Microbial bioconversion of feathers into antioxidant peptides and pigments and their liposome encapsulation

2021 ◽  
Author(s):  
Diego Bertolini ◽  
Maria Elisa Pailliè Jiménez ◽  
Cristiane dos Santos ◽  
Ana Paula Folmer Corrêa ◽  
Adriano Brandelli
Keyword(s):  
Antioxidant Peptides ◽  
Liposome Encapsulation

Thrombolytic Treatment with Tissue-type Plasminogen Activator (t-PA) Containing Liposomes in Rabbits: a Comparison with Free t-PA

1995 ◽  
Vol 73 (03) ◽  
pp. 488-494 ◽  
Author(s):  
J L M Heeremans ◽  
R Prevost ◽  
M E A Bekkers ◽  
P Los ◽  
J J Emeis ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Therapeutic Index ◽  
Tissue Type ◽  
Jugular Vein Thrombosis ◽  
Thrombolytic Activity ◽  
Tissue Type Plasminogen Activator ◽  
Liposome Encapsulation ◽  
Thrombosis Model ◽  
Lysis Activity ◽  
Type Plasminogen Activator

SummaryIn this study, we aimed at improving the therapeutic index of tissue- type Plasminogen Activator (t-PA) as thrombolytic agent in the treatment of myocardial infarction. Liposome-encapsulated t-PA was tested in a rabbit jugular vein thrombosis model: administration of free t-PA (t-PA) as a bolus injection in the ear vein was compared to a similar administration of liposomal t-PA (t-PA-lip), liposomal t-PA in plasminogen-coated liposomes (Plg-t-PA-lip), a mixture of free t-PA and empty liposomes (t-PA+empty lip) and a saline-blank (blank) in terms of thrombolytic activity and side effects.Liposomal t-PA (t-PA-lip/Plg-t-PA-lip) showed a significantly better thrombolysis efficiency than equimolar doses of free t-PA (t-PA/ t-PA+ empty lip): about 0.24 mg/kg of liposomal t-PA practically equalled the lysis-activity of a dose of free t-PA of 1.0 mg/kg (t-PAlmg/kg). On the other hand, liposome encapsulation did not affect the systemic activation of alpha2-antiplasmin and plasminogen by t-PA.We conclude that for this model an improvement in thrombolytic efficacy of t-PA is achieved by liposome encapsulation of t-PA. As t-PA-lip and Plg-t-PA-lip -treatment induced similar results, targeting of liposomal t-PA by coupled glu-Plg remains a topic to be optimized in future studies.

scholarly journals Physicochemical characteristics of liposome encapsulation of stingless bees' propolis

Heliyon ◽  
2021 ◽  
Vol 7 (4) ◽  
pp. e06649
Author(s):  
N.A. Ramli ◽  
N. Ali ◽  
S. Hamzah ◽  
N.I. Yatim
Keyword(s):  
Stingless Bees ◽  
Physicochemical Characteristics ◽  
Liposome Encapsulation

scholarly journals Antioxidant properties and inhibition of angiotensin-converting enzyme by highly active peptides from wheat gluten

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Wen-Ying Liu ◽  
Jiang-Tao Zhang ◽  
Takuya Miyakawa ◽  
Guo-Ming Li ◽  
Rui-Zeng Gu ◽  
...  
Keyword(s):  
Wheat Gluten ◽  
Antioxidant Properties ◽  
Converting Enzyme ◽  
Antioxidant Peptides ◽  
Active Peptides ◽  
Inhibitory Peptides ◽  
Highly Active ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

AbstractThis study aimed to focus on the high-value utilization of raw wheat gluten by determining the potent antioxidant peptides and angiotensin I-converting enzyme (ACE) inhibitory peptides from wheat gluten oligopeptides (WOP). WOP were analyzed for in vitro antioxidant activity and inhibition of ACE, and the identification of active peptides was performed by reversed-phase high-performance liquid chromatography and mass spectrometry. Quantitative analysis was performed for highly active peptides. Five potent antioxidant peptides, Leu-Tyr, Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr and Arg-Gly-Gly-Tyr (6.07 ± 0.38, 7.28 ± 0.29, 11.18 ± 1.02, 5.93 ± 0.20 and 9.04 ± 0.47 mmol 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid (Trolox) equivalent/g sample, respectively), and five potent ACE inhibitory peptides, Leu-Tyr, Leu-Val-Ser, Tyr-Gln, Ala-Pro-Ser-Tyr and Arg-Gly-Gly-Tyr (half maximal inhibitory concentration (IC50) values = 0.31 ± 0.02, 0.60 ± 0.03, 2.00 ± 0.13, 1.47 ± 0.08 and 1.48 ± 0.11 mmol/L, respectively), were observed. The contents of Leu-Tyr, Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr, Arg-Gly-Gly-Tyr, and Leu-Val-Ser were 155.04 ± 8.36, 2.08 ± 0.12, 1.95 ± 0.06, 22.70 ± 1.35, 0.25 ± 0.01, and 53.01 ± 2.73 μg/g, respectively, in the WOP. Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr, Arg-Gly-Gly-Tyr, and Leu-Val-Ser are novel antioxidative/ACE inhibitory peptides that have not been previously reported. The results suggest that WOP could potentially be applied in the food industry as a functional additive.

Identification of antioxidant peptides from Cheddar cheese made with Lactobacillus helveticus

LWT ◽  
2021 ◽  
pp. 110866
Author(s):  
Wanshuang Yang ◽  
Xinyue Hao ◽  
Xiuxiu Zhang ◽  
Gengxu Zhang ◽  
Xiaodong Li ◽  
...  
Keyword(s):  
Cheddar Cheese ◽  
Lactobacillus Helveticus ◽  
Antioxidant Peptides

scholarly journals Identification and Characterization of Novel Antioxidant Protein Hydrolysates from Kiwicha (Amaranthus caudatus L.)

Antioxidants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 645
Author(s):  
Sergio Montserrat-de la Paz ◽  
Alicia Martinez-Lopez ◽  
Alvaro Villanueva-Lazo ◽  
Justo Pedroche ◽  
Francisco Millan ◽  
...  
Keyword(s):  
Antioxidant Capacity ◽  
Reducing Power ◽  
Protein Isolate ◽  
Protein Hydrolysates ◽  
Antioxidant Peptides ◽  
Amaranthus Caudatus ◽  
Intact Proteins ◽  
Identification And Characterization

Kiwicha (Amaranthus caudatus) is considered one of the few multipurpose pseudocereals for its potential use not only as a source of nutrients and fiber but also for its bioactive compounds. In recent years, antioxidant peptides are commonly used as functional ingredient of food. Herein, a kiwicha protein isolate (KPI), obtained from kiwicha defatted flour (KDF), was hydrolyzed by Bioprotease LA 660, a food-grade endoprotease, under specific conditions. The resulting kiwicha protein hydrolysates (KPHs) were chemically characterized and their digestibility and antioxidant capacity were evaluated by in vitro cell-free experiments owing to their measure of capacity to sequester DPPH free radical and reducing power. KPHs showed higher digestibility and antioxidant capacity than intact proteins into KPI. Therefore, the results shown in this study indicate that KPHs could serve as an adequate source of antioxidant peptides, representing an effective alternative to the generation of functional food.

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