Detergent Potential of a Spoilage Protease Enzyme Liberated by a Psychrotrophic Spore Former Isolated from Sterilized Skim Milk

Beena, A. K.; Geevarghese, P I; Jayavardanan, K. K.

doi:10.3923/ajft.2012.89.95

Cited by 14 publications

(19 citation statements)

References 7 publications

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“…Tween 80 caused slightly decrease in the alkaline protease activity. These results are in agreement with the previous findings on other protease from Bacillus cereus which showed high stability with tween 80 51 and alkaline protease from A. terreus which showed slightly decrease in activity with H 2 O 2 25 . A good detergent protease must be stable and compatible with surfactant, bleaches and oxidizing agents found in detergent formulation 52 .…”

Section: Discussionsupporting

confidence: 93%

Laundry Detergent Compatibility and Dehairing Efficiency of Alkaline Thermostable Protease Produced from <i>Aspergillus terreus</i> under Solid-state Fermentation

2020

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Introduction Protease enzymes EC 3.4.21-24 are fit for hydrolyzing the bonds between amino acids of protein molecule and they are the major industrial enzymes, which represented 60 of the complete synthetically produced enzymes 1. Alkaline proteases of microbial origin have impressive industrial intensity because of their biochemical decent variety and enormous applications in detergents, pharmaceutical, nourishment, dairy and leather industries 2. Fungi are the most microbes producing proteases with many advantages, since they are normally GRAS generally regarded as safe strains and their enzymes are secreted outside the cell which easily recover the enzyme 3, 4. Despite the fact that fungi are significant wellsprings of alkaline proteases 5, 6 , studies on their protease production are confined for the reason that the fungi prefer acidic and neutral pH values. Thus, it is of prime interest to search for

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Section: Discussionsupporting

confidence: 93%

Laundry Detergent Compatibility and Dehairing Efficiency of Alkaline Thermostable Protease Produced from <i>Aspergillus terreus</i> under Solid-state Fermentation

2020

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“…This decrease might be explained by the ice crystal formation that inactivates enzymes (Beena et al, 2012). Comparing to this result, Niyonzima and More (2015) found that for Aspergillus terreus the protease decrease with 9% after 40 days storage in -20°C.…”

Section: Effect Of Storage On the Stability Of The Enzyme Activitymentioning

confidence: 71%

“…The storage stability of the enzyme at -20°C was analyzed as described by Beena et al (2012). The enzyme was stored at the corresponding temperature and the residual activity was recorded by the standard assay procedure as described previously after exactly 4 months for a period of 18 months.…”

Section: Effect Of Storage Time On the Enzyme Stabilitymentioning

confidence: 99%

Characterization of the Crude Alkaline Extracellular Protease of Yarrowia lipolytica YlTun15

Bessadok¹,

Masri²,

Breuck³

et al. 2017

IPFS

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Abstract:Yarrowia lipolytica YlTun15 (GeneBank Acc. N° MF327143), isolated from farmed Dicentrarchus labrax's gills, secretes an alkaline extracellular protease, which exhibited the highest activity at pH 9 and temperature 45°C. The enzyme activity extracted was tested in the presence of different ion metal and protein inhibitors. .48% respectively at the 5 mM level. The enzyme was almost (activity=1.47%) inhibited by phenylmethylsulfonyl fluoride at the concentration of 5 mM. However, the protease activity was relatively constant in the presence of EDTA and SDS that may conclude that this enzyme was not a metalloprotease and belong to the serine protease category. After 18 months-storage at -20°C, the enzyme activity has decreased to 23.17%. This protease may have a potential application in food and detergent activity.

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“…Likewise, a proteolytic enzyme was produced by a strain of Lactobacillus brevis at optimum pH of 7.0, the enzyme is probably a neutral metalloprotease as reported by Amund et al (1990). In contrast, Beena et al (2012), Asker et al (2013) and Habib et al (2011) reported alkaline proteases activity from some Bacillus spp. and Halobaterium sp.…”

Section: The Effect Of Phmentioning

confidence: 96%

“…Overall, the protease enzyme obtained in our study was stable over a wide range of temperature and thus indicate its promising potential to be used in the detergent industries using hot or cold wash cycles, and in other different biotechnological applications. Beena et al (2012) explained the reduction in protease activity when exposed to high temperature by its probable thermal denaturation.…”

Section: The Effect Of Temperaturementioning

confidence: 99%

BIOCHEMICAL AND MOLECULAR CHARACTERIZATION OF AN EGYPTIAN MARINE ISOLATE "Alcaligenes faecalis" PRODUCING THERMOSTABLE PROTEASES

El-Eskafy

Abbas

Abdel-Hamid

et al. 2018

Egyptian Journal of Genetics and Cytology

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Detergent Potential of a Spoilage Protease Enzyme Liberated by a Psychrotrophic Spore Former Isolated from Sterilized Skim Milk

Cited by 14 publications

References 7 publications

Laundry Detergent Compatibility and Dehairing Efficiency of Alkaline Thermostable Protease Produced from <i>Aspergillus terreus</i> under Solid-state Fermentation

Laundry Detergent Compatibility and Dehairing Efficiency of Alkaline Thermostable Protease Produced from <i>Aspergillus terreus</i> under Solid-state Fermentation

Characterization of the Crude Alkaline Extracellular Protease of Yarrowia lipolytica YlTun15

BIOCHEMICAL AND MOLECULAR CHARACTERIZATION OF AN EGYPTIAN MARINE ISOLATE "Alcaligenes faecalis" PRODUCING THERMOSTABLE PROTEASES

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