A Randomized Controlled Trial of the Efficacy of Systemic Enzymes and Probiotics in the Resolution of Post-COVID Fatigue.

Muscle fatigue and cognitive disturbances persist in patients after recovery from acute COVID-19 disease. However, there are no specific treatments for post-COVID fatigue. Objective: To evaluate the efficacy and safety of the health supplements ImmunoSEB (systemic enzyme complex) and ProbioSEB CSC3 (probiotic complex) in patients suffering from COVID-19 induced fatigue.

Serratiopeptidase: Insights into the therapeutic applications.

Therapeutic applications of enzymes have been widely accepted in clinical practices for decades. Proteolytic enzymes in particular, have been used for the treatment of diseases and disorders. Serratiopeptidase is a proteolytic enzyme having immense applications in therapeutic areas which have been validated by several , and clinical studies as well as through anecdotal evidences.

Interaction of polyphenol oxidase of Solanum tuberosum with β-cyclodextrin: Process details and applications.

Polysaccharides differing in structure and chemical nature were screened for their ability to bind non-covalently with polyphenol oxidase (PPO) from potato (as a model) and their effect on enzyme activity. All the polysaccharides selected inhibited the PPO but β-cyclodextrin showed maximum inhibition under optimum conditions. Process details for the inhibition of PPO were studied with respect to concentration of β-cyclodextrin, temperature, pH, and time.

Interaction of carbohydrates with alcohol dehydrogenase: Effect on enzyme activity.

Alcohol dehydrogenase was covalently conjugated with three different oxidized carbohydrates i.e., glucose, starch and pectin.

Pullulan-complexed α-amylase and glucosidase in alginate beads: enhanced entrapment and stability.

Enhanced entrapment of the enzymes, α-amylase and glucoamylase, was found in alginate beads on addition of pullulan in the enzyme mixture. Under optimized process conditions of entrapment, enzymes-pullulan complex showed an entrapment of 85% in the alginate beads as opposed to 25% for the free enzymes. Beads of enzymes-pullulan complex showed lower inactivation rate constant and higher half life than corresponding beads of free enzymes.

Enhanced stability of alcohol dehydrogenase by non-covalent interaction with polysaccharides.

Non-covalent interaction of alcohol dehydrogenase with polysaccharides was studied using three neutral and three anionic polysaccharides. The process of interaction of alcohol dehydrogenase with gum Arabic was optimized with respect to the ratio of enzyme to gum Arabic, pH, and molarity of buffer. Alcohol dehydrogenase-gum Arabic complex formed under optimized conditions showed 93% retention of original activity with enhanced thermal and pH stability.

Laccase-gum Arabic conjugate for preparation of water-soluble oligomer of catechin with enhanced antioxidant activity.

Catechin was oligomerized using free laccase and laccase-gum Arabic conjugate. The process of oligomerization was optimized with respect to solvent, ratio of solvent to buffer (0.2:10 to 1:10), pH of buffer (3-10), enzyme (575-18,400 U/mg) and substrate concentration (1-7mM).

Co-conjugation vis-à-vis individual conjugation of α-amylase and glucoamylase for hydrolysis of starch.

Two enzymes, α-amylase and glucoamylase have been individually and co-conjugated to pectin by covalent binding. Both the enzyme systems showed better thermal and pH stability over the free enzyme system with the complete retention of original activities. Mixture of individually conjugated enzymes showed lower inactivation rate constant with longer half life than the co-conjugated enzyme system.

Screening of polysaccharides for preparation of α-amylase conjugate to enhance stability and storage life.

Nine polysaccharides differing in structure and chemical nature were screened for their ability to conjugate with α-amylase by covalent binding for enhancing the thermal and pH stability of α-amylase. Among these polysaccharides, agar, dextran, pectin and xanthan showed better results but dextran stood out among all the polysaccharide for providing both thermal and pH stability to α-amylase. α-Amylase conjugated with agar, dextran, pectin and xanthan showed antimicrobial property with added preservative (0.

Conjugation of α-amylase with dextran for enhanced stability: process details, kinetics and structural analysis.

The influence of enzyme polysaccharide interaction on enzyme stability and activity was elucidated by covalently binding dextran to a model enzyme, α-amylase. The conjugation process was optimized with respect to concentration of oxidizing agent, pH of enzyme solution, ratio of dextran to enzyme concentration, temperature and time of conjugate formation, and was found to affect the stability of α-amylase. α-Amylase conjugated under optimized conditions showed 5% loss of activity but with enhanced thermal and pH stability.