scholarly journals Computational screening of microalgae and cyanobacteria RuBisCO as potential precursor for bioactive peptides

2017 ◽  
Author(s):  
Gurudeeban Selvaraj ◽  
Satyavani Kaliamurthi ◽  
Zeynep Elibol Cakmak ◽  
Turgay Cakmak
Keyword(s):  
Bioactive Peptides ◽  
Proteolytic Enzymes ◽  
Chlorella Pyrenoidosa ◽  
Biologically Active ◽  
Proteinase K ◽  
Peptide Fragments ◽  
Bisphosphate Carboxylase ◽  
Computational Screening ◽  
Active Fragments ◽  
Chaetoceros Calcitrans

Ribulose-1,5-bisphosphate carboxylase/oxygense (RuBisCO) is present in plants and autotrophic organisms like microalgae. The aim of this study was to perform an in silico evaluation of RuBisCo protein in microalgae and cyanobacteria as potential precursors of bioactive peptides, as well as to determine whether such peptides can be released by selected proteolytic enzymes. Fourteen RuBioCo sequences of microalgae and cyanobacteria were analysed by using the BIOPEP server amd database. The biological activity, enzyme action and calculation of active peptide tools were used to determine the frequency of occurrence of fragments, proteolysis, and the frequency of release of fragments with given activity by selected enzymes. The physio-chemical parameters of the selected sequences were performed with Protpram tool. Amongst the RuBisCo proteins of selected algae, Chaetoceros. calcitrans exhibits the best prospect as a source of DPP-IV inhibiting peptides, Chlorella pyrenoidosa for ACE inhibitor and Aphanizomenon flos-aquae for antioxidative, activating ubiquitin, and antiamnestic activities. High number of bioactive fragments in Aphanizomenon flos-aquae, Dunaliella salina, Chlorella pyrenoidosa, and Chlorella vulgaris are associated with a high content of glycine and proline amino acids that are most rich in biologically active fragments. Papain and Proteinase K, an enzyme with wide specificity, can release considerably more biologically active fragments than bromealin and chymotrpsin. These findings will contribute towards consumption of microalgal and cyanobacterial RuBisCO as alternative sources of bioactive peptide fragments based nutraceuticals for human.

scholarly journals Computational screening of microalgae and cyanobacteria RuBisCO as potential precursor for bioactive peptides

2017 ◽  
Author(s):  
Gurudeeban Selvaraj ◽  
Satyavani Kaliamurthi ◽  
Zeynep Elibol Cakmak ◽  
Turgay Cakmak
Keyword(s):  
Bioactive Peptides ◽  
Proteolytic Enzymes ◽  
Chlorella Pyrenoidosa ◽  
Biologically Active ◽  
Proteinase K ◽  
Peptide Fragments ◽  
Bisphosphate Carboxylase ◽  
Computational Screening ◽  
Active Fragments ◽  
Chaetoceros Calcitrans

Ribulose-1,5-bisphosphate carboxylase/oxygense (RuBisCO) is present in plants and autotrophic organisms like microalgae. The aim of this study was to perform an in silico evaluation of RuBisCo protein in microalgae and cyanobacteria as potential precursors of bioactive peptides, as well as to determine whether such peptides can be released by selected proteolytic enzymes. Fourteen RuBioCo sequences of microalgae and cyanobacteria were analysed by using the BIOPEP server amd database. The biological activity, enzyme action and calculation of active peptide tools were used to determine the frequency of occurrence of fragments, proteolysis, and the frequency of release of fragments with given activity by selected enzymes. The physio-chemical parameters of the selected sequences were performed with Protpram tool. Amongst the RuBisCo proteins of selected algae, Chaetoceros. calcitrans exhibits the best prospect as a source of DPP-IV inhibiting peptides, Chlorella pyrenoidosa for ACE inhibitor and Aphanizomenon flos-aquae for antioxidative, activating ubiquitin, and antiamnestic activities. High number of bioactive fragments in Aphanizomenon flos-aquae, Dunaliella salina, Chlorella pyrenoidosa, and Chlorella vulgaris are associated with a high content of glycine and proline amino acids that are most rich in biologically active fragments. Papain and Proteinase K, an enzyme with wide specificity, can release considerably more biologically active fragments than bromealin and chymotrpsin. These findings will contribute towards consumption of microalgal and cyanobacterial RuBisCO as alternative sources of bioactive peptide fragments based nutraceuticals for human.

Bovine Meat Proteins as Potential Precursors of Biologically Active Peptides - a Computational Study based on the BIOPEP Database

2011 ◽  
Vol 17 (1) ◽  
pp. 39-45 ◽  
Author(s):  
P. Minkiewicz ◽  
J. Dziuba ◽  
J. Michalska
Keyword(s):  
Proteolytic Enzymes ◽  
Computational Study ◽  
Angiotensin Converting Enzyme Inhibitors ◽  
Biologically Active ◽  
Proteinase K ◽  
Converting Enzyme Inhibitors ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
Meat Proteins ◽  
Active Fragments

The aim of the present study was to perform an in silico evaluation of bovine meat proteins as potential precursors of biologically active peptides, as well as to determine whether such peptides can be released by selected proteolytic enzymes. The sequences of 19 bovine meat proteins were processed using the BIOPEP database and program. The profiles of potential biological activity of protein fragments were determined and the following parameters were calculated: the frequency of occurrence of fragments with given activity (A), the frequency of release of fragments with given activity by selected enzymes (AE), and the relative frequency of release of fragments with given activity by selected enzymes (W). Among the examined proteins, collagen and elastin appear to be the richest potential source of bioactive peptides, in particular of angiotensin-converting enzyme inhibitors, antithrombotic fragments, inhibitors of dipeptidyl peptidase IV and peptides regulating gastric mucosal activity. The high number of bioactive fragments in collagen and elastin is associated with a high content of glycine and proline, amino acids that are most abundant in biologically active fragments. Of the two investigated proteolytic enzymes, Proteinase K — an enzyme with broad specificity (e.g., against peptide bonds formed by the carboxyl groups of proline) can release considerably more biologically active fragments than Proteinase P1 — an enzyme with narrow specificity, not including proline residues.

Biofunctional properties of milk protein derived bioactive peptides -A review

2015 ◽  
Vol 34 (4) ◽  
Author(s):  
Prasad Patil ◽  
Akanksha Wadehra ◽  
Varsha Garg ◽  
Kanchan Munjal ◽  
Sudhir Kumar Tomar ◽  
...  
Keyword(s):  
Milk Protein ◽  
Bioactive Peptides ◽  
Therapeutic Potential ◽  
Proteolytic Enzymes ◽  
Biological Activities ◽  
Milk Proteins ◽  
Physiological Effect ◽  
Amino Acid Sequences ◽  
The Body ◽  
Biologically Active

Milk has long been acknowledged as a source of macro- and micro nutrients. Presently, several identified biologically active substances from milk and their derivatives has attracted much attention from the scientific community. These bioactive compounds confer many health benefits that might support disease prevention. Worldwide, there is an increasing interest in the therapeutic potential of bioactive peptides which collectively present a cornucopia of bioactivities for utilization in humans. Bioactive peptides are hydrolysates with specific amino acid sequences that exert a positive physiological effect on the body. Most of the biological activities are encrypted within the primary sequence of the native protein and can be released during digestion by proteolytic enzymes in the gastrointestinal tract or during fermentation and food processing. Milk protein is an important source of bioactive peptides which may contribute to regulate the nervous, gastrointestinal, and cardiovascular systems as well as the immune system. Milk protein derived bioactive peptides are shown to have antihypertensive, antimicrobial, immunomodulatory, antioxidative and mineral-binding properties. Bioactive peptides derived from milk proteins are of particular interest to the food industry due to the potential functional and physiological roles that they exhibit.

Synthesis of the carboxy-terminal octapeptide of cholecystokinin (CKK-8) based on incorporation of O4-sulfotyrosine by enzymatically catalyzed formation of peptide bonds

1988 ◽  
Vol 53 (5) ◽  
pp. 1086-1093 ◽  
Author(s):  
Václav Čeřovský ◽  
Jan Hlaváček ◽  
Jiřina Slaninová ◽  
Karel Jošt
Keyword(s):  
Aspartic Acid ◽  
Sodium Salt ◽  
Proteolytic Enzymes ◽  
Biological Activities ◽  
Proteinase K ◽  
Side Chain ◽  
Peptide Fragments ◽  
Peptide Bonds ◽  
Carboxy Terminal ◽  
Amide Fragment

Papain-catalyzed condensation of sodium salt of tert-butyloxycarbonyl-β-tert-butyloxyaspartyl-O4-sulfotyrosine (fragment 1-2) with methionyl-glycyl-tryptophyl-methionyl-aspartyl-phenylalanine amide (fragment 3-8) has been elaborated. Deprotection of the thus-obtained octapeptide afforded CCK-8 which exhibited full biological activities. Benzyloxycarbonylaspartyl-phenylalanine amide (fragment 7-8) was prepared using thermolysin without protecting the aspartic acid side chain. Attempted condensation of tert-butyloxycarbonylmethionyl-glycyl-tryptophan (fragment 3-5) with methionyl-aspartyl-phenylalanine amide (fragment 6-8), catalyzed by α-chymotrypsin, subtilisin or proteinase K, afforded the product (fragment 3-8) in only low yields. Further use of proteolytic enzymes for preparing other peptide fragments of the CCK-8 molecule without side chain protection is investigated.

scholarly journals Peptide Extracts from Seven Medicinal Plants Discovered to Inhibit Oomycete Phytophthora infestans, a Causative Agent of Potato Late Blight Disease

Plants ◽  
2020 ◽  
Vol 9 (10) ◽  
pp. 1294
Author(s):  
Eugene A. Rogozhin ◽  
Alexey S. Vasilchenko ◽  
Anna S. Barashkova ◽  
Alexey N. Smirnov ◽  
Sergey K. Zavriev ◽  
...  
Keyword(s):  
Amino Acid ◽  
Medicinal Plants ◽  
Late Blight ◽  
Phytophthora Infestans ◽  
Causative Agent ◽  
Biologically Active ◽  
Peptide Fragments ◽  
Bisphosphate Carboxylase ◽  
Late Blight Disease ◽  
Blight Disease

We report the inhibitory effect of peptide extracts obtained from seven medicinal plants against a causative agent of late blight disease Phytophthora infestans. We find that all the extracts possess inhibitory activity toward the zoospores output, zoosporangium germination, and the development of P. infestans on potato disc tubers at different quantitative levels. Based on the biological effects detected, an extract of common horsetail (Equisetum arvense) biomass is recognized as the most effective and is selected for further structural analysis. We perform a combination of amino acid analysis and MALDI-TOF mass spectrometry, which reveal the presence of Asn/Asp- and Gln/Glu-rich short peptides with molecular masses in the range of 500–900 Da and not exceeding 1500 Da as the maximum. Analytical anion-exchange HPLC is successfully applied for separation of the peptide extract from common horsetail (E. arvense). We collect nine dominant components that are combined in two groups with differences in retention times. The N-terminal amino acid sequence of the prevalent compounds after analytical ion-exchange HPLC allows us to identify them as peptide fragments of functionally active proteins associated with photosynthesis, aquatic transport, and chitin binding. The anti-oomycete effects may be associated with the conversion of ribulose-1,5-bisphosphate carboxylase/oxygenase to produce a number of biologically active anionic peptides with possible regulatory functions. These data inform our knowledge regarding biologically active peptide fragments; they are the components of programmed or induced proteolysis of plant proteins and can realize secondary antimicrobial functions.

scholarly journals Potential Relevance of Bioactive Peptides in Sports Nutrition

Nutrients ◽  
2021 ◽  
Vol 13 (11) ◽  
pp. 3997
Author(s):  
Daniel König ◽  
Jan Kohl ◽  
Simon Jerger ◽  
Christoph Centner
Keyword(s):  
Bioactive Peptides ◽  
Positive Impact ◽  
Proteolytic Enzymes ◽  
Sports Nutrition ◽  
Biologically Active ◽  
Rehabilitation Process ◽  
Practical Applications ◽  
Active Peptides ◽  
Health Related ◽  
Positive Effect

Bioactive peptides are physiologically active peptides mostly derived from proteins following gastrointestinal digestion, fermentation or hydrolysis by proteolytic enzymes. It has been shown that bioactive peptides can be resorbed in their intact form and have repeatedly been shown to have a positive effect on health-related parameters such as hypertension, dyslipoproteinemia, inflammation and oxidative stress. In recent years, there has been increasing evidence that biologically active peptides could also play an important role in sports nutrition. Current studies have shown that bioactive peptides could have a positive impact on changes in body composition and muscular performance, reduce muscle damage following exercise and induce beneficial adaptions within the connective tissue. In the following overview, potential mechanisms as well as possible limitations regarding the sports-related effect of bioactive peptides and their potential mechanisms are presented and discussed. In addition, practical applications will be discussed on how bioactive peptides can be integrated into a nutritional approach in sports to enhance athletic performance as well as prevent injuries and improve the rehabilitation process.

scholarly journals Weissellicin 110, a Newly Discovered Bacteriocin from Weissella cibaria 110, Isolated from Plaa-Som, a Fermented Fish Product from Thailand

2007 ◽  
Vol 73 (7) ◽  
pp. 2247-2250 ◽  
Author(s):  
Sirinat Srionnual ◽  
Fujitoshi Yanagida ◽  
Li-Hsiu Lin ◽  
Kuang-Nan Hsiao ◽  
Yi-sheng Chen
Keyword(s):  
Proteolytic Enzymes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Band ◽  
Proteinase K ◽  
Mass Spectrometry Analysis ◽  
Fermented Fish ◽  
Spectrometry Analysis ◽  
Weissella Cibaria ◽  
Fish Product

ABSTRACT Weissella cibaria 110, isolated from the Thai fermented fish product plaa-som, was found to produce a bacteriocin active against some gram-positive bacteria. Bacteriocin activity was not eliminated by exposure to high temperatures or catalase but was destroyed by exposure to the proteolytic enzymes proteinase K and trypsin. The bacteriocin from W. cibaria 110 was purified, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the purified bacteriocin contained one protein band that was approximately 2.5 kDa in size. Mass spectrometry analysis showed the mass of the peptide to be approximately 3,487.8 Da. N-terminal amino acid sequence analysis was performed, and 27 amino acids were identified. Because it has no similarity to other known bacteriocins, this bacteriocin was defined as a new bacteriocin and termed weissellicin 110.

The role of hemorheological disorders in the pathogenesis of hemorrhagic pancreonecrosis

2021 ◽  
Author(s):  
Н.П. Александрова ◽  
В.И. Карандашов ◽  
А.В. Варданян
Keyword(s):  
Sialic Acid ◽  
Shear Rate ◽  
Electrophoretic Mobility ◽  
Blood Viscosity ◽  
Proteolytic Enzymes ◽  
Biologically Active ◽  
Erythrocyte Aggregation ◽  
Control Group ◽  
Mechanical Resistance

Введение. Вопросы патогенеза острого панкреатита и панкреонекроза до настоящего времени остаются в центре внимания исследователей и клиницистов. До сих пор до конца не выяснена роль изменений в системе гемостаза и гемореологических нарушений в развитии этого заболевания. Цель исследования: установить роль гемореологических нарушений в патогенезе геморрагического панкреонекроза и изучить специфику механизма этих расстройств. Материалы и методы. Обследовано 29 пациентов с геморрагическим панкреонекрозом (12 женщин и 17 мужчин) в возрасте от 23 до 60 лет. Исследовали вязкость крови, показатель гематокрита, количество эритроцитов и их диаметр, агрегацию, электрофоретическую подвижность, деформируемость и механическую резистентность эритроцитов, белковый состав плазмы, содержание сиаловой кислоты в плазме и в эритроцитах, параметры липидного обмена, содержание кальция и фибриногена в крови,фибринолитическую активность крови и агрегационную активность тромбоцитов, гемокоагуляционная активность исследована методом тромбоэластографии. Для определения нормальных значений исследованных показателей было обследовано 15 практически здоровых лиц (7 женщин и 8 мужчин). Результаты. У больных панкреонекрозом самым грубым нарушениям подвергаются эритроциты: их механическая резистентность снижалась в 2 раза, объем увеличивался на 18,7%, деформируемость падала на 43,8%, количество снижалось на 8,75%, показатель гематокрита при этом оставался на уровне нормальных значений по причине увеличенного объема (сферичности) клеток; в 1,8 раза возрастала агрегация эритроцитов. Вязкость крови при скорости сдвига 1 c–1 увеличивалась в 3,3 раза, а при скорости сдвига 150 c–1 — в 1,58 раза по сравнению с нормой. Причиной повышения агрегации эритроцитов являлось снижение их электрофоретической подвижности на 35,9% из-за десиализации их мембран: концентрация сиаловой кислоты в клеточных мембранах была снижена на 20,8%, а содержание конъюгированной сиаловой кислоты в плазме увеличено в 2,25 раза по сравнению с нормальными значениями. Заключение. Гемореологические расстройства, которые возникают первоначально у больных геморрагическим панкреонекрозом как результат некротических изменений поджелудочной железы, с определенного, довольно раннего этапа сами становятся фактором патогенеза данного заболевания. Доминирующим фактором прогрессивного увеличения вязкости крови у больных панкреонекрозом является нарушение морфофункциональных и физико-химических свой ств эритроцитов на фоне высокой активности протеолитических ферментов, биологически активных аминов и крайней степени токсемии. Background. The pathogenesis of acute pancreatitis and pancreonecrosis is still the focus of researchers and clinicians. The role of hemorheological disorders in these diseases remain uncertain until now. Objectives: to define the role of hemorheological disorders in the pathogenesis of hemorrhagic pancreonecrosis and to study the specifics of the mechanism of these disorders. Patients/Methods. This study included 29 patients (12 women and 17 men, age of 23 to 60 years old) with hemorrhagic pancreatic necrosis. We examined blood viscosity, hematocrit and some erythrocyte properties as count, diameter, aggregation, electrophoretic mobility, deformability and mechanical resistance; other investigated parameters were plasma protein composition, plasma and erythrocytes sialic acid concentrations, lipids, total calcium and fibrinogen concentrations, blood fibrinolytic activity, platelets aggregation activity; total hemocoagulation activity was studied with thromboelastography. Control group contained 15 practically healthy individuals (7 women and 8 men). Results. Expressed disturbances of blood rheological properties, mostly in erythrocytes were detected in patients with pancreonecrosis. Red blood cells (RBC) showed 2-times decreasing of mechanical resistance, of their volume by 18.7%, of deformability by 43.8%, of count by 8.75%. Hematocrit remained normal level due to RBC increased volume (sphericity). RBC aggregation had been increased by 1.8 times. Blood viscosity at the shear rate of 1 s–1 was increased by 3.3 times and at the shear rate of 150 s–1 by 1.58 times. Raised erythrocyte aggregation was caused by a decrease of RBC electrophoretic mobility of 35.9%. Sialic acid concentration in RBC membranes was lower of 20.8% whereas conjugated sialic acid in plasma showed increasing by 2.25 times. Conclusions. RBC morphofunctional and physicochemical disturbances cause the increase in blood viscosity in patients with pancreonecrosis. It is distinguishing feature of hemorheological disorders in hemorrhagic pancreonecrosis developing, seems, due to high activity of proteolytic enzymes and biologically active amines. Of particular importance in hemorrhagic pancreonecrosis belong to platelet involving into intravascular coagulation.

PERSPECTIVES OF BIOINFORMATICS FOR RESEARCHING FOOD BIOACTIVE PEPTIDES USING IN SILICO INSTRUMENTS

2020 ◽  
Author(s):  
К.А. РЯЗАНЦЕВА ◽  
Е.Ю. АГАРКОВА
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
Rapid Development ◽  
Biologically Active ◽  
Food Proteins ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
Speed Up ◽  
Bioinformatic Approaches

В статье приведен обзор основных классических подходов к производству биологически активных пептидов (БП) и способы их идентификации. Показано, что традиционно используемые способы получения и анализа БП требуют значительных временных и материальных затрат, что ограничивает подробные исследования и оперативную разработку БП. Новые биоинформационные подходы in silico, используемые для идентификации, характеристики, разработки биоактивных механизмов и производства БП из пищевых белков, могут упростить получение и исследование БП, что позволит ускорить разработку функциональных продуктов с использованием БП. The article describes the main classical approaches to the production of biologically active peptides and methods for their identification. It has been shown that the traditionally used methods of obtaining and analyzing bioactive peptides (BP) are not only very costly, but also require a significant amount of time, which limits detailed research and rapid development of BP. New bioinformatic approaches in silico used for identification, characterization, development of bioactive mechanisms and production of BP from food proteins can simplify the production and study of biologically active peptides, which will speed up the development of functional products using BP.

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