Clinical applications of amylase: Novel perspectives

Azzopardi, Ernest A.; Lloyd, C. Chad; Teixeira, Sofia Rodrigues; Conlan, R. Steven; Whitaker, Iain S.

doi:10.1016/j.surg.2016.01.005

Cited by 47 publications

(23 citation statements)

References 120 publications

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“…SP has also been confirmed experimentally to demonstrate effective anti-inflammatory outcomes supporting its antioxidant mechanisms [7,46,67,69]. It redesigns the nitric oxide synthase (NOS) isoforms and suppresses pro-inflammatory cytokines such as IL-1β, IL-6, IL-8, TNF-α and IFN [67,[69][70][71], with a simultaneous release of α-Amylase enzyme promoting anti-inflammatory and anti-oxidative effects at the site of inflammation [72,73]. Similar to other herbal extracts [31,74], the capacity of SP to obstruct eicosanoid development may be correlated with the possible mechanism by which SP could employ this combined anti-inflammatory and anti-oxidant effect.…”

Section: Antioxidant and Anti-inflammatory Effectsmentioning

confidence: 99%

Salvadora persica: Nature’s Gift for Periodontal Health

Mekhemar

Geib²,

Kumar

et al. 2021

Antioxidants

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Salvadora persica (SP) extract, displays very valuable biotherapeutic capacities such as antimicrobial, antioxidant, antiparasitic and anti-inflammatory effects. Numerous investigations have studied the pharmacologic actions of SP in oral disease therapies but its promising outcomes in periodontal health and treatment are not yet entirely described. The current study has been planned to analyze the reported effects of SP as a support to periodontal therapy to indorse regeneration and healing. In consort with clinical trials, in vitro investigations show the advantageous outcomes of SP adjunctive to periodontal treatment. Yet, comprehensive supplementary preclinical and clinical investigations at molecular and cellular levels are indispensable to reveal the exact therapeutic mechanisms of SP and its elements for periodontal health and therapy.

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Section: Antioxidant and Anti-inflammatory Effectsmentioning

confidence: 99%

Salvadora persica: Nature’s Gift for Periodontal Health

Mekhemar

Geib²,

Kumar

et al. 2021

Antioxidants

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“…Initially, AC was used to enrich amylase along with its partners from the complex saliva solution. The reaction between amylase and starch is an enzymatic reversible mechanism [ 20 ], allowing for the recovery of intact amylase after its reaction with the starch. The use of a starch column was previously described as a mean for depletion of amylase from saliva [ 31 ].…”

Section: Discussionmentioning

confidence: 99%

“…Amylase is the most abundant protein found in human saliva. Amylase is also present in the secretion of mammary and lacrimal glands [ 20 ]. Despite the vast literature on salivary amylase, the main function of salivary amylase as an efficient initiator of food digestion in the oral cavity is still debatable [ 21 , 22 ].…”

Section: Introductionmentioning

confidence: 99%

Revealing the Amylase Interactome in Whole Saliva Using Proteomic Approaches

Crosara

Zuanazzi

Moffa

et al. 2018

BioMed Research International

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Understanding proteins present in saliva and their function when isolated is not enough to describe their real role in the mouth. Due to protein-protein interactions, structural changes may occur in macromolecules leading to functional modulation or modification. Besides amylase's function in carbohydrate breakdown, amylase can delay proteolytic degradation of protein partners (e.g., histatin 1) when complexed. Due to its biochemical characteristics and high abundance in saliva, amylase probably interacts with several proteins acting as a biological carrier. This study focused on identifying interactions between amylase and other proteins found in whole saliva (WS) using proteomic approaches. Affinity chromatography was used, followed by gel electrophoresis methods, sodium dodecyl sulfate and native, tryptic in-solution and in-gel digestion, and mass spectrometry. We identified 66 proteins that interact with amylase in WS. Characterization of the identified proteins suggests that acidic (pI < 6.8) and low molecular weight (MW < 56 kDa) proteins have preference during amylase complex formation. Most of the identified proteins present biological functions related to host protection. A new protein-amylase network was constructed using the STRING database. Further studies are necessary to investigate individualities of the identified amylase interactors. These observations open avenues for more comprehensive studies on not yet fully characterized biological function of amylase.

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“…3.2.1.1) catalyze the hydrolysis of α -1,4 glycosidic bonds present in starch, glycogen and other related carbohydrates to low molecular weight products, such as glucose, maltose and maltotriose [ 4 , 5 , 6 , 7 , 8 ]. These enzymes are present in plants, animals and microorganisms [ 9 ] and have extensive applications in medicine [ 10 , 11 , 12 , 13 , 14 ], textiles [ 11 ], detergent [ 11 ], fermentation [ 11 ] and the food industry [ 4 , 11 ].…”

Section: Introductionmentioning

confidence: 99%

Determination of Activation Energies and the Optimum Temperatures of Hydrolysis of Starch by α-Amylase from Porcine Pancreas

Miłek

2021

Molecules

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The present paper reports the determination of the activation energies and the optimum temperatures of starch hydrolysis by porcine pancreas α-amylase. The parameters were estimated based on the literature data on the activity curves versus temperature for starch hydrolysis by α-amylase from porcine pancreas. It was assumed that both the hydrolysis reaction process and the deactivation process of α-amylase were first-order reactions by the enzyme concentration. A mathematical model describing the effect of temperature on porcine pancreas α-amylase activity was used. The determine deactivation energies Ea were from 19.82 ± 7.22 kJ/mol to 128.80 ± 9.27 kJ/mol, the obtained optimum temperatures Topt were in the range from 311.06 ± 1.10 K to 326.52 ± 1.75 K. In turn, the values of deactivation energies Ed has been noted in the range from 123.57 ± 14.17 kJ/mol to 209.37 ± 5.17 kJ/mol. The present study is related to the starch hydrolysis by α-amylase. In the industry, the obtained results the values Ea, Ed, Topt can be used to design and optimize starch hydrolysis by α-amylase porcine pancreas. The obtained results might also find application in research on the pharmaceutical preparations used to treat pancreatic insufficiency or prognosis of pancreatic cancer.

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Clinical applications of amylase: Novel perspectives

Cited by 47 publications

References 120 publications

Salvadora persica: Nature’s Gift for Periodontal Health

Salvadora persica: Nature’s Gift for Periodontal Health

Revealing the Amylase Interactome in Whole Saliva Using Proteomic Approaches

Determination of Activation Energies and the Optimum Temperatures of Hydrolysis of Starch by α-Amylase from Porcine Pancreas

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