Purification and Characterization of Intracellular Proteinase from Lactobacillus casei ssp. casei LLG

Shin, Ji‐Young; Jeon, Woo-Min; Kim, G.-B.; Lee, B.H.

doi:10.3168/jds.s0022-0302(04)73552-3

Cited by 13 publications

(9 citation statements)

References 34 publications

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“…Many native proteolytic systems have been reported from Lactobacillus lactis, L. helveticus, L. delbruecki and L. casei (Arora and Lee, 1992;Habibi-Najafi and Lee, 1994;Habibi-Najafi and Lee, 1995;Shin et al, 2004). They exhibit cell-wall proteinases and peptidases with different specificities (Christensen et al, 1999), but the genes of these lactic proteolytic and esterolytic enzymes have not yet been over-expressed in lactic cultures or other hosts.…”

Section: Over-expression Of Lab Enzymesmentioning

confidence: 97%

Biotechnological Methods to Accelerate Cheddar Cheese Ripening

Azarnia

Robert

Lee

2006

Critical Reviews in Biotechnology

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Cheese is one of the dairy products that can result from the enzymatic coagulation of milk. The basic steps of the transformation of milk into cheese are coagulation, draining, and ripening. Ripening is the complex process required for the development of a cheese's flavor, texture and aroma. Proteolysis, lipolysis and glycolysis are the three main biochemical reactions that are responsible for the basic changes during the maturation period. As ripening is a relatively expensive process for the cheese industry, reducing maturation time without destroying the quality of the ripened cheese has economic and technological benefits. Elevated ripening temperatures, addition of enzymes, addition of cheese slurry, attenuated starters, adjunct cultures, genetically engineered starters and recombinant enzymes and microencapsulation of ripening enzymes are traditional and modern methods used to accelerate cheese ripening. In this context, an up to date review of Cheddar cheese ripening is presented.

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Section: Over-expression Of Lab Enzymesmentioning

confidence: 97%

Biotechnological Methods to Accelerate Cheddar Cheese Ripening

Azarnia

Robert

Lee

2006

Critical Reviews in Biotechnology

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“…The thermostable protease by Streptomyces tendae was purified by ChiNam et al (2004), they observed the molecular weight of this enzyme as 21 kDa. Similarly, Shin et al (2004) reported that the molecular mass of the intracellular protease produced by L. casi was 55 kDa. Nakajima et al (1974) were reported two extracellular proteinases produced by Escherichia freundii with the molecular weight of 51 and 41 kDa, respectively.…”

Section: Discussionmentioning

confidence: 92%

Production and partial purification of protease by selected bacterial strains using raw milk as substrate

Prakash¹,

Kannapiran²,

Ramasubburayan³

et al. 2011

MJM

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Aims: The present study was investigated to optimize and partially purify the proteases produced by the food borne bacterial strains. Methodology and Results: Four bacterial strains such as Bacillus cereus, Proteus vulgaris, P. mirabilis and Enterobacter aerogenes were isolated from food wastes. These strains were individually inoculated in to the formulated culture media supplied with three different concentrations (1:1 to 1:3) of raw milk as major substrate. Among the concentrations, 1:2 ratio of substrate supplied medium showed maximum (0.133 to 8.000 IU/mL) protease production by all the tested organisms. After optimization, the organisms were tested for protease production at various pH (3 to 9), and temperature (30 to 80 °C). The result showed that all the organisms were capable of producing maximum protease at pH 6 (8.533 to 10.133 IU/mL) and at 50 °C (8.666 to 10.666 IU/mL). The crude enzymes produced by the tested organisms were individually purified by two different methods viz sodium alginate and ammonium sulphate-butanol methods. The purity of the protease determined in these two methods was ranged between 3.24 to 5.44 I and 3.13 to 5.55 IU/mL respectively. The partially purified enzymes were further analysed through SDS-PAGE; accordingly the molecular weight of protein produced by the test organisms was determined in between 49.44 and 50.98 kDa. Conclusion, significance and impact of study: Among the tested strains P. vulgaris was identified as the major protease producer in optimized culture condition of 50 o C and pH6. The molecular mass of the partially purified protease of P. vulgaris was 50.32 KDa. Further research on optimization of other fermentation parameters using statistical tools with P. vulgaris is needed to scale up the process.

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“…The thermostable protease by Streptomyces tendae was purified by Chi-Nam et al (2004), they observed the molecular weight of this enzyme as 21 KDa. Similarly, Shin et al (2004) reported the molecular mass of the intracellular protease produced by Lactobacillus casei was 55 KDa. Nakajima et al (1974) reported two types of extra cellular protease produced by Escherichia freundii with the molecular weight of 51 and 41 KDa, respectively.…”

Section: Discussionmentioning

confidence: 95%