scholarly journals The Impact of the Adjunct Heat-Treated Starter Culture and Lb. helveticus LH-B01 on the Proteolysis and ACE Inhibitory Activity in Dutch-Type Cheese Model during Ripening

Animals ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 2699
Author(s):  
Monika Garbowska ◽  
Anna Berthold-Pluta ◽  
Lidia Stasiak-Różańska ◽  
Antoni Pluta
Keyword(s):  
Proteolytic Activity ◽  
Inhibitory Activity ◽  
Starter Culture ◽  
Soluble Nitrogen ◽  
Ace Inhibitory Activity ◽  
Adjunct Cultures ◽  
Heat Treated ◽  
The Impact ◽  
Cheese Model ◽  
Ace Inhibitory

Adjunct cultures are used in cheesemaking to improve the sensory characteristics of the ripened cheeses. In addition, it is known that different adjunct cultures are capable of producing enzymes with the specificity to hydrolyze caseins, leading to the release of various bioactive compounds (bioactive peptides, amino acids, etc.). The objective of this study was to evaluate the effect of adjunct heat-treated starter XT–312 and a cheese culture Lb. helveticus LH-B01 on the proteolytic activity and angiotensin converting enzymes inhibitors (ACE) in cheese models during ripening. Seven different cheese models were evaluated for: proteolytic activity using the spectrophotometric method with ortho-phthaldialdehyde (OPA), soluble nitrogen (SN), trichloroacetic acid-soluble nitrogen (TCA-SN) phosphotungstic acid-soluble nitrogen (PTA-SN), total nitrogen (TN), pH, contents of water, fat, as well as for total bacteria count (TBC), count of Lactococcus genus bacteria, count of Lb. helveticus, and number of non-starter lactic acid bacteria (NSLAB). Presence of adjunct bacterial cultures both in the form of a cheese culture LH-B01 and heat-treated XT–312 starter promoted primary and secondary proteolysis, which resulted in acceleration of the ripening process. ACE inhibitory activity and proteolytic activity was the highest throughout of ripening for cheese model with LH-B01 culture. The cheese models with the adjunct heat-treated starter were characterized by lower TBC, NSLAB and lower count of Lactococcus genus bacteria during ripening, compared to control cheeses.

scholarly journals Bacterial Community and Anti-Cerebrovascular Disease-Related Bacillus Species Isolated from Traditionally Made Kochujang from Different Provinces of Korea

2021 ◽  
Vol 9 (11) ◽  
pp. 2238
Author(s):  
Gwangsu Ha ◽  
Hee-Jong Yang ◽  
Myeong-Seon Ryu ◽  
Su-Ji Jeong ◽  
Do-Youn Jeong ◽  
...  
Keyword(s):  
Cerebrovascular Disease ◽  
Inhibitory Activity ◽  
Starter Culture ◽  
The Other ◽  
Bacillus Species ◽  
Probiotic Properties ◽  
Ace Inhibitory Activity ◽  
Lipopolysaccharide Biosynthesis ◽  
Bacillus Spp ◽  
Ace Inhibitory

Traditionally made Kochujang (TMK) is a long-term fermented soybean and rice mixture with red pepper and salts. The ambient bacteria in rice straw and nutrient components of Kochujang influence the bacteria community. We aimed to investigate the bacterial composition and quality of TMK from different provinces of Korea: Chungcheung (CC), Jeolla (JL), Kyungsang (KS), and GeongGee plus Kangwon (GK) provinces, and Jeju island (JJ). Furthermore, Bacillus spp. isolated from TMK were studied to have anti-cerebrovascular disease activity and probiotic properties. Seventy-three TMK samples from different regions were collected to assess the biogenic amine contents, bacteria composition using next-generation methods, and bacterial functions using Picrust2. Bacillus spp. was isolated from the collected TMK, and their antioxidant, fibrinolytic, and angiotensin I conversion enzyme (ACE) inhibitory activities and probiotic properties were examined. KS TMK had lower sodium contents than the other TMK. There were no significant differences in histamine and tyramine contents among the TMK samples in different provinces. The predominant bacteria in TMK was Bacillus spp., but KS included much less Bacillus spp. and higher Enterococcus and Staphylococcus than the other TMK. Gene expression related to lipopolysaccharide biosynthesis was higher in KS TMK than the other TMK in Picrust2. The predominant Bacillus spp. isolated from TMK was B. subtilis and B. velezensis. B. subtilis SRCM117233, SRCM117245, and SRCM117253 had antioxidant activity, whereas B. subtilis had higher fibrinolytic activity than other Bacillus spp. Only B. velezensis SRCM117254, SRCM117311, SRCM117314, and SRCM117318 had over 10% ACE inhibitory activity. In conclusion, KS had less Bacillus related to lower sodium contents than the other TMK. The specific strains of B. subtilis and B. velezensis had antioxidant, fibrinolytic, and ACE inhibitory activity, and they can be used as a starter culture to produce better quality controlled Kochujang with anti-cerebrovascular disease activities.

Effect of simulated gastrointestinal digestion on the antihypertensive properties of synthetic β-lactoglobulin peptide sequences

2007 ◽  
Vol 74 (3) ◽  
pp. 336-339 ◽  
Author(s):  
Blanca Hernández-Ledesma ◽  
Marta Miguel ◽  
Lourdes Amigo ◽  
Maria Amaya Aleixandre ◽  
Isidra Recio
Keyword(s):  
Inhibitory Activity ◽  
Ace Inhibition ◽  
Antihypertensive Activity ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Simulated Gastrointestinal Digestion ◽  
The Impact ◽  
Β Lactoglobulin ◽  
Ace Inhibitory

In this study, the antihypertensive activity in spontaneously hypertensive rats of two peptides isolated from β-lactoglobulin hydrolysates with thermolysin was evaluated. These peptides, with sequences LLF [β-lg f(103–105)] and LQKW [β-lg f(58–61)], showed potent in vitro ACE-inhibitory activity. Two hours after administration, both sequences caused a clear and significant decrease in the blood pressure of these rats. The impact of a simulated gastrointestinal digestion on ACE-inhibitory and antihypertensive activities of these peptides was also studied. The results showed that both fragments were susceptible to proteolytic degradation after incubation with pepsin and Corolase PP®. In addition, their in vitro ACE-inhibitory activity decreased after the simulated digestion. It is likely that fragment LQK was the active end product of the gastrointestinal digestion of peptide LQKW. The fragment LL, observed after digestion of peptide LLF, probably exert its antihypertensive effect through a mechanism of action different than ACE-inhibition.

Changes of proteolysis and angiotensin-I converting enzyme-inhibitory activity in white-brined cheese as affected by adjunct culture and ripening temperature

2014 ◽  
Vol 81 (4) ◽  
pp. 394-402 ◽  
Author(s):  
Didem Sahingil ◽  
Ali A. Hayaloglu ◽  
Huseyin A. Kirmaci ◽  
Barbaros Özer ◽  
Osman Simsek
Keyword(s):  
Inhibitory Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Water Soluble ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Adjunct Cultures ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory ◽  
Adjunct Culture

The effects of use of adjunct cultures (Lactobacillus helveticus and Lb. casei) and ripening temperatures (6 or 12 °C) on proteolysis and angiotensin-I converting enzyme (ACE)-inhibitory activity in white-brined cheeses were investigated during 120 d ripening. Proteolysis was monitored by urea-polyacrylamide gel electrophoresis (urea-PAGE) and reversed phase-HPLC (RP-HPLC) of water-insoluble and -soluble fractions of the cheeses, respectively. Urea-PAGE patterns of the samples revealed that the intensities of the bands representing casein fractions decreased in the experimental cheeses, being more pronounced in the cheeses made with adjunct cultures. Similarly, peptide profiles and the concentrations of individual and total free amino acids were influenced by both the adjunct cultures and ripening temperatures. The ACE-inhibitory activity of the water-soluble extracts of the cheeses were higher in the cheeses made using adjunct cultures (especially Lb. helveticus) and ripened at 12 °C. The ACE-inhibitory activity did not decrease during ripening. The contribution of Lb. helveticus to the development of proteolysis and ACE-inhibitory peptide activities were higher than that of Lb. casei. To conclude, the use of Lb. helveticus as adjunct culture in white-brined cheese and ripening at 12 °C would be recommended to obtain white-brined cheese with high ACE-I-inhibitory peptides activity and higher levels of preoteolysis.

scholarly journals Peptide profiling of goat milk fermented by Lactobacillus delbrueckii ssp. delbrueckii BD7: Identification of potential biological activity

2021 ◽  
Vol 22 (8) ◽  
Author(s):  
Yuliana Tandi Rubak ◽  
Lilis Nuraida ◽  
Dyah Iswantini ◽  
Endang Prangdimurti ◽  
Maxs Urias Ebenhaizar Sanam
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Starter Culture ◽  
Goat Milk ◽  
Lactobacillus Delbrueckii ◽  
Amino Acid Residues ◽  
Ace Inhibitory Activity ◽  
Ace Inhibitory

Abstract. Rubak YT, Nuraida L, Iswantini D, Prangdimurti E, Sanam MUE. 2021. Peptide profiling of goat milk fermented by Lactobacillus delbrueckii ssp. delbrueckii BD7: Identification of potential biological activity. Biodiversitas 22: 3136-3145. This study investigated the angiotensin-converting enzyme (ACE) inhibitory activity in fermented goat milk by Lactobacillus delbrueckii ssp. delbrueckii BD7, characterizing the peptide and its potential as a bioactive peptide. The starter culture (2%) was inoculated into pasteurized goat skim milk (11%), then incubated at 37 °C until it reached pH 4.6. Centrifugation at 6000 g x 10 minutes at 4 °C was applied. The supernatant obtained was then ultrafiltrated using a membrane cut-off with a molecular weight of 3 kDa, and the fraction obtained was analyzed to determine the inhibitory activity of ACE. Peptides were characterized using Nano LC / MS / MS, and identification as bioactive peptides was carried out based on a literature review. ACE inhibitory activity of fermented goat milk of Lb. delbrueckii ssp. delbrueckii BD7 was 55.98 ± 3.53%. A total of 157 peptides were released with molecular weights ranging from 770.78 - 2081.12 Da and having 7-19 amino acid residues. The main peptide was hydrolyzed from casein (72.6%), cleavage in the parent protein, specific for aliphatic and aromatic amino acids. Identification of bioactive peptides based on the similarity of amino acid residues at C-terminal obtained 28 ACE inhibitor peptides, 19 antioxidant peptides, and ten antimicrobial peptides. Some of these peptides have homologous sequences with previously reported peptides. Lb. delbrueckii ssp. delbrueckii BD7 has the potential as a starter culture to produce fermented milk, which is rich in biological activity.

Bioactive property of soymilk fermented by agrowastes‐immobilized lactobacilli

2012 ◽  
Vol 114 (9) ◽  
pp. 1339-1353 ◽  
Author(s):  
Huey‐Shi Lye ◽  
Sue‐Siang The ◽  
Ting‐Jin Lim ◽  
Rajeev Bhat ◽  
Rosma Ahmad ◽  
...  
Keyword(s):  
Proteolytic Activity ◽  
Inhibitory Activity ◽  
Cell Immobilization ◽  
Scanning Electron Micrographs ◽  
Ace Inhibitory Activity ◽  
Garcinia Mangostana ◽  
Content Type ◽  
Durio Zibethinus ◽  
Ace Inhibitory

PurposeThis study aims to evaluate the effect of cell immobilization on bioactive property of lactobacilli‐fermented soymilk.Design/methodology/approachAgrowastes from durian (Durio zibethinus), cempedak (Artocarpus champeden), and mangosteen (Garcinia mangostana) were used as immobilizers for lactobacilli (Lactobacillus acidophilus FTDC 1331, L. acidophilus FTDC 2631, L. acidophilus FTDC 2333, L. acidophilus FTDC 1733, and L. bulgaricus FTCC 0411) in soymilk fermentation. Fermented soymilk was stored at different temperatures (4°C, 25°C and 37°C) for 168 h and sampled for analyses periodically.FindingsScanning electron micrographs showed that cells of lactobacilli were immobilized onto the matrix of agrowastes powder. The proteolytic activity was higher in soymilk supplemented with immobilized lactobacilli at 37°C and 25°C compared to that at 4°C. Soymilk fermented by cells immobilized on cempedak rind powder showed higher proteolytic activity (p<0.0001), followed by durian and mangosteen rinds powder (p<0.001). The highest ACE inhibitory activity was also found in soymilk fermented by cells immobilized on cempedak rind powder for all temperatures studied (p<0.0001). In addition, ACE inhibitory activity was higher in soymilk fermented at 37°C, compared to 25°C and 4°C (p<0.0001).Originality/valueThe results in the paper show that cell immobilization enhances the bioactive property of fermented soymilk, in terms of proteolysis and in‐vitro ACE inhibitory activity.

scholarly journals Bioactivities and ACE-inhibitory peptides releasing potential of lactic acid bacteria in fermented soy milk

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
J. Undhad Trupti ◽  
Sujit Das ◽  
Divyang Solanki ◽  
Dhvany Kinariwala ◽  
Subrota Hati
Keyword(s):  
Proteolytic Activity ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Growth Behavior ◽  
Soy Milk ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptide ◽  
Inhibitory Peptides ◽  
Glucosidase Activity ◽  
Ace Inhibitory

Abstract This study was designed to evaluate the bioactivities such as β-glucosidase activity, α-galactosidase activity, and the growth behavior of the Lactobacillus cultures in soy milk medium. Ten Lactobacillus cultures were considered in this study. L. fermentum (M2) and L. casei (NK9) were selected due to their better α-galactosidase, β-glucosidase activity and growth behavior in soy milk medium during fermentation. Further, soy milk fermented with M2 showed higher proteolytic activity (0.67 OD) and ACE-inhibitory (48.44%) than NK9 (proteolytic activity: 0.48 OD and ACE-inhibitory activity: 41.33%). Bioactive peptides produced during the fermentation of soy milk using the selected Lactobacillus cultures were also identified with potent ACE-inhibitory activity by MALDI-TOF spectrometry, and the identified ACE inhibitory peptide sequences from fermented soy milk were characterized using Biopep database. Graphical abstract

Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Elk (Cervus elaphus) Velvet Antler

2005 ◽  
Vol 10 (3) ◽  
pp. 239-243 ◽  
Author(s):  
Rohan Karawita ◽  
Pyo-Jam park ◽  
Nalin Siriwardhana ◽  
Byong-Tae Jeon ◽  
Sang-Ho Moon ◽  
...  
Keyword(s):  
Cervus Elaphus ◽  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Velvet Antler ◽  
Ace Inhibitory
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