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A comparative study between tilapia (oreochromis niloticus) by-product and tilapia protein hydrolysate on angiotensin I-converting enzyme (ace) inhibition activities and functional properties

Siti Mazlina Mustapa Kamal, Khairul Faezah Md. Yunos, Norhafizah Abdullah

Sains Malaysiana, 2018;47:309-318.

Tilapia is a popular freshwater fish and among the important cultured fish grown worldwide. In this study, fish protein
hydrolysate was produced from tilapia (Oreochromis niloticus) by-product (TB) and tilapia muscle (TM) through enzymatic
hydrolysis using alcalase. The TB and TM protein hydrolysates were evaluated for its characteristics in terms of angiotensin
I-converting enzyme (ACE) inhibition activity, peptide size distribution, and functional properties. Hydrolysis for 1 h for
TB and TM successfully produced low molecular weight peptides (<14.2kDa) with the highest ACE inhibitory activities.
The findings also demonstrated that both samples have high nitrogen solubility (>80% at pH2-9) and good emulsifying,
water and oil holding capacities. The study indicated that tilapia protein hydrolysates have the potential to be used as
functional food products.

Matched MeSH terms: Subtilisins
Fulltext A response surface approach on hydrolysis condition of eel (Monopterus Sp.) protein hydrolysate with antioxidant activity

Halim, N. R. A., Sarbon, N. M.

International Food Research Journal, 2017;24(3):1081-1093.
MyJurnal

The study aims to determine the optimized condition of eel protein hydrolysate (EPH)
produced using alcalase. The proximate compositions of eel flesh were determined as well.
Enzymatic hydrolysis conditions were optimized using response surface methodology (RSM)
by applying four factors, 3-levels Central Composite Design (CCD) with six centre points. The
model equation was proposed with regards to the time (60min, 120min, 180min), temperature
(40°C, 50°C, 60°C), pH (7, 8, 9) and enzyme concentration (1%, 2%, 3%). The optimum of
hydrolysis condition that be suggested to obtain the optimum yield, degree of hydrolysis (DH)
and antioxidant activity were 84.02 min, 50.18°C, pH 7.89 and 2.26% [enzyme]. The predicted
response values using quadratic model were 10.03% for yield, 83.23% for DH and 89.24%
for antioxidant activity. The chemical composition determination showed that the protein
content increased by more than 5-fold (16.88% to 98.53%) while the fat content was decreased
by 96.48% after hydrolysis. Hydrolysis process had significantly increased the amount of
both hydrophilic (serine and threonine) and hydrophobic amino acids (valine, isoleucine,
phenylalanine, methionine) which contributed to the antioxidant activity of hydrolyzed eel
protein. The enzymatic hydrolysis of eel protein had improved the protein content of EPH with
potential as new natural antioxidant.

Matched MeSH terms: Subtilisins
Fulltext ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

Mahmoodani F, Ghassem M, Babji AS, Yusop SM, Khosrokhavar R

J Food Sci Technol, 2014 Sep;51(9):1847-56.
PMID: 25190839 DOI: 10.1007/s13197-012-0742-8

Skin and bone gelatins of pangasius catfish (Pangasius sutchi) were hydrolyzed with alcalase to isolate Angiotensin Converting Enzyme (ACE) inhibitory peptides. Samples with the highest degree of hydrolysis (DH) were separated into different fractions with molecular weight cut-off (MWCO) sizes of 10, 3 and 1 kDa, respectively and assayed for ACE inhibitory activity. Skin and bone gelatins had highest DH of 64.87 and 68.48 % after 2 and 1 h incubation, respectively. Results from this study indicated that by decreasing the molecular weight of fractions, ACE inhibitory activity was increased. Therefore, F3 permeates (MWCO

Matched MeSH terms: Subtilisins
Fulltext Angiotensin-I converting enzyme (ACE) inhibitory peptides from chicken skin gelatin hydrolysate and its antihypertensive effect in spontaneously hypertensive rats

Sarbon, N.M., Howell, N.K., Wan Ahmad, W.A.N.

International Food Research Journal, 2019;26(3):903-911.
MyJurnal

Chicken skin gelatin hydrolysates and peptides with angiotensin converting enzyme inhibitory (ACEI) activity were produced enzymatically using alcalase, pronase E, and collagenase before fractionation into

Matched MeSH terms: Subtilisins
Fulltext Biochemical properties of red tilapia (Oreochromis niloticus) protein hydrolysates

Shamloo, M., Bakar, J., Mat Hashim, D., Khatib, A.

International Food Research Journal, 2012;19(1):183-188.
MyJurnal

The amino-acid composition, 2, 2-Diphenyl-1-picryhydrazyl (DPPH) radical-scavenging activity, and peptide patterns of tilapia protein hydrolysates produced by the enzymatic hydrolysis of Alcalase (AH), Flavourzyme (FH) and Protamex (PH) for 5h using pH-stat method were studied. The ratio of essential amino acids to non-essential amino acids increased after hydrolysis in all samples; however, no significant differences among them were observed. AH had a highest (P < 0.05) DPPH radical-scavenging activity, but no significant difference in the DPPH between FH and PH was observed. SDS-PAGE patterns for all the hydrolysates showed significant (P < 0.05) reduction in the number and the intensity of the bands with increasing time of hydrolysis. Flavourzyme showed the lowest rate of hydrolytic activity towards the tilapia mince.

Matched MeSH terms: Subtilisins
Fulltext Bitterness of green mussel (Perna viridis) hydrolysate as influenced by the degree of hydrolysis

Normah, I., Siti Hafsah, M.S., Nurul Izzaira, A.

International Food Research Journal, 2013;20(5):2261-2268.
MyJurnal

Green mussel (Perna viridis) was hydrolysed with alcalase under two different conditions consisting of pH7, E/S5% or pH 9, E/S 3% at 60°C for two hours. Hydrolysis at pH 9, E/S3% resulted in a higher degree of hydrolysis (DH) than pH7, E/S5% with degree of hydrolysis of 37.00% and 28.33%, respectively. The green mussel hydrolysates were characterized by molecular weight of

Matched MeSH terms: Subtilisins
Fulltext Characteristics of threadfin bream (nemipterus japonicas) hydrolysate produced using bilimbi (averrhoa bilimbi l.) protease and alcalase

Normah, I., Nur Anati, J.

International Food Research Journal, 2015;22(6):2259-2266.
MyJurnal

Threadfin bream (Nemipterus japonicas) muscle was hydrolysed using protease extracted from
bilimbi (Averrhoa bilimbi L.) fruit. This study was performed in order to compare the efficiency of bilimbi protease in producing threadfin bream protein hydrolysate with the commercial protease; alcalase 2.4 L. Initially, protease was extracted and then purified using 40% ammonium sulfate precipitation method. The proteolytic activity of the crude extract and purified protease was determined. Precipitation using 40% ammonium sulfate resulted in bilimbi protease specific activity of 2.36 U/mg and 23.13% recovery. Threadfin bream hydrolysate was prepared based on the pH-stat method by hydrolysis for 2 hrs. Hydrolysis using bilimbi protease produced 34.76% degree of hydrolysis (DH) and 3.75% yield while hydrolysis using alcalase resulted in 86.6% DH with 22.78% yield. Alcalase hydrolysate showed higher solubility than bilimbi protease hydrolysate at pH 7 with 70.87 and 32.16% solubility, respectively. Results also showed that protein content of threadfin bream hydrolysate produced using alcalase was higher (86.86%) than those produced using bilimbi protease (22.12%). However, both hydrolysates showed low moisture content between 3.93 to 7.00%. The molecular weight distribution analysis using SDS–PAGE indicated the distribution of smaller peptides especially in alcalase hydrolysate. Overall, the results showed that alcalase is more efficient enzyme choice than bilimbi protease for preparing threadfin bream hydrolysates. However, both hydrolysates could play an important role thus contribute to the food industry.

Matched MeSH terms: Subtilisins
Cost-Effectiveness Analysis of Non-Statin Lipid-Modifying Agents for Secondary Cardiovascular Disease Prevention Among Statin-Treated Patients in Thailand

Kongpakwattana K, Ademi Z, Chaiyasothi T, Nathisuwan S, Zomer E, Liew D, et al.

Pharmacoeconomics, 2019 Oct;37(10):1277-1286.
PMID: 31243736 DOI: 10.1007/s40273-019-00820-6

BACKGROUND: Using non-statin lipid-modifying agents in combination with statin therapy provides additional benefits for cardiovascular disease (CVD) risk reduction, but their value for money has only been evaluated in high-income countries (HICs). Furthermore, studies mainly derive effectiveness data from a single trial or older meta-analyses.
OBJECTIVES: Our study used data from the most recent network meta-analysis (NMA) and local parameters to assess the cost effectiveness of non-statin agents in statin-treated patients with a history of CVD.
METHODS: A published Markov model was adopted to investigate lifetime outcomes: (1) number of recurrent CVD events prevented, (2) quality-adjusted life-years (QALYs) gained, (3) costs and (4) incremental cost-effectiveness ratios (ICERs) of proprotein convertase subtilisin/kexin type 9 inhibitors (PCSK9i) and ezetimibe added to statin therapy. Event rates and effectiveness inputs were obtained from the NMA. Cost and utility data were gathered from published studies conducted in Thailand. A series of sensitivity analyses were performed.
RESULTS: Patients receiving PCSK9i and ezetimibe experienced fewer recurrent CVD events (number needed to treat [NNT] 17 and 30) and more QALYs (0.168 and 0.096 QALYs gained per person). However, under the societal perspective and at current acquisition costs in 2018, ICERs of both agents were $US1,223,995 and 27,361 per QALY gained, respectively. Based on threshold analyses, the costs need to be reduced by 97 and 85%, respectively, for PCSK9i and ezetimibe to be cost-effective.
CONCLUSIONS: Despite the proven effectiveness of PCSK9i and ezetimibe, the costs of these agents need to reduce to a much greater extent than in HICs to be cost-effective in Thailand.

Matched MeSH terms: Subtilisins
Fulltext Degree of hydrolysis and free tryptophan content of Skipjack Tuna (Katsuwonus pelamis) protein hydrolysates produced with different type of industrial proteases

Herpandi, Huda, N., Rosma, A., Wan Nadiah W. A.

International Food Research Journal, 2012;19(3):863-867.
MyJurnal

Protein-rich by-products from the canning industry, especially dark flesh of skipjack, have limited uses due to several factors such as darken color, susceptibility to oxidation and off flavour. Protein hydrolysates from skipjack dark flesh was produced with different type of industrial proteases (Alcalase®2.4L FG, Protamex®, Neutrase®1.5MG and Flavourzyme®500MG) for 60, 120, 180 and 240 min with level of proteases used of 0.5, 1, 1.5 and 2% per weight of raw material. The degree of hydrolysis and free tryptophan content of hydrolysate were investigated. The results shows longer time with higher concentration of enzyme has increased the degree of hydrolysis. Alcalase®2.4L FG had the highest degree of hydrolysis among all proteases followed by Protamex®, Flavourzyme®500MG and Neutrase® 1.5MG. All enzymes increase free tryptophan content linearly with the increament of protease enzyme level. The longer the hydrolysis time, the higher the content of free tryptophan produced.

Matched MeSH terms: Subtilisins
Fulltext Effects of Non-statin Lipid-Modifying Agents on Cardiovascular Morbidity and Mortality Among Statin-Treated Patients: A Systematic Review and Network Meta-Analysis

Chaiyasothi T, Nathisuwan S, Dilokthornsakul P, Vathesatogkit P, Thakkinstian A, Reid C, et al.

Front Pharmacol, 2019;10:547.
PMID: 31191304 DOI: 10.3389/fphar.2019.00547

Background: Currently, there is a lack of information on the comparative efficacy and safety of non-statin lipid-lowering agents (NST) in cardiovascular (CV) disease risk reduction when added to background statin therapy (ST). This study determine the relative treatment effects of NST on fatal and non-fatal CV events among statin-treated patients. Methods: A network meta-analysis based on a systematic review of randomized controlled trials (RCTs) comparing non-statin lipid-modifying agents among statin-treated patients was performed. PubMed, EMBASE, CENTRAL, and Clinicaltrial.gov were searched up to April 10, 2018. The primary outcomes were CV and all-cause mortalities. Secondary CV outcomes were coronary heart disease (CHD) death, non-fatal myocardial infarction (MI), any stroke, and coronary revascularization. Risks of discontinuations were secondary safety outcomes. Results: Sixty-seven RCTs including 259,429 participants with eight interventions were analyzed. No intervention had significant effects on the primary outcomes (CV mortality and all-cause mortality). For secondary endpoints, proprotein convertase subtilisin/kexin type 9 inhibitor (PCSK) plus statin (PCSK/ST) significantly reduced the risk of non-fatal MI (RR 0.82, 95% CI 0.72-0.93, p = 0.003), stroke (RR 0.74, 95% CI 0.65-0.85, p < 0.001), coronary revascularization (RR 0.84, 95% CI 0.75-0.94, p = 0.003) compared to ST. Combinations of ST and all NST except PCSK and ezetimibe showed higher rate of discontinuation due to adverse events compared to ST. Conclusions: None of NST significantly reduced CV or all-cause death when added to ST. PCSKs and to a lesser extent, ezetimibe may help reduce cardiovascular events with acceptable tolerability profile among broad range of patients.

Matched MeSH terms: Subtilisins
Fulltext Effects of degree of hydrolysis on physicochemical properties of cobia (Rachycentron canadum) frame hydrolysate

Amiza, M.A., Kong, Y.L., Faazaz, A.L.

International Food Research Journal, 2012;19(1):199-206.
MyJurnal

The effect of degree of hydrolysis (DH) on the physicochemical properties of cobia frame hydrolysate was determined. Three levels of degree of hydrolysis of cobia frame hydrolysate were studied, which were 53%, 71% and 96%. After enzymatic hydrolysis using Alcalase®, the samples were spray-dried. Cobia hydrolysate powder samples were analyzed for their proximate analysis and physicochemical properties. The proximate analysis showed significant differences in fat and ash content only. DH96 hydrolysate showed desirable essential amino acid profile for human requirement except for methionine and isoleucine. The study found that cobia frame hydrolysate had good colour, emulsifying capacity and excellent foaming properties. However, there were no significant differences in water-holding capacity, oil-holding capacity and peptide solubility among the hydrolysate samples. This study suggested that cobia frame hydrolysate is a potential ingredient and foaming agent for food industry.

Matched MeSH terms: Subtilisins
Enzymatic hydrolysis: Sialylated mucin (SiaMuc) glycoprotein of edible swiftlet's nest (ESN) and its molecular weight distribution as bioactive ESN SiaMuc-glycopeptide hydrolysate

Hui Yan T, Lim SJ, Babji AS, Rawi MH, Sarbini SR

Int J Biol Macromol, 2021 Apr 01;175:422-431.
PMID: 33561458 DOI: 10.1016/j.ijbiomac.2021.02.007

Bioactive edible swiftlet's nest (ESN) sialylated-mucin (SiaMuc) hydrolysate is produced by alcalase hydrolysis. Enzymatic hydrolysis of ESN breakdown high-valued ESN SiaMuc-glycoprotein into bioactive SiaMuc-glycopeptide. This is a breakthrough for the issue of insolubility and low extraction rate in ESN, and even increases the bioavailability of ESN nutritional functionality and health benefits. Hydrolysis of ESN SiaMuc-glycoprotein was performed for 1 to 4 h and its effect on physicochemical properties, molecular weight (MW) distribution, SiaMuc-glycoprotein and glycopeptide integrity were determined. Other than improvement in solubility and bioavailability as SiaMuc-glycopeptide, results from SDS-PAGE revealed that MW of SiaMuc-glycoprotein decreased from 42.0-148.8 kDa to 17.7-142.7 kDa with increasing hydrolysis period. Further hydrolysis from maximized DH (90 min) showed an insignificant effect on the MW of ESN SiaMuc-glycopeptide and remained constant at 15.2 kDa. This highlights that enzymatic hydrolysis only influences macro SiaMuc-glycoprotein fractions (142.7, 115.3 and 102.7 kDa), while the majority of SiaMuc-glycopeptide fractions from 36.6-98.6 kDa remained intact. Conclusively, alcalase hydrolysis of ESN showed high recovery in the form of bioactive ESN SiaMuc-glycopeptide. Therefore, enzymatic biotechnology is an economic alternative applicable on ESN that broaden industrial utilization by reducing the MW without destroying the quality of bioactive SiaMuc-glycoprotein.

Matched MeSH terms: Subtilisins
Fulltext Enzymatic preparation of palm kernel expeller protein hydrolysate (PKEPH)

Ng, K.L., Mohd Khan, A.

International Food Research Journal, 2012;19(2):721-725.
MyJurnal

Utilization of palm kernel expeller (PKE), a palm oil milling by-product, may be diversified through the exploitation of its protein component. The PKE protein could be effectively extracted using an alkaline
solution and followed by enzymatic hydrolysis to produce PKE protein hydrolysates or crude PKE peptide. The extraction of PKE protein was successfully carried out using an alkaline solution at pH11, at ratio of 1:10 (g/ml), PKE powder to alkaline solution with continuous shaking, 150 rpm, in a water bath operating at 50°C for 30 min. The extracted protein powder (PKEP) had 68.50±3.08% crude protein, 0.54±0.03% fat and 0.73±0.02% ash. The freeze-dried PKEP was re-suspend in particular buffer and hydrolyzed with proteolytic enzymes (Alcalase® 2.4L, Flavourzyme® 500MG, pepsin or trypsin) to obtain PKEP hydrolysate (PKEPH). The effect of enzyme concentration (0, 2, 4, 6, 8 & 10%) and time of hydrolysis (0, 6, 12, 24, 48 h) was studied to determine the most efficient hydrolytic conditions. Results showed that all enzymes tested were capable of hydrolyzing the PKEP and producing hydrolysates with different degree of hydrolysis (DH%). At 8.0% concentration, Alcalase®2.4L hydrolyzed PKEP into the highest DH (75.96%) hydrolysate (PKEPH) after 1h hydrolysis. Although only with 2.0% Alcalase 2.4 L concentration, it was sufficient to produce PKEP hydrolysate of 81.35% DH %, but it required 12 h to hydrolyze the protein. Pepsin was relatively the least efficient protease to hydrolyze the PKEP.

Matched MeSH terms: Subtilisins
Fulltext Enzyme Hydrolysates from Stichopus horrens as a New Source for Angiotensin-Converting Enzyme Inhibitory Peptides

Forghani B, Ebrahimpour A, Bakar J, Abdul Hamid A, Hassan Z, Saari N

Evid Based Complement Alternat Med, 2012;2012:236384.
PMID: 22927875 DOI: 10.1155/2012/236384

Stichopus horrens flesh was explored as a potential source for generating peptides with angiotensin-converting enzyme (ACE) inhibitory capacity using 6 proteases, namely alcalase, flavourzyme, trypsin, papain, bromelain, and protamex. Degree of hydrolysis (DH) and peptide profiling (SDS-PAGE) of Stichopus horrens hydrolysates (SHHs) was also assessed. Alcalase hydrolysate showed the highest DH value (39.8%) followed by flavourzyme hydrolysate (32.7%). Overall, alcalase hydrolysate exhibited the highest ACE inhibitory activity (IC(50) value of 0.41 mg/mL) followed by flavourzyme hydrolysate (IC(50) value of 2.24 mg/mL), trypsin hydrolysate (IC(50) value of 2.28 mg/mL), papain hydrolysate (IC(50) value of 2.48 mg/mL), bromelain hydrolysate (IC(50) value of 4.21 mg/mL), and protamex hydrolysate (IC(50) value of 6.38 mg/mL). The SDS-PAGE results showed that alcalase hydrolysate represented a unique pattern compared to others, which yielded potent ACE inhibitory peptides with molecular weight distribution lower than 20 kDa. The evaluation of the relationship between DH and IC(50) values of alcalase and flavourzyme hydrolysates revealed that the trend between those parameters was related to the type of the protease used. We concluded that the tested SHHs would be used as a potential source of functional ACE inhibitory peptides for physiological benefits.

Matched MeSH terms: Subtilisins
Fruit-specific expression of papaya subtilase gene

Othman R, Nuraziyan A

J Plant Physiol, 2010 Jan 15;167(2):131-7.
PMID: 19729222 DOI: 10.1016/j.jplph.2009.07.015

Subtilisin-like serine proteases (EC 3.4.21) consist of a widespread family of enzymes that is involved in various processes including in plants. The full-length cDNA (CpSUB1) and the corresponding genomic DNA for papaya subtilase have been obtained using rapid amplification of cDNA ends (RACEs) and PCR primer walking techniques, respectively. The cDNA clone contains an open reading frame of 2316bp encoding 772 amino acids with a calculated molecular mass of 82.6kDa and an isoelectric point (pI) of 8.97. The CpSUB1 gene is composed of nine exons and eight introns. The amino acid sequence encoded by CpSUB1 shared high identity (>60%) with the amino acid sequence of other plant subtilisin-like proteases. Sequence analysis of CpSUB1 revealed the presence of a possible signal peptide (25 amino acid residues) and an NH(2)-terminal prosequence (88 amino acid residues). In addition, papaya subtilase possesses the characteristic subtilisin catalytic triad amino acids namely Asp, His and Ser, together with the substrate-binding site, Asn. DNA hybridization analysis showed that subtilase gene exists as a single copy in the papaya genome. RNA hybridization analyses showed that expression of the subtilase transcripts was only detected in mesocarp but not in non-fruit tissues. Gene expression in fruit tissues reached the highest level during the ripening stage at which the fruits undergo dramatic softening process. Subsequently, pro-subtilase ( approximately 80kDa) was expressed as recombinant pro-enzyme ( approximately 97kDa), which was used to generate antiserum against papaya subtilase, anti-sub. Protein gel blot analysis using anti-sub towards total protein extracted from all ripening stages revealed that a protein with a molecular mass of approximately 70kDa reacted with the antiserum. Hence both RNA hybridization and protein gel blot analyses confirmed the presence of subtilase during papaya fruit ripening, pointing to its possible involvement in this important process.

Matched MeSH terms: Subtilisins/genetics; Subtilisins/metabolism*
Fulltext Functional and antioxidant properties of angelwing clam (Pholas orientalis) hydrolysate produced using alcalase

Normah Ismail, Juliana Mahmod, Awatif Khairul Fatihin Mustafa Kamal

Scientific Research Journal, 2014;11(1):0-0.
MyJurnal

In this study, Hydrolysate from angelwing clam (Pholas orientalis) was produced at 0, 1, 2 and 3 hrs and E/S ratio of 0.5 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

Matched MeSH terms: Subtilisins
Generation, Fractionation, and Characterization of Iron-Chelating Protein Hydrolysate from Palm Kernel Cake Proteins

Zarei M, Ghanbari R, Tajabadi N, Abdul-Hamid A, Bakar FA, Saari N

J Food Sci, 2016 Feb;81(2):C341-7.
PMID: 26720491 DOI: 10.1111/1750-3841.13200

Palm kernel cake protein was hydrolyzed with different proteases namely papain, bromelain, subtilisin, flavourzyme, trypsin, chymotrypsin, and pepsin to generate different protein hydrolysates. Peptide content and iron-chelating activity of each hydrolysate were evaluated using O-phthaldialdehyde-based spectrophotometric method and ferrozine-based colorimetric assay, respectively. The results revealed a positive correlation between peptide contents and iron-chelating activities of the protein hydrolysates. Protein hydrolysate generated by papain exhibited the highest peptide content of 10.5 mM and highest iron-chelating activity of 64.8% compared with the other hydrolysates. Profiling of the papain-generated hydrolysate by reverse phase high performance liquid chromatography fractionation indicated a direct association between peptide content and iron-chelating activity in most of the fractions. Further fractionation using isoelectric focusing also revealed that protein hydrolysate with basic and neutral isoelectric point (pI) had the highest iron-chelating activity, although a few fractions in the acidic range also exhibited good metal chelating potential. After identification and synthesis of papain-generated peptides, GGIF and YLLLK showed among the highest iron-chelating activities of 56% and 53%, whereas their IC50 were 1.4 and 0.2 μM, respectively.

Matched MeSH terms: Subtilisins/metabolism
Fulltext Genetic researches among malaysian familial hypercholesterolaemic population

Al-Khateeb, A, Al-Talib, H

JUMMEC, 2016;19(2):1-11.
MyJurnal

Background:
Familial hypercholesterolaemia (FH) is one of the most frequent inherited metabolic disorders that can lead
to a risk of premature cardiovascular disease. Publications on FH are mainly from western patients as there is
little research on Asians, including Malaysians. The aim of this review is to provide an up-to- date information
on Malaysian studies on FH genotyping and its relation to the phenotype of the affected patients.
Method:
A search was conducted for data from online databases on FH in Malaysia.
Results:
The mutation spectrum for FH among Malaysian patients was extremely broad. The gene variants were located
mainly in the low-density lipoprotein receptor (LDLR) and apolipoprotein B-100 (APOB-100) genes rather than
in the proprotein convertase subtilisin kexin type 9 (PCSK9) gene. The exon 9 and 14 were the hotspots in the
LDLR gene. The most frequent mutation was p.Cys255Ser, at 12.5%, followed by p.Arg471Gly, at 11%, and the
most common single nucleotide polymorphism (SNP) was c.1060+7 T>C at 11.7%. The LDLR gene variants were
more common compared to the APOB-100 gene variants, while variants in the PCSK9 gene were very few.
Phenotype-genotype associations were identified. Subjects with LDLR and APOB-100 genes mutations had a
higher frequency of cardiovascular disease, a family history of hyperlipidaemia and tendon xanthoma and a
higher low-density lipoprotein cholesterol (LDL-C) level than non-carriers.
Conclusion:
Research on Malaysian familial hypercholesterolaemic patients by individual groups is encouraging. However,
more extensive molecular studies on FH on a national scale, with a screening of the disease-causing mutations
together with a comprehensive genotype-phenotype association study, can lead to a better outcome for
patients with the disease.

Matched MeSH terms: Subtilisins
High angiotensin-I converting enzyme (ACE) inhibitory activity of Alcalase-digested green soybean (Glycine max) hydrolysates

Hanafi MA, Hashim SN, Chay SY, Ebrahimpour A, Zarei M, Muhammad K, et al.

Food Res Int, 2018 04;106:589-597.
PMID: 29579964 DOI: 10.1016/j.foodres.2018.01.030

As a protein-rich, underutilized crop, green soybean could be exploited to produce hydrolysates containing angiotensin-I converting enzyme (ACE) inhibitory peptides. Defatted green soybean was hydrolyzed using four different food-grade proteases (Alcalase, Papain, Flavourzyme and Bromelain) and their ACE inhibitory activities were evaluated. The Alcalase-generated green soybean hydrolysate showed the highest ACE inhibitory activity (IC50: 0.14 mg/mL at 6 h hydrolysis time) followed by Papain (IC50: 0.20 mg/mL at 5 h hydrolysis time), Bromelain (IC50: 0.36 mg/mL at 6 h hydrolysis time) and Flavourzyme (IC50: 1.14 mg/mL at 6 h hydrolysis time) hydrolysates. The Alcalase-generated hydrolysate was profiled based on its hydrophobicity and isoelectric point using reversed phase high performance liquid chromatography (RP-HPLC) and isoelectric point focusing (IEF) fractionators. The Alcalase-generated green soybean hydrolysate comprising of peptides EAQRLLF, PSLRSYLAE, PDRSIHGRQLAE, FITAFR and RGQVLS, revealed the highest ACE inhibitory activity of 94.19%, 99.31%, 92.92%, 101.51% and 90.40%, respectively, while their IC50 values were 878 μM, 532 μM, 1552 μM, 1342 μM and 993 μM, respectively. It can be concluded that Alcalase-digested green soybean hydrolysates could be exploited as a source of peptides to be incorporated into functional foods with antihypertensive activity.

Matched MeSH terms: Subtilisins/chemistry*
Identification and molecular docking study of novel cholesterol esterase inhibitory peptides from camel milk proteins

Mudgil P, Baby B, Ngoh YY, Vijayan R, Gan CY, Maqsood S

J Dairy Sci, 2019 Dec;102(12):10748-10759.
PMID: 31548068 DOI: 10.3168/jds.2019-16520

Novel bioactive peptides from camel milk protein hydrolysates (CMPH) were identified and tested for inhibition of cholesterol esterase (CEase), and their possible binding mechanisms were elucidated by molecular docking. Papain-generated CMPH showed the highest degree of hydrolysis. All CMPH produced upon enzymatic degradation demonstrated a dramatic enhancement of CEase inhibition compared with intact camel milk proteins, with papain-generated hydrolysate P9 displaying the highest inhibition. Peptide identification and their modeling through PepSite 2 revealed that among 20 potential bioactive peptides in alcalase-generated hydrolysate A9, only 3 peptides, with sequences KFQWGY, SQDWSFY, and YWYPPQ, showed the highest binding toward CEase catalytic sites. Among 43 peptides in 9-h papain-generated hydrolysate P9, 4 peptides were found to be potent CEase inhibitors. Molecular docking revealed that WPMLQPKVM, CLSPLQMR, MYQQWKFL, and CLSPLQFR from P9 hydrolysates were able to bind to the active site of CEase with good docking scores and molecular mechanics-generalized born surface area binding energies. Overall, this is the first study reporting CEase inhibitory potential of peptides generated from milk proteins.

Matched MeSH terms: Subtilisins/chemistry

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