Production, purification and characterisation of proteases from whey by some fungi

El-Shora, Hamed M.; Metwally, Metwally Abdel-Azeem

doi:10.1007/bf03175548

Cited by 16 publications

(8 citation statements)

References 32 publications

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“…Protease assay was carried out by the adopted method of El-Shora & Metwally (2008) and El-Shora et al (2016). A sample (2.5ml) of casein solution (0.65%) prepared in 100mM Tris-HCl buffer (pH 8.5) was mixed with 0.5ml enzyme extract.…”

Section: Assay Of Protease Activitymentioning

confidence: 99%

Biocontrol of wilt-inducing Fusarium oxysporum by aqueous leaf extract from Egyptian Ammi majus and Ammi visnaga

El-Sharkawy

Alshora

2020

Egypt. J. Bot.

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Section: Assay Of Protease Activitymentioning

confidence: 99%

Biocontrol of wilt-inducing Fusarium oxysporum by aqueous leaf extract from Egyptian Ammi majus and Ammi visnaga

El-Sharkawy

Alshora

2020

Egypt. J. Bot.

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“…The second largest use of protease is in cheese making. Proteases are also used for bating (softening) leather, modifying food ingredients, as meat tenderisers, and in flavour development (Fukushima 1983;El-Shora and Metwally 2008). Proteases have also been studied for their role in blood clotting (Kaminishi et al 1994) and inflammatory diseases (Okamoto et al 2001).…”

Section: Introductionmentioning

confidence: 98%

Solid-state protease production using anchovy waste meal by moderate halophile Serratia proteamaculans AP-CMST isolated from fish intestine

et al. 2011

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The possibility of utilising anchovy waste meal as a substrate for protease production by the fish gut isolate Serratia proteamaculans AP-CMST was assessed through solid-state fermentation. A time course for protease production revealed 72 h to be the optimum duration for higher production (146.24 U/g). The most suitable pH, temperature and moisture level observed for higher protease production were pH 7 (123.5 U/g), 30°C (97.22 U/g) and 75% (126.7 U/ g), respectively. Protease production by S. proteamaculans AP-CMST was high in medium with added xylose (198.21 U/g), peptone (118.42 U/g), Triton X-100 (152.56 U/g) and manganese sulphate (178.33 U/g) when compared to other tested medium components. The halotolerancy of S. proteamaculans AP-CMST for protease production was 4% sodium chloride (155.65 U/g). Enzyme recovery from fermented anchovy waste meal was greatest (130.52 U/g) when 10% ethyl acetate was used as the extractant, and the optimum time range for extraction was 90-120 min.

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“…The resulting reveal that the substrate of α -glucosidase offered appreciable protection against dansyl chloride and the protection was dependent on the substrate concentration. Dansyl chloride is known as a reagent for lysyl group in proteins [15]. In this investigation d ansyl chloride inhibited α -glucosidase activity revealing that lysyl residue is present in the active site and taking essential part in the enzyme catalysis.…”

Section: Resultsmentioning

confidence: 65%

Induction, immobilization, modification and natural inhibitors of α-glucosidase from Penicillum chrysogenum

El-Shora

Messgo

Ibrahim

et al. 2019

ijpm

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α-glucosidase (EC: 3.2.1.20) was isolated from Penicillum chrysogenum. The enzyme was enhanced by plant growth regulators such as gibberellic acid (GA3), benzylaminopurine (BAP) and kinetin. Dansyl chloride inhibited the enzyme at 1, 2, 3, 4 and 5 mM with T0.5 67, 52.2, 34.4 and 23.3 min, respectively. The substrate offered partial protection for the enzyme against dansyl chloride inhibition. The enzyme was activated by Ca2+ and Mg2+. However, Pb2+, Cd2+, Zn2+, Ni2+ and Hg2+ inhibited α-glucosidase activity. The enzyme was immobilized on Ca alginate and the optimal concentration for 3% w/v. The optimal concentration of CaCl2 was recorded at 3 mM. The optimal CaCl2 concentration and the optimum time for immobilization was 3mM and 4hr. The enzyme was inhibited by aqueous extracts of Datura stramonium, Trigonella foenum-graecum, Hyoscymus muticus and Cynodon dactylon. The IC50 values for the four extracts were 59.1, 73.6, 68.5 and 77.1 µg ml-1, respectively.

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Production, purification and characterisation of proteases from whey by some fungi

Cited by 16 publications

References 32 publications

Biocontrol of wilt-inducing Fusarium oxysporum by aqueous leaf extract from Egyptian Ammi majus and Ammi visnaga

Biocontrol of wilt-inducing Fusarium oxysporum by aqueous leaf extract from Egyptian Ammi majus and Ammi visnaga

Solid-state protease production using anchovy waste meal by moderate halophile Serratia proteamaculans AP-CMST isolated from fish intestine

Induction, immobilization, modification and natural inhibitors of α-glucosidase from Penicillum chrysogenum

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