Proteolytic activity from chicken intestine and pancreas: extraction, partial characterization and application for hyaluronic acid separation from chicken comb

Srisantisaeng, Pimporn; Garnjanagoonchorn, Wunwiboon; Thanachasai, Saipin; Choothesa, Apassara

doi:10.1002/jsfa.6217

Cited by 7 publications

(4 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It should be emphasized that sapropel, increasing the activity of caseinlytic and hemoglobin-lytic peptidases of the chicken intestine mucosa over a wide range of pH values (from 5 to 12), does not change the pH optimum. Our data agree well to the observation that the crude enzyme extract of the intestine and pancreas of chickens demonstrates a high proteolytic activity with an optimum of pH 7.5 (Srisantisaeng et al, 2013).…”

Section: Resultssupporting

confidence: 92%

Influence of sapropel on the activity of intestinal peptidases of broiler chickens

Кузьмина

Skvortsova

Pivovarova

et al. 2020

J. Indonesian Trop. Anim. Agric.

View full text Add to dashboard Cite

At the beginning of the experiment, the weight of weekly cockerels of the Hisex White egg cross (n = 90) was 64.6 ± 0.47 g. At the age of one week old, 3 groups (30 birds in each group) were formed. They received complete feed. The first group served as a control. The chickens of the second and third groups received combined fodder, in which 3% and 5% of the feed weight was replaced with dry sapropel. The dry sapropel (3% of the daily feed weight) increased the activity of casein-lytic and hemoglobin-lytic peptidases in the chyme by 1.5 (Р<0.05), in large intestine mucosa by 1.3 (Р<0.05) and in small intestine mucosa by 1.7 times (Р<0.01) compared with the control. The increase of sapropel concentration in feed up to 5% did not lead to a further increase in the activity of peptidases. The activity of peptidases were minimal at pH 5 and pH 12 and reached maximal at pH 7–8. The optimal dose of dry sapropel introduced into the diet of chickens to that stimulated the digestive processes is 3% of the mass of feed.

show abstract

Section: Resultssupporting

confidence: 92%

Influence of sapropel on the activity of intestinal peptidases of broiler chickens

Кузьмина

Skvortsova

Pivovarova

et al. 2020

J. Indonesian Trop. Anim. Agric.

View full text Add to dashboard Cite

show abstract

“…) and separation of hyaluronic acid from chicken comb (Srisantisaeng et al . ). Two of these applications namely, preparation of protein hydrolysate and enzymatic degradation of tannery fleshing requiring extensive proteolysis were carried out at low pH values (pH 2–3).…”

Section: Introductionmentioning

confidence: 97%

“…However, in past few years, chicken intestine, which accounts for 20-30% of processing wastes, has been reported as a potential source of proteins (Jamdar and Harikumar 2008), lipids (Rao et al 1996;Ockerman and Hansen 2000) and tissue proteases (Damle et al 2010a;Jamdar and Harikumar 2005). More-over, a few attempts have been made in using this waste for preparation of protein hydrolysate (Jamdar and Harikumar 2008); debittering of casein and soybean protein hydrolysates (Damle et al 2010b); enzymatic degradation of tannery fleshing (Raju et al 1997) and separation of hyaluronic acid from chicken comb (Srisantisaeng et al 2013). Two of these applications namely, preparation of protein hydrolysate and enzymatic degradation of tannery fleshing requiring extensive proteolysis were carried out at low pH values (pH 2-3).…”

Section: Introductionmentioning

confidence: 99%

Purification, Identification and Characterization of Aspartic Proteases of Chicken Intestine

Jamdar

Harikumar

2016

Journal of Food Biochemistry

View full text Add to dashboard Cite

Chicken intestine, an underutilized by-product of poultry industry is a rich source of tissue proteases, especially aspartic proteases. Two of the major aspartic proteases of the tissue were purified from lysosomal and post lysosomal fractions and identified by N-terminal amino acid sequencing as cathepsin D and pepsin, respectively. The enzymes differed in their molecular and biochemical properties like molecular weight, optimum conditions for protein degradation and stability in different conditions of pH and temperature. Both enzymes were completely inhibited by pepstatin. The kinetic constant, Km for chicken intestinal pepsin and cathepsin D (for haemoglobin substrate) were estimated to be 6.45 lM and 22.7 lM, respectively. The interaction of both enzymes with different food proteins suggests pepsin could be used in applications demanding extensive hydrolysis of proteins, while cathepsin D could be used in those needing controlled degradation of proteins. PRACTICAL APPLICATIONSChicken intestine is a by-product of poultry industry. The tissue could serve as a major source of proteases especially aspartic proteases, which can be used as an alternative for proteases currently used in food industries. Aspartic proteases (pepsin and cathepsin D) from this tissue can be recovered and used for preparation of protein hydrolysates in a more economical way. Furthermore, the byproduct can be exploited to increase revenues for poultry processors.

show abstract

“…Collagen, the most abundant protein in mammals, is the main structural protein of the extracellular matrix found in various connective tissues in the body. Notably, the collagen used in the medical and cosmetic field is derived from the skin of cows and pigs [ 16 ]. Pigs are an excellent model for understanding human diseases because their anatomy and physiology closely resembles those of humans, which is not the case with other experimental animal models.…”

Section: Introductionmentioning

confidence: 99%

Industrialization possibilities of purified pig sperm hyaluronidase

Park,

Myeong,

Wee

et al. 2023

J Anim Sci Technol

View full text Add to dashboard Cite

The goals of the present study were to develop a simple method for obtain highly purified pig sperm hyaluronidase (pHyase) and to assess its activity, function, and safety. In mammals, sperm-specific glycophosphatidylinositol (GPI)-anchored Hyase assists sperm penetration through the cumulus mass surrounding the egg and aids in the dispersal of the cumulus–oocyte complex. Recently, Purified bovine sperm hyaluronidase (bHyase) has been shown to enhance therapeutic drug transport by breaking down the hyaluronan barrier to the lymphatic and capillary vessels, thereby facilitating tissue absorption. Commercially available Hyase is typically isolated from bovine or ovine; which have several disadvantages, including the risk of bovine spongiform encephalopathy, low homology with human Hyase, and the requirement for relatively complex isolation procedures. This study successfully isolated highly purified pHyase in only two steps, using ammonium sulfate precipitation and fast protein liquid chromatography. The isolated Hyase had activity equal to that of commercial bHyase, facilitated in vitro fertilization, and effectively dissolved high molecule hyaluronic acid. This simple, effective isolation method could improve the availability of pHyase for research and clinical applications.

show abstract

Proteolytic activity from chicken intestine and pancreas: extraction, partial characterization and application for hyaluronic acid separation from chicken comb

Abstract: The crude enzyme extract from chicken intestine and pancreas had high proteolytic activity and could be used successfully to separate HA from broiler combs. The method provides an appropriate means to add value to poultry-processing waste.

Cited by 7 publications

References 23 publications

Influence of sapropel on the activity of intestinal peptidases of broiler chickens

Influence of sapropel on the activity of intestinal peptidases of broiler chickens

Purification, Identification and Characterization of Aspartic Proteases of Chicken Intestine

Industrialization possibilities of purified pig sperm hyaluronidase

Contact Info

Product

Resources

About