Biotechnology of Cold-Active Proteases

Joshi, Swati; Satyanarayana, T.

doi:10.3390/biology2020755

Cited by 80 publications

(44 citation statements)

References 143 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, cold active enzymes obtained from cold adaptive microorganisms are active at lower temperature, therefore, energy saving and prevention of undesirable by-product formation could be possible [54,67]. Additionally, it has been reported that cold active proteolytic enzymes have higher specificity than mesophilic ones [54,67,68,69,70].…”

Section: Production Of Ace-inhibitory Peptides From Plantsmentioning

confidence: 99%

Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

et al. 2017

View full text Add to dashboard Cite

Hypertension is an important factor in cardiovascular diseases. Angiotensin-I-converting enzyme (ACE) inhibitors like synthetic drugs are widely used to control hypertension. ACE-inhibitory peptides from food origins could be a good alternative to synthetic drugs. A number of plant-based peptides have been investigated for their potential ACE inhibitor activities by using in vitro and in vivo assays. These plant-based peptides can be obtained by solvent extraction, enzymatic hydrolysis with or without novel food processing methods, and fermentation. ACE-inhibitory activities of peptides can be affected by their structural characteristics such as chain length, composition and sequence. ACE-inhibitory peptides should have gastrointestinal stability and reach the cardiovascular system to show their bioactivity. This paper reviews the current literature on plant-derived ACE-inhibitory peptides including their sources, production and structure, as well as their activity by in vitro and in vivo studies and their bioavailability.

show abstract

Section: Production Of Ace-inhibitory Peptides From Plantsmentioning

confidence: 99%

Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

et al. 2017

View full text Add to dashboard Cite

show abstract

“…Enzymes are known to be sensitive to temperature changes and the change in activity of any particular enzyme to such conditions is a distinguishing characteristic of such an enzyme. The use of non-thermophilic, cold-adapted proteases in detergents is desired as it promotes decrease in energy consumption (Joshi and Satyanarayana, 2013). …”

Section: Effect Of Temperature On Protease Activitymentioning

confidence: 99%

“…They also find usage in research. They constitute one of the largest groups of industrial enzymes and account for up to 60% of the total global sale of enzymes (Joshi and Satyanarayana, 2013). Proteases can be sourced from animals, plants, viruses, bacteria and fungi.…”

Section: Introductionmentioning

confidence: 99%

Partial Purification and Characterization of Extracellular Protease from <i>Pedicoccus acidilactici</i>

Oke¹,

Onilude²

2014

Nig J Bas App Sci

View full text Add to dashboard Cite

Microbial proteases have wide industrial applications and proteases of the lactic acid bacteria (LAB) have received special attention because of their importance in the food and dairy industry. Of all the LAB, the proteolytic system of the pediococci is the least studied. Therefore, this study was aimed at characterizing and purifying the protease produced by Pediococcus acidilactici grown in de Man, Rogosa and Sharpe (MRS) broth. Casein concentration of 2% (w/v) and 2.5 ml of the crude enzyme were optimal for the activity of the protease. The crude protease had temperature and pH optima of 28 o C and 4.0 respectively thus indicating that the enzyme is a mesophilic and acidic protease. Purification of the enzyme by gel filtration chromatography on Sephadex G75 following ammonium sulphate precipitation gave 2.26 fold increase in purification with specific activity of 46.13 units/mg protein while purification on Sephadex CM50 resulted in reduced purification fold (1.24 -1.59) with specific activity ranging between 25.39 -32.54 units/mg protein. The protease showed a characteristic band on SDS-PAGE and the molecular weight was estimated between 45 and 66 kDa. The potential applications of the protease are discussed.

show abstract

“…Most of the phytases have been reported to possess even number of cysteine residues which might be involved in the formation of disulphide bridges as in Aspergillus niger [27]. The enzyme is insensitive to phenylmethanesulphoonyl fluoride (PMSF), a well-known serine protease inhibitor [28]. N-ethylmaleimide (NEM) had no observable effect on the enzyme activity.…”

Section: Effect Of Various Modulators On Rpphy Activitymentioning

confidence: 99%

Characteristics and Applicability of Phytase of the Yeast Pichia anomala in Synthesizing Haloperoxidase

Joshi

Satyanarayana

2015

Appl Biochem Biotechnol

Self Cite

View full text Add to dashboard Cite

The phytase of the yeast Pichia anomala is a histidine acid phosphatase based on signature sequences and catalytic amino acids identified by site-directed mutagenesis. Among modulators, N-bromosuccinimide and butanedione inhibit phytase, while Ca(2+) and Ni(2+) stimulate slightly. Vanadate exhibits competitive inhibition of phytase, making it bifunctional to act as haloperoxidase. Molecular docking supports vanadate to share its binding site with phytate. The T 1/2, activation energy (E a ), temperature quotient (Q 10), activation energy of thermal inactivation (Ed), and enthalpy (ΔH d (0) ) of the enzyme are 4.0 min (80 °C), 27.72 kJ mol(-1), 2.1, 410.62 kJ mol(-1), and ∼407.8 kJ mol(-1) (65-80 °C), respectively. The free energy of the process (ΔG d (o) ) increases from 49.56 to 71.58 kJ mol(-1) with rise in temperature, while entropy of inactivation (ΔS d (0) ) remains constant at ∼1.36 kJ mol(-1) K(-1). The supplementation of whole wheat dough with rPPHY resulted in 72.5 % reduction in phytic acid content of bread. These characteristics confirm that the phytase has adequate thermostability for its applicability as a food and feed additive.

show abstract

Biotechnology of Cold-Active Proteases

Cited by 80 publications

References 143 publications

Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

Partial Purification and Characterization of Extracellular Protease from <i>Pedicoccus acidilactici</i>

Characteristics and Applicability of Phytase of the Yeast Pichia anomala in Synthesizing Haloperoxidase

Contact Info

Product

Resources

About