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Tzuming Pan - One of the best experts on this subject based on the ideXlab platform.
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Monascus purpureus ntu 568 fermented product improves memory and learning ability in rats with aluminium induced alzheimer s disease
Journal of Functional Foods, 2016Co-Authors: Chienli Chen, Kuangyao Chang, Tzuming PanAbstract:Abstract Oxidative stress and neuroinflammation induced by accumulation of amyloid β (Aβ) and phosphorylated tau protein (p-tau) are the main causes of Alzheimer's disease (AD). We examined the effects of Monascus purpureus NTU 568 fermented product (ANKASCIN 568 plus) in the model of Sprague–Dawley rats via oral garage to induce AD pathology which received aluminium chloride on a daily basis. ANKASCIN 568 plus mitigated cognitive impairment in behavioural tests, reduced oxidative stress in the brain, reversed aluminium-induced AD brain pathology including accumulation of Aβ, p-tau, and amyloid precursor protein; elevated acetylcholinesterase activity, and altered biomarker levels in the cerebrospinal fluid. ANKASCIN 568 plus showed a significant improvement relative to Aricept, an approved drug for AD, in several parameters. Thus, by suppressing free radical generation and activating antioxidant enzymes, ANKASCIN 568 plus can reduce oxidative stress and ameliorate AD pathology, thus protecting rats against aluminium-induced memory and learning deficits.
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induction of apoptosis in human breast adenocarcinoma cells mcf 7 by monapurpyridine a a new azaphilone derivative from Monascus purpureus ntu 568
Molecules, 2012Co-Authors: Lichuan Hsu, Yawen Hsu, Yuhan Liang, Yaohaur Kuo, Chiaching Liaw, Tzuming PanAbstract:A new azaphilonidal derivative, monapurpyridine A (MPA), has recently been isolated from the fermented products of Monascus purpureus NTU 568. The structure of MPA was elucidated by nuclear magnetic resonance (1H-NMR, 13C-NMR, COSY, HMQC, and HMBC) and other spectroscopic analyses. Biological evaluation revealed that MPA could induce cell death in human breast adenocarcinoma cells MCF-7, and it has no significant toxicity to normal mammary epithelial cells M10. The MTT assay and flow cytometric analysis were employed to investigate cell viability and cell cycle influenced by MPA. Moreover, we used Western blot and caspase activity assay to demonstrate the activation of caspase-3, -8 and -9 resulted from MPA. All evidence supported that MPA was suitable for developing into a chemotherapeutic or chemopreventive agent against breast cancer.
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anti tumor and anti inflammatory properties of ankaflavin and monaphilone a from Monascus purpureus ntu 568
Journal of Agricultural and Food Chemistry, 2011Co-Authors: Lichuan Hsu, Yawen Hsu, Yuhan Liang, Yaohaur Kuo, Tzuming PanAbstract:An azaphilonidal derivative monaphilone A (MA) was recently isolated from the fermented products of Monascus purpureus NTU 568 by our laboratory. We report here the exploration of apoptosis-related and anti-inflammatory properties of MA and ankaflavin (AK) by some experiments about inducing death of human laryngeal carcinoma cell line HEp-2 and reducing inflammatory responses on murine macrophage RAW 264.7 cells. We employed a ssDNA enzyme-linked immunosorbent assay (ELISA) kit to investigate the nuclear changes of early apoptosis induced by AK and MA on HEp-2 cells and used a western blot and an enzyme activity assay to demonstrate the activation of caspase-3, caspase-8, and caspase-9 by MA and AK. Our studies revealed that AK and MA may decrease lipopolysaccharide (LPS)-induced inflammatory responses, including nitrite productions and expressions of inducible nitric oxide synthase (iNOS) and cyclooxygenase 2 (COX-2) in RAW 264.7 cells. All evidence support that azaphilonidal derivatives from M. purpureus NTU 568, such as AK and MA, are suitable for the development of chemotherapy or chemopreventive agents.
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monaphilones a c three new antiproliferative azaphilone derivatives from Monascus purpureus ntu 568
Journal of Agricultural and Food Chemistry, 2010Co-Authors: Yawen Hsu, Lichuan Hsu, Yuhan Liang, Yaohaur Kuo, Tzuming PanAbstract:Monascus purpureus NTU 568 was a mutant strain from M. purpureus HM105. The methanol extract of red mold rice fermented by this strain exhibited four major yellow pigment signals on HPLC profile. By repeated chemical chromatography methods, three new azaphilone derivatives, namely, monaphilone A (1), B (2) and C (3), along with the known pigments ankaflavin (4) and monascin (5), were isolated and characterized. Based on spectroscopic analyses, mainly 1D and 2D NMR data, the structures of compounds 1-3 were completely elucidated; in addition, 1-3 were determined to be new azaphilone structures, due to the decrease of carbon monoxide for producing a gamma-lactone ring, compared with other azaphilone derivatives. Biological evaluations showed that monaphilone A (1) and B (2) exhibited an antiproliferative effect against HEp-2 (human laryngeal carcinoma cell line) and WiDr (human colon adenocarcinoma cell line), and none of the five compounds had toxicity to normal human lung cell lines (WI-38 and MRC-5) at 70 muM.
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anti diabetic effects of Monascus purpureus ntu 568 fermented products on streptozotocin induced diabetic rats
Journal of Agricultural and Food Chemistry, 2010Co-Authors: Yeuching Shi, Tzuming PanAbstract:Red-mold-fermented products have the unique ability to economically produce many secondary metabolites and are known to improve blood circulation. Diabetes mellitus is a chronic disease that is characterized by hyperglycemia caused by insufficient insulin action. In the current study, we examine the effect of Monascus purpureus NTU 568 fermented products on fasting blood glucose and oral glucose tolerance testing (OGTT) in streptozotocin-induced diabetic rats. After 8 weeks of being fed with red-mold-fermented products at a dose of 200 mg/kg, the experimental results indicate that oral administration of red-mold-fermented products can delay the development of the plasma glucose level in rats. A significant reduction was found in urine sugar and urine protein levels. The study scientifically validates the widely claimed use of red-mold-fermented products as an ethnomedicine to treat diabetes mellitus.
Masaaki Yasuda - One of the best experts on this subject based on the ideXlab platform.
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application of an acid proteinase from Monascus purpureus to reduce antigenicity of bovine milk whey protein
Journal of Industrial Microbiology & Biotechnology, 2011Co-Authors: P Nilantha L Lakshman, Shinjiro Tachibana, Hirohide Toyama, Toki Taira, Toshihiko Suganuma, Worapot Suntornsuk, Masaaki YasudaAbstract:An acid proteinase from Monascus purpureus No. 3403, MpuAP, was previously purified and some characterized in our laboratory (Agric Biol Chem 48:1637–1639, 1984). However, further information about this enzyme is lacking. In this study, we investigated MpuAP’s comprehensive substrate specificity, storage stability, and prospects for reducing antigenicity of whey proteins for application in the food industry. MpuAP hydrolyzed primarily five peptide bonds, Gln4–His5, His10–Leu11, Ala14–Leu15, Gly23–Phe24 and Phe24–Phe25 in the oxidized insulin B-chain. The lyophilized form of the enzyme was well preserved at 30–40°C for 7 days without stabilizers. To investigate the possibility of reducing the antigenicity of the milk whey protein, enzymatic hydrolysates of the whey protein were evaluated by inhibition ELISA. Out of the three main components of whey protein, casein and α-lactalbumin were efficiently degraded by MpuAP. The sequential reaction of MpuAP and trypsin against the whey protein successfully degraded casein, α-lactalbumin and β-lactoglobulin with the highest degree of hydrolysis. As a result, the hydrolysates obtained by using the MpuAP–trypsin combination showed the lowest antigenicity compared with the single application of pepsin, trypsin or pepsin–trypsin combination. Therefore, the overall result suggested that the storage-stable MpuAP and trypsin combination will be a productive approach for making hypoallergic bovine milk whey protein hydrolysates.
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angiotensin i converting enzyme inhibitory peptides in red mold rice made by Monascus purpureus
Process Biochemistry, 2009Co-Authors: Megumi Kuba, Kumi Tanaka, Masayasu Sesoko, Fumihide Inoue, Masaaki YasudaAbstract:Abstract The ACE inhibitory activity in red-mold rice extracts, prepared from 24 strains of the genus Monascus , was measured. The most effective strain for ACE inhibition was Monascus purpureus IFO 4489 (IC 50 = 0.71 mg/ml). Although the antihypertensive substance γ-amino butyric acid was detected in the red-mold rice (85.2 mg/kg), it did not contribute to ACE inhibition. Four ACE inhibitory peptides were isolated from the extract and identified as Ile-Tyr (IC 50 = 4.0 μM), Val-Val-Tyr (22.0 μM), Val-Phe (49.7 μM) and Val-Trp (3.1 μM) by protein sequencing. The ACE inhibitory activity of these peptides was almost completely preserved after successive in vitro digestion by pepsin, chymotrypsin and trypsin. These results suggest that red-mold rice made by M. purpureus could be useful in alleviating hypertension.
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purification and characterization of heterogeneous glucoamylases from Monascus purpureus
Bioscience Biotechnology and Biochemistry, 2007Co-Authors: Shinjiro Tachibana, Masaaki YasudaAbstract:Two forms of an extracellular glucoamylase, MpuGA-I and MpuGA-II, were purified to homogeneity from Monascus purpureus RY3410. The molecular weights of these enzymes were estimated to be 60,000 (MpuGA-I) and 89,000 (MpuGA-II). These enzymes were glycoproteins with a carbohydrate content of 15.0% (MpuGA-I) and 16.2% (MpuGA-II) respectively. The pH optima were 5.0 for both enzymes, and the optimal temperatures were 50 °C (MpuGA-I) and 65 °C (MpuGA-II). The K m values for soluble starch were calculated to be 4.0±0.8 mg/ml (MpuGA-I) and 1.1±0.2 mg/ml (MpuGA-II) respectively.
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production of angiotensin i converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase
Process Biochemistry, 2005Co-Authors: Megumi Kuba, C Tana, Shinkichi Tawata, Masaaki YasudaAbstract:Abstract Soybean proteins, β-conglycinin and glycinin were hydrolysed by an acid proteinase from Monascus purpureus . The degree of hydrolysis and inhibitory activities of angiotensin I-converting enzyme (ACE) increased with increasing proteolysis time. After 10 h of incubation, the IC 50 values of the β-conglycinin and glycinin hydrolysates were determined as 0.126 mg/ml and 0.148 mg/ml, respectively. Four ACE inhibitory peptides were isolated from the soybean protein hydrolysates and identified by protein sequencer. ACE inhibitory peptides isolated from the β-conglycinin hydrolysate were identified as LAIPVNKP (IC 50 = 70 μM) and LPHF (670 μM), and those from the glycinin hydrolysate as SPYP (850 μM) and WL (65 μM). The inhibitory activity of SPYP markedly increased after successive digestion by pepsin, chymotrypsin and trypsin in vitro.
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Purification and characterization of a new type of serine carboxypeptidase from Monascus purpureus
Journal of Industrial Microbiology and Biotechnology, 2004Co-Authors: Fang Liu, Masanobu Ishihara, Shinjiro Tachibana, Toki Taira, Masaaki YasudaAbstract:Carboxypeptidase produced by Monascus purpureus IFO 4478 was purified to homogeneity. The purified enzyme is a heterodimer with a molecular mass of 132 kDa and consists of two subunits of 64 and 67 kDa. It is an acidic glycoprotein with an isoelectric point of 3.67 and 17.0% carbohydrate content. The optimum pH and temperature were 4.0 and 40 °C, respectively. The enzyme was stable between pH 2.0 and 8.0 at 37 °C for 1 h, and up to 50 °C at pH 5.0 for 15 min. The enzyme was strongly inhibited by piperastatin A, diisopropylfluoride phosphate (DFP), phenylmethylsulfonylfluoride (PMSF), and chymostatin, suggesting that it is a chymotrypsin-like serine carboxypeptidase. Monascus purpureus carboxypeptidase was also strongly inhibited by p -chloromercuribenzoic acid (PCMB) but not by ethylenediaminetetraacetic acid (EDTA) and 1,10-phenanthroline, indicating that it requires cysteine residue but not metal ions for activity. Benzyloxycarbonyl- l -tyrosyl- l -glutamic acid (Z-Tyr-Glu), among the substrates tested, was the best substrate of the enzyme. The K _m, V _max, K _cat, and K _cat /K _m values of the enzyme for Z-Tyr-Glu at pH 4.0 and 37 °C were 0.86 mM, 0.917 mM min^−1, 291 s^−1, and 339 mM^−1 s^−1, respectively.
Bibhu Prasad Panda - One of the best experts on this subject based on the ideXlab platform.
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production of angkak through co culture of Monascus purpureus and Monascus ruber
Brazilian Journal of Microbiology, 2010Co-Authors: Bibhu Prasad Panda, Saleem Javed, M T AliAbstract:Angkak (red mold rice, red yeast rice, Chinese red rice) is a traditional Chinese medicine produced by solid-state fermentation of cooked non-glutinous rice with Monascus species. The secondary metabolite of Monascus species, monacolin K /lovastatin, has been proven to lower blood lipid levels. In this study, a co-culture of Monascus purpureus MTCC 369 and Monascus ruber MTCC 1880 was used for angkak production. Four medium parameters screened by Plackett-Burman design were optimized by response surface methodology for highest lovastatin production in angkak during solid-state fermentation by the co-culture. Maximum lovastatin production of 2.84 mg g-1 was predicted in solid medium containing 20 g rice and 40 ml liquid nutrients medium (malt extract 9.68 g l-1, dextrose 38.90 g l-1, MnSO4.H2O 1.96 g l-1, and MgSO4.7H2O 0.730 g l-1) by point prediction tool of Design Expert 7.1 software (Statease Inc. USA).
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optimization of fermentation parameters for higher lovastatin production in red mold rice through co culture of Monascus purpureus and Monascus ruber
Food and Bioprocess Technology, 2010Co-Authors: Bibhu Prasad Panda, Saleem Javed, Mohammad AliAbstract:Monascus, fermented rice (red mold rice), has been found to reduce the serum total cholesterol and triglyceride due to presence of lovastatin. Lovastatin acts as an inhibitor of 3-hydroxy-3-methyl glutaryl coenzyme A reductase. Coculture of Monascus purpureus MTCC 369 and Monascus ruber MTCC 1880 was used to produce red mold rice by solid-state fermentation. Optimization of different fermentation process parameters such as temperature, fermentation time, inoculum volume, and pH of the solid medium was carried out by Box–Behnken’s factorial design of response surface methodology to maximize lovastatin concentration in red mold rice. Maximum lovastatin production of 2.83 mg/g was predicted at 14th day in solid medium under optimized process condition.
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statistical analysis and validation of process parameters influencing lovastatin production by Monascus purpureus mtcc 369 under solid state fermentation
Biotechnology and Bioprocess Engineering, 2009Co-Authors: Bibhu Prasad Panda, Saleem Javed, M T AliAbstract:Monascus, a fermented rice (red mold rice), was found to reduce total cholesterol and triglyceride in serum due to the presence of lovastatin, a 3-hydroxy-3-methyl glutaryl coenzyme A (HMG-CoA) reductase inhibitor. Optimization and validation of different process parameters such as temperature, fermentation time, inoculum volume, and pH of the solid medium was done using Box-Behnken’s factorial design of response surface method for maximum production of lovastatin by Monascus purpureus MTCC 369. A maximum lovastatin production of 3.422 mg/g was predicted by day 14.43 of fermentation in a rice based solid medium of pH 6 when fermented at a temperature of 29.46°C, an inoculum volume of 5.11 mL, and using response surface plots and the point prediction tool of Design Expert 7.1.3 (Statease Inc., USA) software.
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optimization of nutrient parameters for lovastatin production by Monascus purpureus mtcc 369 under submerged fermentation using response surface methodology
Applied Microbiology and Biotechnology, 2007Co-Authors: Sadik Ali Sayyad, Bibhu Prasad Panda, Saleem Javed, Mohd AliAbstract:Lovastatin, an inhibitor of HMG-CoA reductase, was produced by submerged fermentation using Monascus purpureus MTCC 369. Five nutritional parameters screened using Plackett–Burman experimental design were optimized by Box–Behnken factorial design of response surface methodology for lovastatin production in shake flask cultures. Maximum lovastatin production of 351 mg/l were predicted in medium containing 29.59 g/l dextrose, 3.86 g/l NH4Cl, 1.73 g/l KH2PO4, 0.86 g/l MgSO4·7H2O, and 0.19 g/l MnSO4·H2O using response surface plots and point prediction tool of DESIGN EXPERT 7.0 (Statease, USA) software.
Sanlang Wang - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of a protease extracellularly produced by Monascus purpureus ccrc31499 in a shrimp and crab shell powder medium
Enzyme and Microbial Technology, 2006Co-Authors: Tzu Wen Liang, Jane Jean Lin, Yuehorng Yen, Chuan Lu Wang, Sanlang WangAbstract:Abstract Monascus purpureus CCRC31499 produced a protease when it was grown in a medium containing shrimp and crab shell powder (SCSP) of marine wastes. An extracellular protease was purified from the culture supernatant to homology. The protease had a molecular weight of 40,000 and a pI of 7.9. The optimal pH, optimum temperature, pH stability, and thermal stability of the protease were pH 7–9, 40 °C, pH 5–9, and 40 °C, respectively. In addition to protease activity, CCRC31499 also exhibited activity of enhancing vegetable growth in culture supernatant. This is also the first report of isolation of a protease from Monascus species.
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purification and characterization of an antimicrobial chitinase extracellularly produced by Monascus purpureus ccrc31499 in a shrimp and crab shell powder medium
Journal of Agricultural and Food Chemistry, 2002Co-Authors: Sanlang Wang, Weijen Hsiao, Wenteish ChangAbstract:Monascus purpureus CCRC31499 produced an antimicrobial chitinase when it was grown in a medium containing shrimp and crab shell powder (SCSP) of marine wastes. An extracellular antimicrobial chitinase was purified from the culture supernatant to homology. The chitinase had a molecular weight of approximately 81,000 and a pI of 5.4. The optimal pH, optimum temperature, and pH stability of the chitinase were pH 7, 40 degrees C, and pH 6-8, respectively. The activity of the chitinase was activated by Fe(2+) and strongly inhibited by Hg(2+). The unique characteristics of the purified chitinase include high molecular weight, nearly neutral optimum pH, protease activity, and antimicrobial activity with bacteria and fungal phytopathogens. This is also the first report of isolation of a chitinase from a Monascus species.
Megumi Kuba - One of the best experts on this subject based on the ideXlab platform.
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angiotensin i converting enzyme inhibitory peptides in red mold rice made by Monascus purpureus
Process Biochemistry, 2009Co-Authors: Megumi Kuba, Kumi Tanaka, Masayasu Sesoko, Fumihide Inoue, Masaaki YasudaAbstract:Abstract The ACE inhibitory activity in red-mold rice extracts, prepared from 24 strains of the genus Monascus , was measured. The most effective strain for ACE inhibition was Monascus purpureus IFO 4489 (IC 50 = 0.71 mg/ml). Although the antihypertensive substance γ-amino butyric acid was detected in the red-mold rice (85.2 mg/kg), it did not contribute to ACE inhibition. Four ACE inhibitory peptides were isolated from the extract and identified as Ile-Tyr (IC 50 = 4.0 μM), Val-Val-Tyr (22.0 μM), Val-Phe (49.7 μM) and Val-Trp (3.1 μM) by protein sequencing. The ACE inhibitory activity of these peptides was almost completely preserved after successive in vitro digestion by pepsin, chymotrypsin and trypsin. These results suggest that red-mold rice made by M. purpureus could be useful in alleviating hypertension.
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production of angiotensin i converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase
Process Biochemistry, 2005Co-Authors: Megumi Kuba, C Tana, Shinkichi Tawata, Masaaki YasudaAbstract:Abstract Soybean proteins, β-conglycinin and glycinin were hydrolysed by an acid proteinase from Monascus purpureus . The degree of hydrolysis and inhibitory activities of angiotensin I-converting enzyme (ACE) increased with increasing proteolysis time. After 10 h of incubation, the IC 50 values of the β-conglycinin and glycinin hydrolysates were determined as 0.126 mg/ml and 0.148 mg/ml, respectively. Four ACE inhibitory peptides were isolated from the soybean protein hydrolysates and identified by protein sequencer. ACE inhibitory peptides isolated from the β-conglycinin hydrolysate were identified as LAIPVNKP (IC 50 = 70 μM) and LPHF (670 μM), and those from the glycinin hydrolysate as SPYP (850 μM) and WL (65 μM). The inhibitory activity of SPYP markedly increased after successive digestion by pepsin, chymotrypsin and trypsin in vitro.