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Rossawan Intarasirisawat - One of the best experts on this subject based on the ideXlab platform.
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skipjack roe Protein Hydrolysate combined with tannic acid increases the stability of fish oil upon microencapsulation
European Journal of Lipid Science and Technology, 2015Co-Authors: Rossawan Intarasirisawat, Soottawat Benjakul, Wonnop Vissessanguan, Sajid Maqsood, Kazufumi OsakoAbstract:Microencapsulation of fish oil was achieved by spray drying the micro-emulsion, in which skipjack roe Protein Hydrolysate (SRPH: degree of hydrolysis, 5%) was used as the wall material in the absence or presence of tannic acid (TA) or oxidized tannic acid (OTA). Microcapsule using SRPH had a lower encapsulation efficiency (EE) than those having sodium caseinate-whey Protein concentrate (Ca-WPC) as the wall materials (p < 0.05). The incorporation of TA or OTA in combination with SRPH yielded spherical encapsulated fish oil with higher EE but lower particle size (p < 0.05) than achieved with SRPH alone. Furthermore, the addition of TA retarded lipid oxidation of microcapsule more effectively as indicated by lower peroxide value and thiobarbituric acid reactive substances (TBARS) value during storage at 30°C for 4 weeks, compared with those using only SRPH (p < 0.05). Nevertheless, OTA in conjunction with SRPH yielded the higher EE than TA. Therefore, SRPH could serve as an alternative wall material for microencapsulation of fish oil, especially with the aid of TA or OTA. Practical application: SRPH having 5% DH in the presence of TA as wall materials could be alternatively used to encapsulate fish oil. The use of SRPH-TA could improve EE and oxidative stability of the obtained fish oil microcapsule. The fish oil microcapsule prepared using SRPH and TA could be incorporated in food products for increasing nutritive value. Additionally, the utilization of skipjack roe, which is a by-product of the tuna canning industry, can be maximized. Scanning electron micrographs of fish oil microencapsules prepared using different wall materials. SRPH: Skipjack roe Protein Hydrolysate, TA: Tannic acid, OTA: Oxidized tannic acid, Ca-WPC: Sodium caseinate-whey Protein concentrate. Magnification at 3,000×.
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Effects of skipjack roe Protein Hydrolysate on properties and oxidative stability of fish emulsion sausage
LWT - Food Science and Technology, 2014Co-Authors: Rossawan Intarasirisawat, Wonnop Visessanguan, Jianping WuAbstract:Effects of skipjack roe Protein Hydrolysate (SRPH) at various levels (0-3 g/100g) on properties and oxidative stability of emulsion sausage from broadhead catfish (Clarias macrocephalus) fortified with skipjack tuna roe lipids were investigated. The addition of SRPH increased hardness, cohesiveness and resilience of sausage (p
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isolation of antioxidative and ace inhibitory peptides from Protein Hydrolysate of skipjack katsuwana pelamis roe
Journal of Functional Foods, 2013Co-Authors: Rossawan Intarasirisawat, Soottawat Benjakul, Wonnop VisessanguanAbstract:Abstract Bioactive peptides from Protein Hydrolysate of defatted skipjack ( Katsuwonus pelamis ) roe with 5% degree of hydrolysis (DH) prepared by Alcalase digestion were isolated and characterised. Two active fractions with ABTS radical scavenging activity (973.01–1497.53 μmol TE/mg sample) and chelating activity (0.05–0.07 μmol EE/mg sample) from consecutive purification steps including ultrafiltration, cation exchange column chromatography and reverse phase high performance liquid chromatography (RP-HPLC), were subjected to analysis of amino acid sequence by LC–MS/MS. Seven dominant peptides with 6–11 amino acid residues were identified as DWMKGQ, MLVFAV, MCYPAST, FVSACSVAG, LADGVAAPA, YVNDAATLLPR and DLDLRKDLYAN. These peptides were synthesised and analysed for ACE-inhibitory activity and antioxidative activities. MLVFAV exhibited the highest ACE inhibitory activity (IC 50 = 3.07 μM) ( p
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antioxidative and functional properties of Protein Hydrolysate from defatted skipjack katsuwonous pelamis roe
Food Chemistry, 2012Co-Authors: Rossawan Intarasirisawat, Soottawat Benjakul, Wonnop VisessanguanAbstract:Abstract Antioxidative and functional properties of Protein Hydrolysate from defatted skipjack (Katsuwonous pelamis) roe, hydrolysed by Alcalase 2.4 L (RPH) with different degrees of hydrolysis (DH) at various concentrations were examined. As DH increased, the reduction of DPPH, ABTS radicals scavenging activities and reducing power were noticeable (p
N Bhaskar - One of the best experts on this subject based on the ideXlab platform.
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Protein Hydrolysate from visceral waste Proteins of catla catla catla optimization of hydrolysis conditions for a commercial neutral protease
Bioresource Technology, 2008Co-Authors: N Bhaskar, N S MahendrakarAbstract:Protein Hydrolysate was prepared from visceral waste Proteins of an Indian freshwater major carp, Catla catla. Hydrolysis conditions (viz., time, temperature and enzyme to substrate level) for preparing Protein Hydrolysates from the fish visceral waste Proteins using in situ pH of the visceral mass were optimized by response surface methodology (RSM) by employing a factorial design. The regression coefficient close to 1.0, observed during both experimental and validation runs, indicated the validity of prediction model. An enzyme to substrate level of 1.25 % (v/w), temperature of 55 degrees C and a hydrolysis time of 165 min were found to be the optimum conditions to obtain a higher degree of hydrolysis of >48% using multifect-neutral. The amino acid composition of the Protein Hydrolysate prepared using the optimized conditions revealed that the Protein Hydrolysate was similar to FAO/WHO reference Protein. The chemical scores computed indicated methionine to be the most limiting amino acid. The Protein Hydrolysate has the potential for application as an ingredient in balanced fish diets.
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optimization of enzymatic hydrolysis of visceral waste Proteins of catla catla catla for preparing Protein Hydrolysate using a commercial protease
Bioresource Technology, 2008Co-Authors: N Bhaskar, T Benila, C Radha, R G LalithaAbstract:Protein Hydrolysate was prepared from visceral waste Proteins of Catla (Catla catla), an Indian freshwater major carp. Hydrolysis conditions (viz., time, temperature, pH and enzyme to substrate level) for preparing Protein Hydrolysates from the fish visceral waste Proteins were optimized by response surface methodology (RSM) using a factorial design. Model equation was proposed with regard to the effect of time, temperature, pH and enzyme to substrate level. An enzyme to substrate level of 1.5% (v/w), pH 8.5, temperature of 50 degrees C and a hydrolysis time of 135 min were found to be the optimum conditions to obtain a higher degree of hydrolysis close to 50% using alcalase. The amino acid composition of the Protein Hydrolysate prepared using the optimized conditions revealed that the Protein Hydrolysate was similar to FAO/WHO reference Protein. The chemical scores computed indicated methionine to be the most limiting amino acid. The Protein Hydrolysate can well be used to meet the amino acid requirements of juvenile common carp and hence has the potential for application as an ingredient in balanced fish diets.
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utilization of meat industry by products Protein Hydrolysate from sheep visceral mass
Bioresource Technology, 2007Co-Authors: N Bhaskar, C Radha, V K Modi, K Govindaraju, R G LalithaAbstract:Protein Hydrolysate was prepared from pre-treated sheep visceral mass (including stomach, large and small intestines) by enzymatic treatment at 43+/-1 degrees C (at the in situ pH 7.1+/-0.2 of the visceral mass) using fungal protease. The enzyme readily solubilized the Proteins of the visceral mass as indicated by the degree of hydrolysis (34%) and nitrogen recovery (>64%). Hydrolysis with an enzyme level of 1% (w/w of total solids) at 43+/-1 degrees C with a pH around 7.0 for 45 min was found to be the optimum condition. The yield of Protein Hydrolysate was about 6% (w/w). The amino acid composition of the Protein Hydrolysate that was very hygroscopic, was comparable to that of casein.
R G Lalitha - One of the best experts on this subject based on the ideXlab platform.
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optimization of enzymatic hydrolysis of visceral waste Proteins of catla catla catla for preparing Protein Hydrolysate using a commercial protease
Bioresource Technology, 2008Co-Authors: N Bhaskar, T Benila, C Radha, R G LalithaAbstract:Protein Hydrolysate was prepared from visceral waste Proteins of Catla (Catla catla), an Indian freshwater major carp. Hydrolysis conditions (viz., time, temperature, pH and enzyme to substrate level) for preparing Protein Hydrolysates from the fish visceral waste Proteins were optimized by response surface methodology (RSM) using a factorial design. Model equation was proposed with regard to the effect of time, temperature, pH and enzyme to substrate level. An enzyme to substrate level of 1.5% (v/w), pH 8.5, temperature of 50 degrees C and a hydrolysis time of 135 min were found to be the optimum conditions to obtain a higher degree of hydrolysis close to 50% using alcalase. The amino acid composition of the Protein Hydrolysate prepared using the optimized conditions revealed that the Protein Hydrolysate was similar to FAO/WHO reference Protein. The chemical scores computed indicated methionine to be the most limiting amino acid. The Protein Hydrolysate can well be used to meet the amino acid requirements of juvenile common carp and hence has the potential for application as an ingredient in balanced fish diets.
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utilization of meat industry by products Protein Hydrolysate from sheep visceral mass
Bioresource Technology, 2007Co-Authors: N Bhaskar, C Radha, V K Modi, K Govindaraju, R G LalithaAbstract:Protein Hydrolysate was prepared from pre-treated sheep visceral mass (including stomach, large and small intestines) by enzymatic treatment at 43+/-1 degrees C (at the in situ pH 7.1+/-0.2 of the visceral mass) using fungal protease. The enzyme readily solubilized the Proteins of the visceral mass as indicated by the degree of hydrolysis (34%) and nitrogen recovery (>64%). Hydrolysis with an enzyme level of 1% (w/w of total solids) at 43+/-1 degrees C with a pH around 7.0 for 45 min was found to be the optimum condition. The yield of Protein Hydrolysate was about 6% (w/w). The amino acid composition of the Protein Hydrolysate that was very hygroscopic, was comparable to that of casein.
Wonnop Visessanguan - One of the best experts on this subject based on the ideXlab platform.
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Effects of skipjack roe Protein Hydrolysate on properties and oxidative stability of fish emulsion sausage
LWT - Food Science and Technology, 2014Co-Authors: Rossawan Intarasirisawat, Wonnop Visessanguan, Jianping WuAbstract:Effects of skipjack roe Protein Hydrolysate (SRPH) at various levels (0-3 g/100g) on properties and oxidative stability of emulsion sausage from broadhead catfish (Clarias macrocephalus) fortified with skipjack tuna roe lipids were investigated. The addition of SRPH increased hardness, cohesiveness and resilience of sausage (p
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isolation of antioxidative and ace inhibitory peptides from Protein Hydrolysate of skipjack katsuwana pelamis roe
Journal of Functional Foods, 2013Co-Authors: Rossawan Intarasirisawat, Soottawat Benjakul, Wonnop VisessanguanAbstract:Abstract Bioactive peptides from Protein Hydrolysate of defatted skipjack ( Katsuwonus pelamis ) roe with 5% degree of hydrolysis (DH) prepared by Alcalase digestion were isolated and characterised. Two active fractions with ABTS radical scavenging activity (973.01–1497.53 μmol TE/mg sample) and chelating activity (0.05–0.07 μmol EE/mg sample) from consecutive purification steps including ultrafiltration, cation exchange column chromatography and reverse phase high performance liquid chromatography (RP-HPLC), were subjected to analysis of amino acid sequence by LC–MS/MS. Seven dominant peptides with 6–11 amino acid residues were identified as DWMKGQ, MLVFAV, MCYPAST, FVSACSVAG, LADGVAAPA, YVNDAATLLPR and DLDLRKDLYAN. These peptides were synthesised and analysed for ACE-inhibitory activity and antioxidative activities. MLVFAV exhibited the highest ACE inhibitory activity (IC 50 = 3.07 μM) ( p
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antioxidative and functional properties of Protein Hydrolysate from defatted skipjack katsuwonous pelamis roe
Food Chemistry, 2012Co-Authors: Rossawan Intarasirisawat, Soottawat Benjakul, Wonnop VisessanguanAbstract:Abstract Antioxidative and functional properties of Protein Hydrolysate from defatted skipjack (Katsuwonous pelamis) roe, hydrolysed by Alcalase 2.4 L (RPH) with different degrees of hydrolysis (DH) at various concentrations were examined. As DH increased, the reduction of DPPH, ABTS radicals scavenging activities and reducing power were noticeable (p
Richard J. Fitzgerald - One of the best experts on this subject based on the ideXlab platform.
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Blue whiting (Micromesistius poutassou) muscle Protein Hydrolysate with in vitro and in vivo antidiabetic properties
Journal of Functional Foods, 2017Co-Authors: Pádraigín A. Harnedy, Vadivel Parthsarathy, Chris M. Mclaughlin, Martina B. O'keeffe, Philip J. Allsopp, Emeir M. Mcsorley, Finbarr O'harte, Richard J. FitzgeraldAbstract:A blue whiting (Micromesistius poutassou) Protein Hydrolysate generated using Alcalase 2.4L and Flavourzyme 500L and its simulated gastrointestinal digestion (SGID) sample was assessed for antidiabetic potential in vitro and in vivo. In addition to inhibiting dipeptidyl peptidase-IV (DPP–IV), the Hydrolysates mediated insulin and glucagon-like peptide-1 (GLP-1) release from BRIN-BD11 and GLUTag cells, respectively. No significant difference was observed in insulinotropic and DPP-IV inhibitory activity following SGID, while GLP-1 secretion increased significantly (p < 0.01). SGID resulted in a significant increase in membrane potential, intracellular calcium and cyclic AMP concentration (p < 0.001) versus a glucose control, indicating that insulin secretion may be mediated by the KATP channel-dependent and the Protein kinase A pathways. Additionally, acute (90–120 min) and persistent (4 h) glucose-lowering effects of the blue whiting Hydrolysate were observed in normal healthy mice. These results demonstrate that the blue whiting Protein Hydrolysate had significant metabolic effects relevant to glucose control in vivo.
