Molecular and enzymatic properties of an aspartic proteinase from Rhizopus hangchow

Ichishima, Eiji; Ojima, Motoko; Yamagata, Yuriko; Hanzawa, Satoshi; Nakamura, Tetsuo

doi:10.1016/0031-9422(94)00552-5

Cited by 18 publications

(11 citation statements)

References 36 publications

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“…The (major) protease detected in the culture filtrate of chemostat cultures of F. graminearum was a 40 kDa aspartic protease. Aspartic proteases have been identified in a number of fungi: Rhizopus hangchow (Ichishima et al ., 1995), Rhizopus chinensis (Takahashi, 1987), Rhizopus niveus (Kurono et al ., 1971; Horiuchi et al ., 1988), Penicillium janthinellum (Hsu et al ., 1977; James & Sielechi, 1983), Cryphonectoria parasitica (Barkholt, 1987), Rhizomucor pusillus (Tonouchi et al ., 1986), Rhizomucor miehei (Christensen et al ., 1988), Aspergillus saitoi (Shintani & Ichishima, 1994), Aspergillus niger (Archer et al ., 1992; Mattern et al ., 1992; Calmers et al ., 1991; Inoue et al ., 1991; van Noort, 1991), Aspergillus awamori (Berka et al ., 1990; Hayashida & Flor, 1981), Mucor miehei (Gray et al ., 1986) and Botrytis cinerea (Movahedi & Heale, 1990a, b), all of which have a molecular mass between 34 and 43 kDa. Thus, the aspartic protease produced by F. graminearum would appear to be typical of fungal aspartic proteases.…”

Section: Discussionmentioning

confidence: 99%

Extracellular proteases produced by the Quorn® myco-protein fungus Fusarium graminearum in batch and chemostat culture

et al. 1997

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Fusarium gramhearum was grown in batch and continuous (chemostat) culture on a glucose-mineral salts medium in the presence and absence of casein. In the absence of casein no protease activity was detected in the culture filtrate from either batch or chemostat culture. For batch cultures grown on medium containing casein, most of the proteolytic activity detected in the supernatant during exponential growth had an optimum at ca pH 50. However, as the cultures passed from late exponential into stationary phase, the pH profile of the protease activity broadened until most of it was in the alkaline pH region. For glucose-limited chemostat cultures grown on media containing casein, protease activity had a narrow pH optimum with maximum activity at pH 59. For all concentrations of casein examined, protease activity was greater in chemostat culture than in batch culture. Extracellular proteases from batch and chemostat cultures were purified by bacitracin-Sepharose affinity chromatography. A t least seven proteins were purified from batch cultures but chemostat cultures contained only a single aspartic protease with a molecular mass of 40 kDa.

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Section: Discussionmentioning

confidence: 99%

Extracellular proteases produced by the Quorn® myco-protein fungus Fusarium graminearum in batch and chemostat culture

et al. 1997

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“…Rhizopuspepsins are a family of acidic proteases isolated form the Rhizopus genus [12,13]. Rhizopuspepsins have been isolated and biochemically characterized in R. chinensis [14], R. microsporus [15], R. hangchow [16], R. oryzae MTCC 3690 [11], and R. oryzae NBRC 4749 [17]. However, few studies concern the characterisation of Rhizopus stolonifer isolates.…”

Section: Introductionmentioning

confidence: 99%

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Liu¹,

Huang²

2015

TOBIOTJ

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Abstract:The present study characterises an acidic protease purified from the Rhizopus stolonifer strain, RN-11. The acidic protease with a 70 kDa molecular weight, was stable within pH 2-4 at temperatures 40-50℃. The temperature and pH value conducive to optimal catalytic activity were pH 2.5 and 50℃, respectively. Treatment with 5 mmol metal ions showed that the acidic protease was activated by Na . It was proposed that the studied acidic protease might represent a previously uncharacterised type of acidic protease produced by the Rhizopus stolonifer RN-11 strain.

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“…Of these cleavage sites, the peptide bonds Gln 4 -His 5 , Gly 23 -Phe 24 and Phe 24 -Phe 25 are speciWc to all acid proteinases of the genus Monascus [7,13]. The cleavage sites of Leu 15 -Tyr 16 and Tyr 16 -Leu 17 appeared to be common to all the fungal acid proteinases except for MpuAP [9,15,21,30]. On the other hand, the enzyme from M. purpureus preferentially split oV His 10 -Leu 11 and Gly 23 -Phe 24 in the oxidized insulin B-chain compared with other fungal acid proteinases.…”

Section: Cleavage Analysis On the Oxidized Insulin B-chainmentioning

confidence: 94%

“…Overall, these outcomes suggest that the enzyme combination reaction using MpuAP and trypsin might allow complete degradation of components of the whey protein. [13], 3 MpiAP2 of M. pilosus [13], 4 acid proteinase from M. kaoliang [7], 5 aspartic proteinase from Rhizopus hangchow [9], 6 Aspergillus saitoi aspartic proteinase [30], 7 Aspergillus fumigatus acid proteinase [21], 8 Penicillium janthinellum aspartic proteinase [15] To achieve the lowest antigenicity via an eYcient degradation of the whey protein, we also investigated the enzyme combination study. As we expected, the remaining band corresponding to -LG (as shown in Fig.…”

Section: Enzymatic Hydrolysis Of Whey Proteinmentioning

confidence: 99%

Application of an acid proteinase from Monascus purpureus to reduce antigenicity of bovine milk whey protein

Lakshman¹,

Tachibana²,

Toyama³

et al. 2011

J Ind Microbiol Biotechnol

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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, Gln(4)-His(5), His(10)-Leu(11), Ala(14)-Leu(15), Gly(23)-Phe(24) and Phe(24)-Phe(25) 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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Molecular and enzymatic properties of an aspartic proteinase from Rhizopus hangchow

Cited by 18 publications

References 36 publications

Extracellular proteases produced by the Quorn® myco-protein fungus Fusarium graminearum in batch and chemostat culture

Extracellular proteases produced by the Quorn® myco-protein fungus Fusarium graminearum in batch and chemostat culture

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

Application of an acid proteinase from Monascus purpureus to reduce antigenicity of bovine milk whey protein

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