Identification of peptide molecular weight from rice bran protein hydrolysate with high antioxidant activity

2016 ◽  
Vol 69 ◽  
pp. 329-335 ◽  
Author(s):  
Parichart Thamnarathip ◽  
Kamolwan Jangchud ◽  
Sunee Nitisinprasert ◽  
Bongkosh Vardhanabhuti
2021 ◽  
Author(s):  
Kanrawee Hunsakul ◽  
Thunnop Laokuldilok ◽  
Vinyoo Sakdatorn ◽  
Wannaporn Klangpetch ◽  
Niramon Utama-ang

Abstract This study aimed to optimize the hydrolysis conditions for producing jasmine rice bran protein hydrolysate (JBH) using response surface methodology (RSM). The independent variables were the ratio of flavourzyme to alcalase (Fl: Al; 0: 100 to 15: 85; 2.84% enzyme concentration) and hydrolysis time (60–540 min). The optimum hydrolysate was obtained at an Fl: Al ratio of 9.81: 90.19 for 60 min, since it enabled high amounts of protein, high antioxidant activity and more low molecular weight proteins. The experimental values obtained were a degree of hydrolysis (DH) of 7.18%, a protein content of 41.73%, an IC50 for DPPH of 6.59 mg/mL, an IC50 for ABTS of 0.99 mg/mL, FRAP of 724.81 mmol FeSO4/100 g, and 322.35 and 479.05 mAU*s for peptides with a molecular weight of <3 and 3–5 kDa, respectively. Using a mixture of enzymes revealed the potential of mixed enzymes to produce JBH containing more small peptides and high antioxidant activity.


Author(s):  
Imboon WONGTHAWEEWATANA ◽  
Thongchai Rohitatisha SRINOPHAKUN ◽  
Issara SARAMALA ◽  
Kittiwut KASEMWONG

2020 ◽  
Vol 859 ◽  
pp. 9-14
Author(s):  
Thaniya Wunnakup ◽  
Chaowalit Monton ◽  
Laksana Charoenchai ◽  
Duangdeun Meksuriyen

The objective of this study was to apply rice bran protein hydrolysates (RBH) as bioactive additives of gelatin/Eudragit® NE 30D film and characterize the physicochemical and mechanical properties of its. The RBH was obtained by extraction with 2% sodium chloride (RBH-NaCl) and 0.1 N sodium hydroxide (RBH-NaOH) followed by digestion with Alcalase®. Then, RBH was incorporated in gelatin/Eudragit® NE 30D film. Effect of RBHs on film thickness, moisture content, pH, Young's modulus, tensile strength and the elongation at break were investigated. The RBH-NaCl enriched film showed non-homogeneous mixture and reduced moisture content, tensile strength and the elongation at break (1.8 – 2 folds). However, the RBH-NaOH enriched film exhibited a few non-homogeneous mixture and the Young's modulus was slightly decreased. The pH value was increased in the range of 6.77 – 6.88. Our results provide insight for the potential to develop RBH containing films as topical products.


Molecules ◽  
2019 ◽  
Vol 24 (8) ◽  
pp. 1628 ◽  
Author(s):  
Yuchen Guo ◽  
Nicholas Michael ◽  
Jorge Fonseca Madrigal ◽  
Carlos Sosa Aguirre ◽  
Paula Jauregi

Pterygoplichthys disjunctivus, locally named the armoured catfish, is a by-catch of tilapia fishing that accounts for up to 80% of total captured fish in the Adolfo Lopez Mateos dam, in Michoacán, México, affecting the economy of its surrounding communities. This invasive fish is discarded by fishermen since native people do not consume it, partly due to its appearance, yet it is rich in protein. The aim of this study was to produce hydrolysates from armoured catfish using food-grade proteases (neutrases HT and PF and alcalase PAL) and investigate the processing conditions (pH and temperature) that lead to a high degree of hydrolysis, antioxidant activity, and Angiotensin I-Converting Enzyme (ACE) Inhibitory activity. No other similar research has been reported on this underutilized fish. The antioxidant activity was measured by three different methods, ABTS, FRAP and ORAC, with relevance to food and biological systems in order to obtain a more comprehensive assessment of the activity. In addition, the main peptide sequences were identified. All enzymes produced hydrolysates with high antioxidant activity. In particular, the protease HT led to the highest antioxidant activity according to the ABTS (174.68 μmol Trolox equivalent/g fish) and FRAP (7.59 mg ascorbic acid equivalent/g fish) methods and almost the same as PAL according to the ORAC method (51.43 μmol Trolox equivalent/g fish). Moreover, maximum activity was obtained at mild pH and temperature (7.5; 50 °C). Interestingly, the ORAC values obtained here were higher than others previously reported for fish hydrolysates and similar to those reported for fruits such as blueberries, apples and oranges. The peptide sequence IEE(E) was present in several peptides in both hydrolysates; this sequence may be partly responsible for the high antioxidant activity, particularly the one based on iron-reducing power. These findings will be relevant to the valorization of other fish/fish muscle discards and could contribute to the production of food supplements and nutraceuticals.


LWT ◽  
2019 ◽  
Vol 111 ◽  
pp. 573-581 ◽  
Author(s):  
Xiaodan Zang ◽  
Junwen Wang ◽  
Guoping Yu ◽  
Jianjun Cheng

Sign in / Sign up

Export Citation Format

Share Document