Chemical composition, molecular mass distribution and antioxidant capacity of rohu (Labeo rohita) roe (egg) protein hydrolysates prepared by gastrointestinal proteases

Chalamaiah, Meram; Jyothirmayi, T.; Bhaskarachary, K.; Vajreswari, Ayyalasomayajula; Hemalatha, R.; Kumar, B. Dinesh

doi:10.1016/j.foodres.2013.03.020

Cited by 51 publications

(37 citation statements)

References 28 publications

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“…Many studies have reported that low molecular weight peptides are better ACE inhibitors than high MW peptides (Raghavan and Kristinsson 2009;Barbana and Boye 2010;Nasri et al 2014). In the current study, the low molecular mass peptides present in the pepsin hydrolysate might have contributed to higher ACE inhibitory activity than trypsin hydrolysate (Chalamaiah et al 2013). In addition, the aromatic and hydrophobic amino acids present in the pepsin and trypsin hydrolysates play an important role in ACE inhibitory activity (Chalamaiah et al 2013;Lee et al 2011;Nasri et al 2014).…”

Section: Ace-inhibitory Activitymentioning

confidence: 60%

“…Protein content of the hydrolysates was 69 ± 0.57 and 73 ± 1.59 %, respectively for pepsin and trypsin hydrolysates (Chalamaiah et al 2013).…”

Section: Resultsmentioning

confidence: 97%

“…Rohu (Labeo rohita) roe protein hydrolysates were prepared by gastrointestinal proteases (pepsin and trypsin) according to earlier reported method (Chalamaiah et al 2013). Briefly, rohu roe powder (5 g, protein content basis) was suspended in 150 ml of distilled water and the mixture was adjusted (0.5 M HCl or 0.5 M NaOH) to the optimum pH 2.0 for pepsin and pH 8.0 for trypsin for proteolytic enzyme hydrolysis.…”

Section: Preparation Of Rohu Roe (Egg) Protein Hydrolysatesmentioning

confidence: 99%

“…Fish egg is present in ovarian membrane of female fish and is a valuable source of high quality protein (Chalamaiah et al 2013;Intarasirisawat et al 2011). In India and other Asian countries, large quantities of fish roes are considered by-products of fish processing industry and are normally processed into low market-value products, such as animal feed, fish meal and fertilizer (Chalamaiah et al 2012).…”

Section: Introductionmentioning

confidence: 99%

“…Hence, production of protein hydrolysates with anticancer, antihypertensive and improved functional properties would improve economic benefits as well as solve the disposal problems (He et al 2013). In our previous study, the preparation, chemical composition, molecular mass distribution and antioxidant activities of protein hydrolysates from rohu (Labeo rohita) egg were reported (Chalamaiah et al 2013). The objectives of this study were to evaluate the anticancer, antihypertensive and functional (solubility, foaming properties and emulsifyings activities) properties of protein hydrolysates derived from rohu roe by enzymatic hydrolysis using pepsin and trypsin as gastrointestinal proteases.…”

Section: Introductionmentioning

confidence: 99%

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Antiproliferative, ACE-inhibitory and functional properties of protein hydrolysates from rohu (Labeo rohita) roe (egg) prepared by gastrointestinal proteases

et al. 2015

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Previously, we have reported the chemical composition, molecular mass distribution and antioxidant activity of rohu roe protein hydrolysates. In the current study, antiproliferative, angiotensin-converting enzyme (ACE)-inhibitory activities and functional properties of protein hydrolysates from rohu (Labeo rohita) roe proteins, prepared by gastrointestinal proteases (pepsin and trypsin), were investigated. Antiproliferative activity was evaluated against human colon cancer cell line Caco-2. The results showed that the pepsin hydrolysate possessed dose dependent inhibitory effect on Caco-2 cell line. Pepsin and trypsin hydrolysates displayed ACE-inhibitory activity in vitro. The ACE-inhibitory activity of the hydrolysate generated by pepsin (47 ± 1.7 %, at 1 mg/ml) is higher than that obtained by trypsin (36 ± 3.2 %). Additionally, the undigested rohu roe proteins and its hydrolysates exhibited functional properties. Solubilities of the hydrolysates were above 81 ± 9.2 % at all pH values tested. Pepsin and trypsin hydrolysates showed good foaming capacity (45-211 %) and emulsification activity (4-29 m 2 /g). The foaming abilities and emulsifying activity index (EAI) were affected by pH. The results suggest that protein hydrolysates from rohu roe could be useful in food industry for various applications.

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Section: Ace-inhibitory Activitymentioning

confidence: 60%

“…Protein content of the hydrolysates was 69 ± 0.57 and 73 ± 1.59 %, respectively for pepsin and trypsin hydrolysates (Chalamaiah et al 2013).…”

Section: Resultsmentioning

confidence: 97%

Section: Preparation Of Rohu Roe (Egg) Protein Hydrolysatesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Antiproliferative, ACE-inhibitory and functional properties of protein hydrolysates from rohu (Labeo rohita) roe (egg) prepared by gastrointestinal proteases

et al. 2015

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Biodegradable and Bioactive Films or Coatings From Fish Waste Materials

Delava

Maestre

Triques

et al. 2022

Biodegradable Materials and Their Applications

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Cryoprotective effect of glycopeptide complex from abalone viscera on frozen surimi and its underlying mechanism

Chen,

Yu,

et al. 2024

Food Frontiers

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Freezing technology is important for the long‐term preservation of aquatic products such as surimi. However, mechanical damage caused by ice crystals would lead to quality deterioration. Abalone viscera glycopeptide (AVGP) complex was prepared by hydrolysis technology, which exhibited ice recrystallization ability and antioxidant activity. Moreover, effects of AVGP on Ca2+‐ATPase activity, total sulfhydryl content, secondary structure of myofibrillar protein (MP), rheological properties, and gel properties of surimi frozen were investigated. Results showed that surimi treated with AVGP could improve the gel strength and rheological properties of surimi, reduce the gel ice crystal holes, and improve the degradation of gel matrix caused by freeze–thaw. AVGP can significantly inhibit the decrease of Ca2+‐ATPase activity and total sulfhydryl group content. When the addition of AVGP exceeded 4% (w/w), its freezing protection effect on MP was better than that of commercial antifreeze agents. Moreover, the α‐helix and β‐fold contents in the 4% AVGP group were significantly higher than those in the control group, indicating that the addition of an appropriate amount of AVGP can protect the secondary structure of MP. Therefore, AVGP could serve as a new food ingredient with antifreeze and antioxidant functions for frozen surimi.

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Chemical composition, molecular mass distribution and antioxidant capacity of rohu (Labeo rohita) roe (egg) protein hydrolysates prepared by gastrointestinal proteases

Cited by 51 publications

References 28 publications

Antiproliferative, ACE-inhibitory and functional properties of protein hydrolysates from rohu (Labeo rohita) roe (egg) prepared by gastrointestinal proteases

Antiproliferative, ACE-inhibitory and functional properties of protein hydrolysates from rohu (Labeo rohita) roe (egg) prepared by gastrointestinal proteases

Biodegradable and Bioactive Films or Coatings From Fish Waste Materials

Cryoprotective effect of glycopeptide complex from abalone viscera on frozen surimi and its underlying mechanism

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