Extracellular acid protease from Rhizopus oryzae: Purification and characterization

Kumar, Sushil; Sharma, Neeru S.; Saharan, Mukh R.; Singh, Randhir

doi:10.1016/j.procbio.2004.06.047

Cited by 187Enzyme Production and CharacterizationFungal and yeast genetics researchEnzyme Catalysis and Immobilization

Extracellular acid protease from Rhizopus oryzae: Purification and characterization

Kumar, Sushil, Sharma, Neeru S., Saharan, Mukh R., Singh, Randhir·2005·Process Biochemistry

DOI 10.1016/j.procbio.2004.06.047

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Most aspartyl proteases synthesized by fungi exhibit the highest activity under acidic conditions.
“as most aspartyl proteases synthesized by fungi exhibit the highest activity under acidic conditions.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Kumar et al., 2005
A broader range of stability has been observed for proteases derived from Rhizopus oryzae (pH 4.0 to 9.0), Thermoascus aurantiacus (pH 3.0 to 6.0), and Piptoporus soloniensis (pH 3.0 to 9.0).
“A broader range of stability has been observed for proteases derived from R. oryzae (pH 4.0 to 9.0; Kumar et al., 2005), Thermoascus aurantiacus (pH 3.0 to 6.0; Merheb et al., 2007), and Piptoporus soloniensis (pH 3.0 to 9.0; El-Baky et al., 2011).”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Kumar et al., 2005

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Purification and characterization of an aspartic protease from the Rhizopus oryzae protease extract, Peptidase R
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“, 1972), and the purified protease from Rhizopus oryzae (Kumar et al., 2005).”
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“SDS–PAGE To determine the molecular weight of purified protease, Sodium dodecyl sulphate poly acrylamide gel electrophoresis (SDS–PAGE) was performed according to the method of Laemmli (1970).”
Method
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“Maximal activity of fungal aspartic peptidases under acidic conditions was described for Cryptococcus sp. S-2, pH 5.0 (Rao et al., 2011); R. oryzae, pH 3.4 (Hsiao et al., 2014) and pH 5.5 (Kumar et al., 2005); and R. miehei, pH 5.5 (Silva et al., 2016).”
Influential
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“Vishwanatha et al. (2009 ) reported a molar mass of 47 kDa for a monomeric acid protease purified from Aspergillus oryzae , whereas the molecular mass of extracellular acid protease from Rhizopus oryzae was 34 kDa ( Kumar et al, 2004 ).”
Background
Purification and some properties of an extracellular acid protease from Aspergillus clavatus
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“acid proteases show maximal activity at low pH and thus find extensive applications in the production of seasoning materials [1, 2].”
Background
Extracellular protease from Mucor pusillus: purification and characterization
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“oryzae [19], the crude enzymatic extract from Penicillium oxalicum [35],”
Background
Cloning and Characterization of a Novel Aspartic Protease Gene from Marine-Derived Metschnikowia reukaufii and its Expression in E. coli
Li, J., Chi, Z., Liu, Z., Yue, L., Peng, Y., & Wang, L. (2008) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-008-8400-3 · Cited by 24 · see citing works
Purification and characterization of Bacillussubtilis milk-clotting enzyme from Tibet Plateau and its potential use in yak dairy industry
Li, Y., Liang, S., Zhi, D.-J., Chen, P., Su, F., & Li, H.-Y. (2012) · European Food Research and Technology · doi:10.1007/s00217-012-1663-5 · Cited by 22 · see citing works
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BackgroundMethodResultInfluential
Purification and characterisation of an acid protease from theAspergillus hennebergiiHX08 and its potential in traditional fermentation
Huang, Y., Wang, Y., & Xu, Y. (2017) · Journal of the Institute of Brewing · doi:10.1002/jib.427 · Cited by 23 · see citing works
Screening fermentation parameters of the milk-clotting enzyme produced by newly isolated Bacillus amyloliquefaciens D4 from the Tibetan Plateau in China
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“A milk-clotting enzyme has an important role in the process of cheese maturation (Kumar et al. 2005), and calf rennet has traditionally been used for this purpose.”
Background
Solid-State Fermentation for the Production of Proteases and Amylases and Their Application in Nutrient Medium Production
de Castro, A. M., dos Santos, A. F., Kachrimanidou, V., Koutinas, A., & Freire, D. M. G. (2017) · Elsevier eBooks · doi:10.1016/b978-0-444-63990-5.00010-4 · Cited by 22 · see citing works
New Biocatalyst with Multiple Enzymatic Activities for Treatment of Complex Food Wastewaters
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A glimpse of the endophytic bacterial diversity in roots of blackberry plants (Rubus fruticosus)
Contreras-Pérez, M., Loeza, P. D., Villegas, J., Farias, R. D. R., & Santoyo, G. (2016) · Genetics and Molecular Research · doi:10.4238/gmr.15038542 · Cited by 22 · see citing works
“Skim milk agar plates were used to detect protease production (Kumar et al., 2005) and siderophore production was determined by the chrome azurol S assay (Alexander and Zuberer, 1991).”
Method
Biochemical study of the extracellular aspartyl protease Eap1 from the phytopathogen fungus Sporisorium reilianum
Mandujano-González, V., Arana-Cuenca, A., Anducho-Reyes, M. Á., Téllez‐Jurado, A., González-Becerra, A. E., & Mercado-Flores, Y. (2013) · Protein Expression and Purification · doi:10.1016/j.pep.2013.10.003 · Cited by 21 · see citing works
“Different fungal genera, such as Aspergillus and Rhizopus [20,44,46], have been used for acid protease production in industrial applications.”
Background
Purification and characterization of an extracellular haloalkaline serine protease from the moderately halophilic bacterium, Bacillus iranensis (X5B)
Ghafouri, H., Askari, M., & Sarikhan, S. (2015) · Extremophiles · doi:10.1007/s00792-015-0804-8 · Cited by 21 · see citing works
“There has been a meaningful increase in the use of the enzymes as industrial catalysts (Zanphorlin et al. 2010; Gupta and Roy 2004; Masuii et al. 2004; Kumar et al. 2005).”
Background
PURIFICATION AND CHARACTERIZATION OF ACIDIC PROTEASE FROM ASPERGILLUS ORYZAE BCRC 30118
Yin, L., Chou, Y.-H., & Jiang, S. (2013) · Journal of Marine Science and Technology · doi:10.6119/jmst-012-0529-1 · Cited by 21 · see citing works
Purification and Characterization of a New Rhizopuspepsin fromRhizopus oryzaeNBRC 4749
Chen, C.-C., Cho, Y.-C., Lai, C., & Hsu, W.-H. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf8040337 · Cited by 21 · see citing works
Cloning, expression, and characterization of serine protease from thermophilic fungus Thermoascus aurantiacus var. levisporus
Li, A., Xie, C., Zhang, J., Zhang, J., & Li, D. (2011) · The Journal of Microbiology · doi:10.1007/s12275-011-9355-6 · Cited by 21 · see citing works
Purification of a killer toxin from Aureobasidium pullulans for the biocontrol of phytopathogens
Moura, V. S., Pollettini, F. L., Ferraz, L. P., Mazzi, M. V., & Kupper, K. C. (2020) · Journal of Basic Microbiology · doi:10.1002/jobm.202000164 · Cited by 20 · see citing works
Optimum production and characterization of an acid protease from marine yeast Metschnikowia reukaufii W6b
Li, J., Peng, Y., Wang, X., & Chi, Z. (2010) · Journal of Ocean University of China · doi:10.1007/s11802-010-1765-2 · Cited by 20 · see citing works
Neutral Serine Protease from Penicillium italicum. Purification, Biochemical Characterization, and Use for Antioxidative Peptide Preparation from Scorpaena notata Muscle
Abidi, F., Aissaoui, N., Chobert, J., Haertlé, T., & Marzouki, M. N. (2014) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-014-1052-6 · Cited by 20 · see citing works
Thermostable acidic protease production inAspergillus terreusNCFT 4269.10 using chickling vetch peels
Sethi, B. K., Jana, A., Nanda, P. K., MOHAPATRA, P. K. D., & Sahoo, S. L. (2015) · Journal of Taibah University for Science · doi:10.1016/j.jtusci.2015.11.001 · Cited by 20 · see citing works
Molecular modification and biotechnological applications of microbial aspartic proteases
Herman, R. A., Ayepa, E., Zhang, W.-X., Li, Z.-N., Zhu, X., Ackah, M., Yuan, S.-S., You, S., & Wang, J. (2024) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2023.2171850 · Cited by 20 · see citing works
Production and characterization of milk-clotting enzyme from Bacillus amyloliquefaciens JNU002 by submerged fermentation
Ding, Z., Wang, W.-F., Wang, B., Ouyang, A., Xiao, S., Wang, Y.-N., Liu, S.-P., Ding, M., Zhang, L., & Shi, G.-Y. (2012) · European Food Research and Technology · doi:10.1007/s00217-011-1650-2 · Cited by 17 · see citing works
“This trend was comparable with the MCE of Mucor baciliformi [25] and Rhizopus oryzae [26], while”
Result
Surface display of acid protease on the cells of Yarrowia lipolytica for milk clotting
Yu, X., Madzak, C., Li, H., Chi, Z., & Li, J. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2549-8 · Cited by 19 · see citing works
“In fact, the milkclotting activity is a common characteristic of all the aspartic protease (Kumar et al. 2005).”
Background
Structural modifications of plant proteins through fermentation: unlocking their functional and sensory potential in food applications
Cirunay, A. T., Barry-Ryan, C., & McAuliffe, O. (2025) · Critical reviews in food science and nutrition · doi:10.1080/10408398.2025.2560680 · Cited by 22 · see citing works
“Rhizopus species are known to produce extracellular aspartic proteases, known as rhizopuspepsins, with an optimal activity and stability in an acidic environment of around pH 3–6 (Chen et al. 2009; Kumar et al. 2005; Wu et al. 2018).”
Identification and Characterization ofEurotium rubrumIsolated from Meju in Korea
Yun, Y. H., Hyun, M. W., Suh, D. Y., Kim, Y. M., & Kim, S. H. (2009) · Mycobiology · doi:10.4489/myco.2009.37.4.251 · Cited by 18 · see citing works
Characterisation of the enzymatic properties of MpAPr1, an aspartic protease secreted by the wine yeast Metschnikowia pulcherrima
Theron, L. W., Bely, M., & Divol, B. (2017) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.8217 · Cited by 18 · see citing works
A novel thermostable aspartic protease from Talaromyces leycettanus and its specific autocatalytic activation through an intermediate transition state
Guo, Y., Tu, T., Zheng, J., Ren, Y., Wang, Y., Bai, Y., Su, X., Wang, Y., Yao, B., Huang, H., et al. (2020) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-10569-0 · Cited by 18 · see citing works
Optimization of milk-clotting enzyme production by Bacillus amyloliquefaciens SP1 isolated from apple rhizosphere
Guleria, S., Walia, A., Chauhan, A., & Shirkot, C. K. (2016) · Bioresources and Bioprocessing · doi:10.1186/s40643-016-0108-6 · Cited by 16 · see citing works
Evaluation of the milk clotting properties of an aspartic peptidase secreted by Rhizopus microsporus
da Silva, R. R., Souto, T. B., da Rosa-Garzon, N. G., de Oliveira, L. C. G., Juliano, M. A., Juliano, L., Rosa, J. C., & Cabral, H. (2019) · Preparative Biochemistry & Biotechnology · doi:10.1080/10826068.2019.1683861 · Cited by 16 · see citing works
“The optimal activity for this peptidase was at pH 5.5, with minor stability changes at a higher pH of 6 and temperature of 40 C. Contrary to what we observed, the optimal milk-clotting temperature for this peptidase was 35–40 C, with a loss of 75% of activity at 45 C. El-Baky et al.[26] also found a progressive improv…”
BackgroundResultInfluential
Cloning of the SAP6 gene of Metschnikowia reukaufii and its heterologous expression and characterization in Escherichia coli
Li, J., Chi, Z., & Wang, X. (2008) · Microbiological Research · doi:10.1016/j.micres.2008.08.003 · Cited by 16 · see citing works
“The milk-clotting activity is the common characteristics of all the aspartic protease (Kumar et al., 2005).”
Background
Optimization of milk-clotting protease production by a local isolate of Aspergillus niger FFB1 in solid-state fermentation
Bensmail, S., Mechakra, A., & Fazouane-Naimi, F. (2015) · Journal of Microbiology Biotechnology and Food Sciences · doi:10.15414/jmbfs.2015.4.5.467-472 · Cited by 14 · see citing works
“Consequently rennet substitutes from different origins are now used widely for cheese manufacture with more or less satisfactory results (Kumar et al., 2005; El-Bendary et al., 2007; Kumari et al., 2012).”
Background
Extracellular proteases and laccases produced by Pleurotus ostreatus PoB: the effects of proteases on laccase activity
Cruz-Vázquez, A., Tomasini, A., Armas-Tizapantzi, A., Marcial‐Quino, J., & Montiel-González, A. M. (2022) · International Microbiology · doi:10.1007/s10123-022-00238-9 · Cited by 14 · see citing works
Purification and characterization of the extracellular aspartyl protease APSm1 from the phytopathogen fungus Stenocarpella maydis
Mandujano-González, V., Téllez‐Jurado, A., Anducho-Reyes, M. Á., Arana-Cuenca, A., & Mercado-Flores, Y. (2015) · Protein Expression and Purification · doi:10.1016/j.pep.2015.09.017 · Cited by 14 · see citing works
UTILIZATION OF SALT WHEY FROM EGYPTIAN RAS (CEPHALOTYRE) CHEESE IN MICROBIAL MILK CLOTTING ENZYMES PRODUCTION
El-Tanboly, E.-S., El-Hofi, M. A., Youssef, Y. B., El-Desoki, W., & ISMAIL, A. A. (2012) · Journal of Food and Dairy Sciences · doi:10.21608/jfds.2012.75391 · Cited by 13 · see citing works
“(1978), ElBatawy (1991), Kumar et al. (2005) and El-Bendary et al. (2007) reported that the purified enzyme from A. ochraceus (MCA) was greatly enhanced by manganous ions and by increasing concentration of Cacl2.”
BackgroundResultInfluential
Pleurotus albidus: A new source of milk-clotting proteases
Martim, S. R., Larissa, S. C. S., Leilane, B. D. S., Edson, J. D. C., Alecrim, M. M., de Vasconcellos, M. C., Ila, M. D. A. O., & Maria, F. S. T. (2017) · African Journal of Microbiology Research · doi:10.5897/ajmr2017.8520 · Cited by 15 · see citing works
“The optimum temperature was determined at 60°C. Milk-clotting enzymes from other fungi as Rhizopus oryzae (Kumar et al., 2005), Penicillium oxalicum (Hashem, 1999) and Rhizopus microsporus var. rhizopodiformis (Sun et al., 2014) also presented optimum activity at 60°C.”
Background
Rhizopus oligosporus alkaline protease in cassava fermentation: Characterization and detergent potential
Egbune, E. O., Avwioroko, O. J., Orororo, O. C., Egbune, O. U., Aganbi, E., Anigboro, A. A., & Tonukari, N. J. (2023) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2023.102954 · Cited by 13 · see citing works
Purification and partial characterization of milk-clotting enzyme extracted from glutinous rice wine mash liquor
Wang, Y., Cheng, Q., Ahmed, Z., Jiang, X., & Bai, X. (2009) · Korean Journal of Chemical Engineering · doi:10.1007/s11814-009-0225-4 · Cited by 13 · see citing works
Purification and characterization of a milk-clotting protease from Mucor pusillus: Method comparison
Nouani, A., Moulti, F., & Belbraouet, S. (2011) · AFRICAN JOURNAL OF BIOTECHNOLOGY · Cited by 13 · see citing works
CHARACTERIZATION OF AN ASPARTIC PROTEASE PRODUCED BY Amylomyces rouxii
Marcial‐Quino, J., Santos, A., Fernández, F. J., Dı́az-Godı́nez, G., Montiel-González, A. M., & Tomasini, A. (2011) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) · Cited by 13 · see citing works
Production of highly active fungal milk-clotting enzyme by solid-state fermentation
Chinmayee, C. V., Vidya, C., Rani, A., & Singh, S. A. (2019) · Preparative Biochemistry & Biotechnology · doi:10.1080/10826068.2019.1630647 · Cited by 12 · see citing works
“Mucor and Rhizopus species have been reported to produce aspartic and serine/ cysteine proteases.([34,35]) Mucor thermohyalospora and R.”
Background
Characterization and immobilization of protease secreted by the fungus Moorella speciosa
de Oliveira, J. M., Fernandes, P. C. D. B., Benevides, R. G., & de Assis, S. A. (2020) · 3 Biotech · doi:10.1007/s13205-020-02412-0 · Cited by 12 · see citing works
Production of a novel milk‐clotting enzyme from solid‐substrate Mucor spp. culture
Qasim, F., Diercks‐Horn, S., Gerlach, D., Schneider, A., & Fernández‐Lahore, M. (2022) · Journal of Food Science · doi:10.1111/1750-3841.16307 · Cited by 12 · see citing works
Comparison of Milk-clotting Activity of Proteinase Produced by Bacillus Subtilis var, natto and Rhizopus oligosporus with Commercial Rennet
Chen, M. T., Lu, Y. Y., & Weng, T. M. (2010) · Asian-Australasian Journal of Animal Sciences · doi:10.5713/ajas.2010.80694 · Cited by 12 · see citing works
“Purification of clotting enzyme was carried out by the procedure of Kumar et al. (2005).”
BackgroundMethod
Utilization of salt whey from Egyptian Ras (cephalotyre) cheese in microbial milk clotting enzymes production.
El-Tanboly, E.-S., El-Hofi, M. A., Youssef, Y. B., El-Desoki, W., & ISMAIL, A. A. (2013) · PubMed · Cited by 12 · see citing works
Production of a Milk-Clotting Enzyme by Glutinous Rice Fermentation and Partial Characterization of the Enzyme: Production and Characterization of a Milk-Clotting Enzyme
Zhao, X., Wang, J., Zheng, Z., Zhao, A., & Yang, Z. (2015) · Journal of Food Biochemistry · doi:10.1111/jfbc.12108 · Cited by 11 · see citing works
Produção e caracterização de enzimas proteolíticas de Lentinus crinitus (L.) Fr. 1825 DPUA 1693 do bioma amazônico (Polyporaceae)
Magalhães, A. A. D. S., Silva, T. D. A., Teixeira, M. F. S., Filho, R. F. C., da Silva, S. D., Gomes, D. M. D., & Pereira, J. O. (2019) · Boletim do Museu Paraense Emílio Goeldi - Ciências Naturais · doi:10.46357/bcnaturais.v14i3.231 · Cited by 11 · see citing works
“A obtenção de proteases por microrganismos é possível graças à sua diversidade genética e bioquímica e por apresentarem fácil manipulação, o que viabiliza seu cultivo em grande escala (Rao et al., 1998; Kumar et al., 2005).”
Effect of Some Growth Factors on Protease Production by Rhizopus oryzae
Ahmed, S. A., & Abood, N. H. (2017) · Journal of Al-Nahrain University-Science · doi:10.22401/jnus.20.2.12 · Cited by 11 · see citing works
“[5-6] have ability to produce proteases.”
The catalytic and kinetic characterization of Bacillus subtilis MK775302 milk clotting enzyme: comparison with calf rennet as a coagulant in white soft cheese manufacture
Wehaidy, H. R., Abdel–Naby, M. A., Kholif, A. M. M., Elaaser, M. M., Bahgaat, W. K., & Wahab, W. A. A. (2023) · Journal of Genetic Engineering and Biotechnology · doi:10.1186/s43141-023-00513-w · Cited by 10 · see citing works
“The type of milk-clotting enzyme plays a vital role in milk coagulation and cheese maturation as it has a significant impact on the quality of the produced cheese [5].”
Background
Polidocanol inhibits Enterococcus faecalis virulence factors by targeting fsr quorum sensing system
Ashraf, D., Shaaban, M. I., Hassan, R., & El-Aziz, A. M. A. (2024) · BMC Microbiology · doi:10.1186/s12866-024-03548-2 · Cited by 10 · see citing works
Optimization of metalloprotease production by Eupenicillium javanicum in both solid state and submerged bioprocesses
Abou, A., Neto, H., de Souza‐Motta, C. M., & Cabral, H. (2013) · African Journal of Biochemistry Research · doi:10.5897/ajbr.9000179 · Cited by 10 · see citing works
Purification and Characterization of an Extracellular Acidic Protease of Pediococcus pentosaceus Isolated from Fermented Fish
Xu, Y., Dai, M., Zang, J., Jiang, Q., & Xia, W. (2015) · Food Science and Technology Research · doi:10.3136/fstr.21.739 · Cited by 10 · see citing works
“But the optimum temperature of acidic protease from P.pentosaceus 220 was lower than that from Aspergillus clavatus (50℃) (Silva et al., 2011) and Aspergillus oryzae LK-101 (50℃) (Lee et al., 2010), and Rhizopus oryzae (60℃) (Kumar et al., 2005).”
BackgroundInfluential

Purification and characterization of an aspartic protease from the Rhizopus oryzae protease extract, Peptidase R
Hsiao, N., Chen, Y., Kuan, Y.-C., Lee, Y.-C., Lee, S.-K., Chan, H.-H., & Kao, C. (2014) · Electronic Journal of Biotechnology · doi:10.1016/j.ejbt.2014.02.002 · Cited by 80 · see citing works
Purification and Characterization of a New Rhizopuspepsin fromRhizopus oryzaeNBRC 4749
Chen, C.-C., Cho, Y.-C., Lai, C., & Hsu, W.-H. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf8040337 · Cited by 21 · see citing works
Purification and characterization of protease from a newly isolated Rhizopus oryzae
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Purification and Characterization of Acidic Protease from Aspergillus oryzae
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Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11
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Authors: Kumar, S., Sharma, N. S., Saharan, M. R., & Singh, R.
Affiliations: Sher-e-Kashmir University of Agricultural Sciences and Technology of Jammu (IN)
Chaudhary Charan Singh Haryana Agricultural University (IN)
Corresponding author: Kumar, Sushil
ORCID: Kumar, Sushil
Singh, Randhir
Venue: Process Biochemistry
Publisher: Elsevier BV
Published: 2005-04
Volume: 40
Issue: 5
Pages: 1701-1705
ISSN: 0032-9592 (ISSN-L)
1359-5113
DOI: 10.1016/j.procbio.2004.06.047
OpenAlex: W2077610870
Cited by: 187
References: 29
Citations by year: 2026: 2 · 2025: 5 · 2024: 6 · 2023: 19 · 2022: 9 · 2021: 10 · 2020: 6 · 2019: 8 · 2018: 4 · 2017: 14 · 2016: 9 · 2015: 18 · 2014: 9 · 2013: 16 · 2012: 6
FWCI: 1.83
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Process Biochemistry (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
Keywords: Rhizopus oryzae, aspartic protease, enzyme purification, enzyme characterization, thermal stability, pH stability, calcium activation, substrate kinetics, pepstatin inhibition, histidine residues, diethylpyrocarbonate

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Extracellular acid protease from Rhizopus oryzae: Purification and characterization

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