Song³

et al. 2016

Journal of Digital Convergence

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요 약 연산오계는 오래전부터 건강기능 증진 및 치료 효능이 높은 것으로 알려져 왔다. 최근 건강 기능식품 소재 로 기능성 펩타이드 효능이 알려짐에 따라, 연산오계 내장 부산물로 부터 올리고 펩타이드 최적 생산 공정 및 생성주제어 : 연산오계, 내장, 펩타이드, 효소 가수분해, 최적 공정 Abstract Yeonsan Ogae has been known as supporting health and high efficacy of treatment. In recent days, as the efficacy of functional peptides has known, the optimization of oligo peptides production and its characteristics from Ogae viscera has been performed. Response surface method was used to perform the optimizaion of enzyme hydrolysis. The range of processes was temperature ( 40, 50 and 60℃ ), pH( 6.0, 7.0 and 8.0 ), and enzyme( 1, 2 and 3% ). The degree of hydrolysis, amono acids, molecular weight of products were analyzed. The optimum process of enzyme hydrolysis were determined as temperature 58℃, pH 7.5, and enzyme concetration 3%. At optimum conditions, the degree of hydrolysis after 2 h reaction was 75-80%. The total amino acids of amino acid and were 386.15 mg/100 g and 155.26 mg/100 g, respectively. The molecular weight of products by using Maldi-TOF was ranged from 300 to 1,000 Da.

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Separation of Iron-Binding Peptides from Shrimp Processing By-products Hydrolysates

Cited by 77 publications

References 45 publications

Stability of Mackerel (Trachurus japonicas) Hydrolysate with Iron-Binding Capacity in Simulated Gastrointestinal Fluids

Stability of Mackerel (Trachurus japonicas) Hydrolysate with Iron-Binding Capacity in Simulated Gastrointestinal Fluids

Optimization of Enzymatic Hydrolysis for Producing Ferrous Binding Peptides from Horse Mackerel (Trachurus japonicus) Processing Byproducts

Optimization of enzymatic hydrolysis of viscera waste proteins of black body fowl(Yeonsan Ogae) to produce peptides using a commercial protease and it's characters analysis

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