Antioxidant activity of chemically and enzymatically modified sericin extracted from cocoons of Bombyx mori

Sangwong, Giraporn; Sumida, Motoyuki; Sutthikhum, Vallaya

doi:10.1016/j.bcab.2016.01.010

Cited by 35 publications

(17 citation statements)

References 47 publications

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“…Inhibition of -glucosidase may currently be used to reduce intestinal uptake of glucose and subsequently lower post-prandial hyperglycemia in type 2 diabetics (Umpierrez et al, 2017). Animal studies describing the antihypertensive (Onsa-ard et al, 2013;Yuan, Wang, & Zhou, 2012), antioxidant (Sangwong, Sumida, & Sutthikhum, 2016;Yuan et al, 2012), antidiabetic (Han, Lee, Lee, Suh, & Park, 2016;Jung et al, 2010), memory enhancement (Kang, Lee, Kang, & Kang, 2013) and hypocholesterolemic (Lapphanichayakool, Sutheerawattananonda, & Limpeanchob, 2017) properties of silk protein hydrolysates have been reported. However, it appears that, to date, BAPs and protein hydrolysates derived from edible insects (other than B. mori), having bioactive properties in vitro and in small animals, have not been extensively studied in comparison to silk protein-derived peptides (Xia et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Unlocking the biological potential of proteins from edible insects through enzymatic hydrolysis: A review

Nongonierma

Fitzgerald

2017

Innovative Food Science & Emerging Technologies

173

105

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This review, focusing on studies published between 2005 and 2017, analysed the literature on the generation of bioactive peptides (BAPs) from edible insect proteins following enzymatic hydrolysis. The protein extraction and quantification methodologies used for edible insects varied considerably. While several edible insects have been evaluated for their ability to release BAPs, silkworm (Bombyx mori) is currently the most studied. Specifically, the angiotensin converting enzyme (ACE) inhibitory, antioxidant and antidiabetic properties of edible insect protein enzymatic hydrolysates have been studied. Potent in vitro ACE inhibitory and antioxidant hydrolysates/peptides have been reported. In certain instances, these properties were validated in small animal studies (i.e. hypotensive effects). Enzymatic hydrolysis of edible insect proteins may also enhance technofunctional properties (i.e. solubility). The wider application of enzymatic hydrolysis protocols to edible insect proteins may ultimately allow for the increased discovery and utilisation of novel BAPs as sustainable protein/peptide sources for human nutrition.

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Section: Introductionmentioning

confidence: 99%

Unlocking the biological potential of proteins from edible insects through enzymatic hydrolysis: A review

Nongonierma

Fitzgerald

2017

Innovative Food Science & Emerging Technologies

173

105

View full text Add to dashboard Cite

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“…[50][51][52][53][54][55][56][57][58] However, some investigators noticed such effects only in the extracts likely containing mainly non-sericinoid substances, 59,60 while others reported them both in sericin and in its extracts. 61,62 As shown in Figure 10, the presence of sericin in the composition of the substrata does not have any effect upon the number of cells remaining viable after oxidative stress was applied to the cultures.…”

Section: Cell Proliferation and Oxidative Stress Assaysmentioning

confidence: 96%

Silk fibroin/sericin native blends as potential biomaterial templates

Suzuki

Rayner

2019

ATROA

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The silk produced by the domesticated silkworm (Bombyx mori) consists of two major polypeptidic components, fibroin and sericin. Both are used as biomaterial templates in tissue engineering applications, with variable success. While fibroin membranes are mechanically strong, they do not promote satisfactorily attachment and proliferation of cells. Sericin membranes display a precisely opposite behavior. In order to generate silk-based templates with optimal cell-adhesive properties and acceptable mechanical strength, we propose a method to manufacture fibroin/sericin blends in one single step, by processing the whole silk cocoons. The membranes prepared from these "native" blends were physically characterized in this study, and assessed as substrata for the growth of retinal photoreceptor cells. The antioxidant effect putatively inducible by sericin was also evaluated. The blend membranes were found to be mechanically stronger than the fibroin membranes and led to significant enhancement of cell proliferation. Our method also prevented the advanced hydrothermal degradation of fibroin and sericin during processing. The membranes displayed both excellent transparency and suitable water content. However, their permeability was low, and no antioxidative activity related to the presence of sericin was detected when oxidative stress was induced in the cell cultures. The method developed in this study provides silk-based membranes with improved characteristics for tissue engineering applications.

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“…J. Food Technol., Campinas, v. 23, e2019058, 2020 | https://doi.org/10.1590/1981-6723.05819 7/14 2016; Napavichayanun et al, 2017;Deori et al, 2016;Sangwong et al, 2016;Kumar & Mandal (2017); Fan et al, 2010;Kaewkon et al, 2012;Zhaorigetu et al, 2001;Dash et al, 2008), and inhibits tyrosinase activity (Aramwit et al, 2010a;Kato et al, 1998;Thongsook & Tiyaboonchai, 2011;Puangphet et al, 2015;Wu et al, 2008;Manosroi et al, 2010). Table 3 provides an overview of studies supporting the sericin's antioxidant activity.…”

Section: Antioxidant Activity Of Sericin Proteinmentioning

confidence: 99%

“…Moreover, there was found an inverse relation between the sericin molecular size and the antioxidant activity. When sericin size decreased by the action of proteases, the scavenger activity increased (Sangwong et al, 2016). In a recent study, the radical scavenging activity of a sericin extract obtained by a novel isolated bacterial protease was compared with a sericin extract produced by a commercial alcalase.…”

Section: Sericin Effect In Reactive Oxygen Species (Ros)mentioning

confidence: 99%

Extraction and antioxidant activity of sericin, a protein from silk

Miguel

Álvarez‐López

2020

Braz. J. Food Technol.

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Sericin is a globular protein that represents 20% to 30% of the silk fiber from Bombyx mori silkworm cocoon. This protein is usually removed from the raw fiber and discarded by silk producers, a process known as degumming. However, sericin possesses significant biological properties that allows its application in various fields. The antioxidant activity is one of its most relevant benefits. Several authors have reported its anti-tyrosinase activity, lipid peroxidation inhibition and free radical neutralization. The antioxidant potential of sericin protein varies according to the extraction method used. Even though a wide variety of extraction techniques have been studied, simple technics including water at high temperature have exhibited efficient results. Furthermore, this method does not interfere with the safety of sericin for subsequent applications in food.

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Antioxidant activity of chemically and enzymatically modified sericin extracted from cocoons of Bombyx mori

Cited by 35 publications

References 47 publications

Unlocking the biological potential of proteins from edible insects through enzymatic hydrolysis: A review

Unlocking the biological potential of proteins from edible insects through enzymatic hydrolysis: A review

Silk fibroin/sericin native blends as potential biomaterial templates

Extraction and antioxidant activity of sericin, a protein from silk

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