scholarly journals Karakteristik Hidrolisat Gelatin Tulang Itik Dengan Enzim Tripsin Sebagai Penghambat Alfa Amilase (α-Amylase Inhibitor)

2020 ◽  
Vol 20 (3) ◽  
Author(s):  
MUHAMMAD HABBIB KHIRZIN
Keyword(s):  
Inhibitory Activity ◽  
Soluble Protein ◽  
Treatment Time ◽  
Positive Control ◽  
Alpha Amylase ◽  
Total Soluble Protein ◽  
Degree Of Hydrolysis ◽  
Hydrolysis Time ◽  
Amylase Inhibitor ◽  
Hydrolysis Degree

Gelatin is extracted from beef or pork. One of the potential sources of gelatin to be developed apart from land base mammalian is from poultry, namely duck bones. Gelatin extraction from duck bones can be carried out by the acid method. Several studies have reported that hydrolysis of gelatin using various types of enzymes will increase its bioactivity, such as antioxidants, antibacterials, and antihyperglycemic (alpha amylase inhibitors). The purpose of this study was to determine the characteristics of duck bone gelatin which hydrolyzed with trypsin enzyme as an alpha amylase inhibitor. This study used nonfactorial completely randomized design (CRD) with different hydrolysis time treatments. Research parameters such as total soluble protein, TCA soluble protein, hydrolysis degree, and alpha amylase inhibitory activity. The results showed that the different treatment times for hydrolysis had a significant effect (P <0.05) on the TCA soluble protein value and the degree of hydrolysis. However, there was no significant effect (P> 0.05) on the total dissolved protein. 180 minutes hydrolysis treatment time with a concentration series of 250; 500; 1000; 2000 ppm has inhibitory activity against alpha amylase, respectively, 39.42; 41.75; 44.58; 48.11%. It has IC50 value of 2.74 mg / mL. The inhibitory activity was still weaker than the positive control for acarbose.

scholarly journals Effect of Hydrolysis time and Papain Concentration on Some Properties of Apple Snail (Pilla ampullacea) Hydrolysate

2020 ◽  
Vol 1 (02) ◽  
pp. 1-5
Author(s):  
Andre Yusuf Trisna Putra ◽  
Dedin Finatsiyatull Rosida ◽  
Anugerah Dany Priyanto
Keyword(s):  
Soluble Protein ◽  
Enzyme Concentration ◽  
Total Soluble Protein ◽  
Apple Snail ◽  
Gut Content ◽  
Hydrolysis Time ◽  
Umami Taste ◽  
Nutritional Potential

content and total peptide content were investigated in the non-farmed freshwater apple snail (Pila ampullacea) to understand its nutritional potential as alternative umami taste enhancer. Apple Snail samples with removed gut content were collected from a local snail non-farm in Surabaya City. Papain enzyme was used. The two variables, hydrolysis time (3, 6, 9, 12, 15, 18 h) and enzyme concentration (1%, 5%, 10%), was used to produce the apple snail hydrolysate. The result showed that total soluble protein was about 2.1%-7.3%, whereas total peptide content was 5.05-15.73mg/ml. The highest total soluble protein was achieved at 12 hour. Longer hydrolysis time significantly effect on total peptide content of apple snail hydrolysate.

scholarly journals The analysis of Angiotensin-I Converting Enzyme (ACE) by maitake (Grifrola frondosa) mycelia

2021 ◽  
Vol 8 (2) ◽  
pp. 69-72
Author(s):  
Yuen Sim Kheng ◽  
Young Liew Jeng ◽  
Maryana Mohamad Nor ◽  
Geng Boon Jia
Keyword(s):  
Inhibitory Activity ◽  
Protein Concentration ◽  
Bioactive Peptides ◽  
Biological Properties ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Hydrolysis Time ◽  
Angiotensin I Converting Enzyme ◽  
Freeze Dried

The Maitake (Grifola frondosa) is useful in treating diseases, specifically hypertension. Research on the maitake mycelia’s biological properties, nevertheless, are limited in the literature. This study aimed to (i) produce mushroom biomass adopting submerged fermentation, and (ii) investigate the Angiotensin-I Converting Enzyme inhibitory activity. Maitake mycelia’s yield after 14 days of fermentation under controlled conditions (approx. 1.32 g/L) were freeze-dried into powder and later were hydrolysed for analyses of Angiotensin-I Converting Enzyme inhibitory activity. Current results showed that the degree of hydrolysis increased in line with hydrolysis time, as the protein concentration for hydrolysed sample was 283.61 ± 7.14 µg/mL, however, the non-hydrolysed sample resulted in lesser protein content (46.76 ± 1.09 µg/mL). The hydrolysate maitake mycelia has higher Angiotensin-I Converting Enzyme inhibitory activity (46.48%) as compared to the non-hydrolysate maitake mycelia (20.19 ± 0.17%). This finding suggested maitake mycelia hydrolysate can be a source of potential bioactive peptides used in treating hypertension.

scholarly journals Influence of Enzyme Concentration and Hydrolysis Time on Soluble Protein Content of Protein Hydrolysate Prepared from Apple Snail (Pila ampullacea)

2021 ◽  
Vol 2 (02) ◽  
pp. 26-29
Author(s):  
Andre Yusuf Trisna Putra ◽  
Dedin Finatsiyatull Rosida ◽  
Anugerah Dany Priyanto
Keyword(s):  
Enzymatic Hydrolysis ◽  
Protein Content ◽  
Soluble Protein ◽  
Protein Hydrolysate ◽  
Enzyme Concentration ◽  
Total Soluble Protein ◽  
Apple Snail ◽  
Soluble Protein Content ◽  
Hydrolysis Time ◽  
Enzyme Substrate

The objective of this study was to evaluate soluble protein content of protein hydrolysates obtained by enzymatic hydrolysis of apple snail using a trypsin enzyme. Apple snail were collected from traditional market at Pabean-Sidoarjo. Trypsin enzyme was used in enzymatic hydrolysis. The two variables, enzyme/substrate (E/S) ( 0.01, 0.05, 0.1) ratio and hydrolysis time (3 h, 6 h, 9 h, 12 h, 15 h, 18 h) and was used to produce the apple snail hydrolysate. The result showed that soluble protein content was about 2.3%-4.52%. The increase E/S ratio and hydrolysis time, the higher soluble protein content values was. The highest total soluble protein was achieved E/S 0.1 ratio at 12 h, 4.52%. But, after 12 h hydrolysis time, soluble protein was decreased. Optimum treatment to hydrolyzing apple snail using trypsin enzyme was E3H4 treated (E/S 0.1 ratio and 3 h)

Hidrolisis Protein Teripang Hitam (Holothuria edulis) Menggunakan Bromelin Kasar dari Batang Nanas (Ananas comocus L)

KOVALEN ◽  
2021 ◽  
Vol 7 (3) ◽  
pp. 214-219
Author(s):  
Fakhrija Sahraini ◽  
Abd. Rahman Razak ◽  
Syaiful Bahri ◽  
Hardi Ys.
Keyword(s):  
Protein Content ◽  
Black Sea ◽  
Sea Cucumber ◽  
Degree Of Hydrolysis ◽  
Enzyme Extract ◽  
Hydrolysis Time ◽  
Optimum Degree ◽  
Protein Hydrolyzate ◽  
Hydrolysis Degree ◽  
A Value

Black sea cucumber is one type of sea cucumber whose protein content is quite high at 74-82%, not yet widely used by the community as a source of protein. One way to use it is to process the protein into a protein hydrolyzate using the bromelain enzyme which was isolated from pineapple stems. This study aims to determine the concentration of the bromelain enzyme extract and the optimum hydrolysis time to the value of the hydrolysis degree of the hydrolyzate of black sea cucumber protein. Protein hydrolysates are produced by variations of the crude bromelain concentration of 9%, 10%, 11%, and 12% (v/v) and hydrolysis time of 120, 180, 240, and 300 minutes. The results showed that the optimum degree of hydrolysis was obtained with the use of bromelain extract with a concentration of 12% with a value of 11.43% and a hydrolysis time of 240 minutes with a value of 19.17%.

scholarly journals Evaluation of Inhibitory Activity, Purification and X-Ray Crystallography of Alpha—Amylase Inhibitor from Phaseolus Vulgaris Cultivars of Uttarakhand

2021 ◽  
Author(s):  
Ravinder Singh ◽  
Anoop Kumar Dobriyal ◽  
Rattan Deep Singh ◽  
Patricio De los Rios-Escalante
Keyword(s):  
Phaseolus Vulgaris ◽  
Crude Extract ◽  
Inhibitory Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Heat Stability ◽  
Alpha Amylase ◽  
Native Page ◽  
X Ray Crystallography ◽  
Amylase Inhibitor ◽  
Alpha Amylase Inhibitor

Abstract The present work is based on analysis of inhibitory activity of alpha-amylase inhibitor in selected cultivars of Phaseolus vulgaris of Uttarakhand. Fifteen samples were assessed for inhibitory activity of alpha-amylase inhibitor. Significant variations were found in different cultivars. Crude extract of alpha-amylase inhibitor from sample PUR (Purola) have shown maximum inhibitory activity (70.2 ± 0.84). Crude extract of all the cultivars have shown considerable variations in inhibitory activity in the temperature ranging from 20ºC to 100ºC. Based on inhibitory activity and heat stability profile, the alpha amylase inhibitor was purified from PUR cultivar. The purified inhibitor was found to be stable even at 90ºC with an inhibitory activity of 97.20 ±0.09. The molecular weight of purified inhibitor on Native PAGE (Polyacrylamide gel electrophoresis) was found to be 31kd, consisting of two subunits of 17kd and 14kd on SDS-PAGE.

scholarly journals HYPOGLYCEMIC ACTIVITY OF FRUITING BODY EXTRACTS FROM Pycnoporus sanguineus (L.: Fr.) Murr. MUSHROOM

2018 ◽  
Vol 40 (3) ◽  
Author(s):  
Tran Duc Tuong ◽  
Duong Xuan Chu ◽  
Bui Thi Minh Dieu
Keyword(s):  
Fruiting Body ◽  
Inhibitory Activity ◽  
Ethanolic Extract ◽  
Positive Control ◽  
Hypoglycemic Activity ◽  
Alpha Amylase ◽  
Moderate Activity ◽  
Pycnoporus Sanguineus ◽  
Ic50 Values

ABSTRACT Alpha-amylase and α-glucosidase are two main enzymes involved in carbohydrate metabolism. Inhibition of α-amylase and α-glucosidase can be said as an effective treatment for delaying the absorption of glucose after meals in people with diabetes mellitus. The objective of the present study is to provide an in vitro evidence for the potential hypoglycemic activity via inhibitory activity of the ethanolic and aqueous extracts from fruiting bodies of Pycnoporus sanguineus mushroom on α-amylase and α-glucosidase enzymes. Alpha-amylase and α-glucosidase inhibitory activities of aqueous and ethanolic extracts of P. sanguineus fruiting body were examined in a dose-response manner. Acarbose was used as a positive control. The results showed that the ethanolic extract of P. sanguineus possessed strong inhibitory activity on α-amylase and α-glucosidase with IC50 values of 97.08 and 92.60 μg/mL, respectively. The aqueous extract also exhibited moderate activity against α-amylase and α-glucosidase with IC50 values of 150.15 and 102.29 μg/mL, respectively. Which was significantly lower than that of acarbose with IC50 values of 85.12 and 68.36 μg/mL, respectively. The degree of α-amylase and α-glucosidase inhibition was correlated with the dose of inhibitors. From these results Pycnoporus sanguineus (Trametes sanguinea) possesses high potential in lowering blood glucose level, reduced insulin resistance and the risk of diabetic-related complications.

Inhibitory effects of bioaccessible anthocyanins and procyanidins from apple, red grape, cinnamon on α-amylase, α-glucosidase and lipase

2020 ◽  
pp. 1-9
Author(s):  
Pınar Ercan ◽  
Sedef Nehir El
Keyword(s):  
Inhibitory Activity ◽  
Digestive Enzymes ◽  
Positive Control ◽  
Anthocyanin Content ◽  
Inhibitory Effects ◽  
Total Anthocyanin ◽  
Total Anthocyanin Content ◽  
Before And After ◽  
Red Grape

Abstract. The goals of this study were to determine and evaluate the bioaccessibility of total anthocyanin and procyanidin in apple (Amasya, Malus communis), red grape (Papazkarası, Vitis vinifera) and cinnamon (Cassia, Cinnamomum) using an in vitro static digestion system based on human gastrointestinal physiologically relevant conditions. Also, in vitro inhibitory effects of these foods on lipid (lipase) and carbohydrate digestive enzymes (α-amylase and α-glucosidase) were performed with before and after digested samples using acarbose and methylumbelliferyl oleate (4MUO) as the positive control. While the highest total anthocyanin content was found in red grape (164 ± 2.51 mg/100 g), the highest procyanidin content was found in cinnamon (6432 ± 177.31 mg/100 g) (p < 0.05). The anthocyanin bioaccessibilities were found as 10.2 ± 1%, 8.23 ± 0.64%, and 8.73 ± 0.70% in apple, red grape, and cinnamon, respectively. The procyanidin bioaccessibilities of apple, red grape, and cinnamon were found as 17.57 ± 0.71%, 14.08 ± 0.74% and 18.75 ± 1.49%, respectively. The analyzed apple, red grape and cinnamon showed the inhibitory activity against α-glucosidase (IC50 544 ± 21.94, 445 ± 15.67, 1592 ± 17.58 μg/mL, respectively), α-amylase (IC50 38.4 ± 7.26, 56.1 ± 3.60, 3.54 ± 0.86 μg/mL, respectively), and lipase (IC50 52.7 ± 2.05, 581 ± 54.14, 49.6 ± 2.72 μg/mL), respectively. According to our results apple, red grape and cinnamon have potential to inhibit of lipase, α-amylase and α-glucosidase digestive enzymes.

Functional and Antioxidant Properties of Angelwing Clam (Phplas orientalis) Hydrolysate Produced using Alcalase

2014 ◽  
Vol 11 (1) ◽  
pp. 29
Author(s):  
Nonnah Ismail ◽  
Juliana Mahmod ◽  
Awatif Khairul Fatihin Mustafa Kamal
Keyword(s):  
Antioxidant Properties ◽  
Enzyme Concentration ◽  
Degree Of Hydrolysis ◽  
Emulsifying Properties ◽  
Hydrolysis Time ◽  
Chelating Activity ◽  
Metal Chelating ◽  
Metal Chelating Activity ◽  
Intermediate Concentration ◽  
As Solubility

In this study, Hydrolysate from angelwing clam (Pholas orientalis) was produced at 0, 1, 2 and 3 hrs and E/S ratio of0.5 and 3%using alcalase where the pH and temperature were kept constant at pH 8.5 and 60°C, respectively. The hydrolysates were analysed for antioxidant and functional properties such as solubility, emulsifying properties and water and oil holding capacity. Degree of hydrolysis (DH), yield, functional and antioxidant properties were influenced by the hydrolysis time and E/S ratio. Higher enzyme concentration (E/S 3%) and longer hydrolysis time increased the DH. Yield was higher at E/S 3% but reduced with hydrolysis time. Longer hydrolysis time produced more soluble hydrolysate and higher metal chelating activity but lower in emulsifying properties and DPPH activity. Higher enzyme concentration resulted in increase only in solubility and metal chelating activity. This study revealed that enzymatic hydrolysis using alcalase should be performed at shorter hydrolysis time using intermediate concentration of enzyme (E/S between 0.5 to 3%) in order to produce angelwing clam hydrolysate with collectively good functional and antioxidant properties. 

Inhibition of Protein Tyrosine Phosphatase 1B by Lutein Derivatives isolated from Mexican Oregano (Lippia graveolens)

2018 ◽  
Vol 17 (3) ◽  
pp. 134-139
Author(s):  
R.M. Perez-Gutierrez
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Inhibitory Activity ◽  
Spectroscopic Data ◽  
Methanol Extract ◽  
Tyrosine Phosphatase ◽  
Positive Control ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Ic50 Value ◽  
Ic50 Values

Methanol extract from Lippia graveolens (Mexican oregano) was studied in order to identify inhibitory bioactives for protein tyrosine phosphatase 1B (PTP1B). Known flavone as lutein (1), and another flavone glycoside such as lutein-7-o-glucoside (2), 6-hydroxy-lutein-7-ohexoside (3) and lutein-7-o-ramnoide (4) were isolated from methanol extract of aerial parts of the Lippia graveolens. All isolates were identified based on extensive spectroscopic data analysis, including UV, IR, NMR, MS and compared with spectroscopic data previously reported. These flavones were evaluated for PTP1B inhibitory activity. Among them, compounds 1 and 3 displayed potential inhibitory activity against PTP1B with IC50 values of 7.01 ± 1.25 μg/ml and 18.4 μg/ml, respectively. In addition, compound 2 and 4 showed moderate inhibitory activity with an IC50 value of 23.8 ± 6.21 and 67.8 ± 5.80 μg/ml respectively. Among the four compounds, luteolin was found to be the most potent PTP1B inhibitor compared to the positive control ursolic acid, with an IC50 value of 8.12 ± 1.06 μg/ml. These results indicate that flavonoids constituents contained in Lippia graveolens can be considered as a natural source for the treatment of type 2 diabetes.

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