scholarly journals Purification and Characterization of Milk Clotting Enzyme from Edible Mushroom (Pleurotus florida)

2021 ◽  
Vol 11 (2) ◽  
pp. 3362-3373
Keyword(s):  
Specific Activity ◽  
Maximal Activity ◽  
Edible Mushroom ◽  
Size Exclusion ◽  
Oyster Mushroom ◽  
Edible Fungi ◽  
Pleurotus Florida ◽  
Milk Clotting ◽  
Milk Clotting Enzyme

Oyster mushroom (Pleurotus florida 14 MICC) is one of the most widely cultivated edible fungi in the world. Milk clotting enzyme (MCE) derived from the mold was developed as a calf rennet alternative; thus, it was purified and characterized, and its effect on different milk species was investigated. The highest MCE activity (75.49 SU/ml) was observed in mushroom fruit bodies dissolved in 0.2 M sodium acetate pH 5.0; as well as the highest total MCE activity (367.85 SU) was recorded at 20% of ammonium sulfate with a specific activity of 343.79 SU mg-1 protein while size exclusion column chromatography on Sephadex G-100 purified MCE 3.46-fold with 17.96% yield. Also, it could be capable of coagulating different milk species. Mushroom MCE exhibited their optimal activity at pH 5.0 for crude extract (CE) while at pH 6.0 for partial purified (PP) and purified (P) MCE fractions; as well as at 55 °C for CE and PP MCE fractions while 50 °C for P MCE. CaCl2 concentration (0.01%) recorded the maximal activity for CE while (0.04%) and (0.02%) for PP and P fractions, respectively. It could be concluded that MCE from Oyster mushroom may be a good candidate as a calf rennet substitute in cheese production.

Optimization of the production and characterization of milk-clotting enzyme from Bacillus subtilis isolated from marine sponge

2016 ◽  
Vol 15 (3) ◽  
pp. 158 ◽  
Author(s):  
HalaR Wehaidy ◽  
MohamedA Abdel-Naby ◽  
WafaaG Shousha ◽  
MohammedI.Y. El Mallah ◽  
MichaelM Shawky
Keyword(s):  
Bacillus Subtilis ◽  
Marine Sponge ◽  
Milk Clotting ◽  
Milk Clotting Enzyme

scholarly journals Purification and Biochemical Characterization of Alkaline Serine Protease from Caesalpinia bonducella

2010 ◽  
Vol 5 (6) ◽  
pp. 1934578X1000500
Author(s):  
Hidayatullah Khan ◽  
Irshad Ali ◽  
Arif-ullah Khan ◽  
Mushtaq Ahmed ◽  
Zamarud Shah ◽  
...  
Keyword(s):  
Serine Protease ◽  
Biochemical Characterization ◽  
Specific Activity ◽  
Sodium Dodecyl ◽  
Exchange Chromatography ◽  
Size Exclusion ◽  
Alkaline Serine Protease ◽  
Protease Enzyme ◽  
Caesalpinia Bonducella

A high molecular weight serine protease has been purified to electrophoretic homogeneity from the seeds of Caesalpinia bonducella Flem. (Caesalpiniaceae) by the combination of size exclusion and ion exchange chromatography. About 524 fold purification was achieved with an overall recovery of 6.8%. The specific activity was found to be 86 U/mg/min at pH 8.0. The calculated Km and Vmax were 1.66 mg/mL and 496.68 units/min per mg of protein, respectively. The molecular mass was estimated to be about 63 kDa by sodium dodecyl sulfate PAGE. The enzyme showed optimum activity at pH 8.0 and exhibited its highest activity at 40°C. The enzyme was strongly inhibited by 2mM phenylmethylsulfonyl fluoride (PMSF), suggesting the presence of a serine residue at the active site. PMSF showed a pure competitive type of inhibition with the serine protease enzyme. It was observed that enzyme activity was enhanced in the presence of dications and was active against a variety of modified substrates and natural proteins.

Production and characterization of a milk-clotting enzyme from Aspergillus oryzae MTCC 5341

2009 ◽  
Vol 85 (6) ◽  
pp. 1849-1859 ◽  
Author(s):  
Kurutahalli S. Vishwanatha ◽  
A. G. Appu Rao ◽  
Sridevi Annapurna Singh
Keyword(s):  
Aspergillus Oryzae ◽  
Milk Clotting ◽  
Milk Clotting Enzyme

scholarly journals Extracellular expression and characterization of an α-glucosidase from Oryza sativa and its transglycosylation for synthesis of 2-O-α-D-glucopyranosyl-L-ascorbic acid

2021 ◽  
Author(s):  
Xuelian Qi ◽  
Junlan Shao ◽  
Yinchu Cheng ◽  
Xiaoying He ◽  
Yan Li ◽  
...  
Keyword(s):  
Ascorbic Acid ◽  
Oryza Sativa ◽  
Pichia Pastoris ◽  
Specific Activity ◽  
Maximal Activity ◽  
Batch Cultivation ◽  
Glycoside Hydrolases ◽  
Glycosylation Reaction ◽  
Fed Batch Cultivation

Abstract: 2-O-α-D-Glucopyranosyl-L-ascorbic acid (AA-2G) is an important industrial derivative of L-ascorbic acid (AA), which has the distinct advantages of non-reducibility, antioxidation, and reproducible decomposition into L-ascorbic acid and glucose. Enzymatic synthesis is a preferred method for AA-2G production over alternative chemical synthesis owing to the regioselective glycosylation reaction. α-Glucosidase, an enzyme classed into O- glycoside hydrolases, may be used in glycosylation reactions to synthesize AA-2G. Here, one α-glucosidase from Oryza sativa (rAGL) was recombinantly produced in Pichia pastoris GS115 and used for biosynthesis of AA-2G with few intermediates and byproducts. The extracellular rAGL reached 9.11 U/mL after fed-batch cultivation for 102 h in a 5-L fermenter. The specific activity of purified rAGL is 49.83 U/mg at 37 °C and pH 4.0. The optimal temperature of rAGL was 65 °C, and it was stable below 55 °C. rAGL was active over the range of pH 3.0–7.0, with the maximal activity at pH 4.0. Under the condition of 37 °C , pH 4.0, equimolar maltose and AA·Na, 8.7±0.4 g/L of AA-2G was synthesized by rAGL. These studies lay the basis for the industrial application of recombinant α-glucosidase. Keywords: α-Glucosidase; Oryza sativa; 2-O-α-D-glucopyranosyl-L-ascorbic acid; Transglycosylation; Pichia pastoris

Production and characterization of milk-clotting enzyme from Bacillus amyloliquefaciens JNU002 by submerged fermentation

2011 ◽  
Vol 234 (3) ◽  
pp. 415-421 ◽  
Author(s):  
Zhongyang Ding ◽  
Wangfei Wang ◽  
Boda Wang ◽  
Anran Ouyang ◽  
Siwei Xiao ◽  
...  
Keyword(s):  
Submerged Fermentation ◽  
Bacillus Amyloliquefaciens ◽  
Milk Clotting ◽  
Milk Clotting Enzyme

Purification and partial characterization of milk-clotting enzyme extracted from glutinous rice wine mash liquor

2009 ◽  
Vol 26 (5) ◽  
pp. 1313-1318 ◽  
Author(s):  
Yanping Wang ◽  
Qiaoling Cheng ◽  
Zaheer Ahmed ◽  
Xiaoxue Jiang ◽  
Xiaojia Bai
Keyword(s):  
Partial Characterization ◽  
Rice Wine ◽  
Milk Clotting ◽  
Glutinous Rice ◽  
Milk Clotting Enzyme

scholarly journals Characterization of a Milk-clotting Enzyme from Hericium erinaceum and Its Proteolytic Action on Bovine Caseins

2018 ◽  
Vol 24 (4) ◽  
pp. 669-676 ◽  
Author(s):  
Kaoru Sato ◽  
Kenya Goto ◽  
Azusa Suzuki ◽  
Takayuki Miura ◽  
Motoi Endo ◽  
...  
Keyword(s):  
Milk Clotting ◽  
Milk Clotting Enzyme ◽  
Hericium Erinaceum ◽  
Proteolytic Action

Isolation and Characterization of Wild-Type Lipoxygenase LOXPsa1 from Pleurotus sapidus

2014 ◽  
Vol 69 (3-4) ◽  
pp. 149-154 ◽  
Author(s):  
Ina Plagemann ◽  
Ulrich Krings ◽  
Ralf G. Berger
Keyword(s):  
De Novo ◽  
Specific Activity ◽  
Maximal Activity ◽  
Wild Type ◽  
Isolation And Characterization ◽  
Peptide Mass ◽  
Purification Scheme ◽  
Pleurotus Sapidus ◽  
Nano Liquid Chromatography

The lipoxygenase LOXPsa1 of Pleurotus sapidus, originally investigated because of its ability to oxidize (+)-valencene to the valuable grapefruit aroma (+)-nootkatone, was isolated from the peptidase-rich lyophilisate using a three-step purification scheme including preparative isoelectric focusing and chromatographic techniques. Nano-liquid chromatography electrospray ionization tandem mass spectrometry (nLC-ESI-MS=MS) of the purified enzyme and peptide mass fingerprint analysis gave 38 peptides of the lipoxygenase from P. sapidus. Nearly 50% of the 643 amino acids long sequence encoded by the cDNA was covered. Both terminal peptides of the native LOXPsa1 were identified by de novo sequencing, and the postulated molecular mass of 72:5 kDa was confirmed. With linoleic acid as the substrate, the LOXPsa1 showed a specific activity of 113 U mg-1 and maximal activity at pH 7.0 and 30 °C, respectively.

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