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Lipases

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Overview

Fig.1 Lipase A.Fig.1 Phosphorylated Bacillus pumilus lipase A. (Van der Ent, et al., 2022)

Lipases are a class of enzymes that hydrolyze the ester bonds in fat molecules, breaking them down into glycerol and fatty acids. Obesity, as a complex metabolic disease, is closely related to the imbalance of fat metabolism. Alterations in lipase activity affect fat absorption, storage, and utilization, thus having an impact on body weight and body fat distribution.

Protheragen offers lipase products from a variety of sources and at different concentrations to meet our clients' research needs in the field of obesity.

Highly Active Lipase Helps Clients with In-Depth Research

Our company is deeply committed to research in the field of obesity and has always been committed to providing our clients with all kinds of high-quality lipase and its related products, aiming to promote the development of obesity research comprehensively.

Our lipase products meet the diverse needs of clients in obesity research with their excellent activity and stability. From basic obesity mechanism research to drug screening, functional food development, and nutritional research, our products are widely used in various fields of obesity and related metabolic diseases.

Rich Sources (Animal, Plant, and Microbial)


  • Fungal sources of lipases
    • Antrodia cinnamomea
    • Aspergillus aculeatus
    • Aspergillus awamori
    • Aspergillus flavus
    • Aspergillus fumigatous
    • Aspergillus niger
    • Aspergillus sydowi
    • Aspergillus terreus
    • Fusarium incarnatum
    • Fussarium solani
    • Penicillium aurantiogriseum
    • Penicillium chrysogenum
    • Penicillium restrictum
    • Penicillium roqueforti
    • Penicillium verrucosum
    • Rhizopus homothallicus
    • Rhizopus oryzae
    • Talaromyces thermophiles
    • Thermomyces lanoginosus
  • Yeast sources of lipases
    • Yarrowia lipolytica
    • Crytococcus sp.
    • Meyerozyma guilliermondii
    • Candida rugose
    • Candida 99-125
    • Magnusiomyces capitatus JT 5
    • Trichosporon asahii MSR 54
    • Guehomyces pullulans
    • Thermomyces lanuginosus
    • Candida W 3.8
  • Other sources of lipases
    • Porcine pancreas
    • Rabbit pancreas
    • Wheat germ
  • Artificially engineered lipase

Publication

Technology: Radioimmunoassay, Real-time quantitative polymerase chain reaction (abbreviated PCR)

Journal: International Journal of Molecular Sciences

Published: 2020

IF: 4.9

Results: In this study, researchers explored the metabolic impact of angiopoietin-like protein 4 (ANGPTL4) and lipoprotein lipase (LPL) expression in visceral adipose tissue (VAT) in obese individuals, particularly in individuals with abnormal glucose metabolism (AGM). ANGPTL4 overexpression in VAT was found to be associated with impaired local metabolism and inflammation and predicted impaired glucose regulation and type 2 diabetes (T2D) in obese individuals. In contrast, high LPL expression describes a state of increased adipocyte lipid storage, which may serve as a protective mechanism against ectopic fat accumulation and related metabolic diseases.

Fig.2 VAT ANGPTL4 and LPL mRNA expression levels across quartiles of vitamin D receptor (VDR) mRNA levels.Fig.2 VAT ANGPTL4 and LPL mRNA expression levels. (Barchetta, et al., 2020)

Applications

Advantages of lipase products. (Protheragen)

  • Studies on the mechanisms of obesity: To study the role of lipase in fat metabolism and the effect of altered lipase activity on body weight and body fat distribution.
  • Drug screening: Our products can be used to screen drugs that modulate lipase activity as new targets for obesity treatment.
  • Functional excipient development: Our products can be used to develop functional excipients containing lipase-inhibiting ingredients to help control weight and reduce the risk of obesity.
  • Nutritional studies: Our products can be used to examine the effect of different dietary components on lipase activity and the role of this effect on obesity and metabolic health.

Advantages of Our Products

  • High quality: Our lipase products undergo strict quality control to ensure that enzyme activity and purity meet the highest industry standards.
  • Versatility: We offer lipase products from a variety of sources (animal, plant, and microbial) to meet the diverse research needs of our clients.
  • Specificity: The lipases we offer are highly substrate-specific, selectively catalyzing specific chemical reactions.
  • Customized service: We provide customized service to provide customized lipase products and solutions according to the client's specific research needs.

Frequently Asked Questions

  1. Why is lipase the third most popular enzyme?

    Lipase is the third-largest enzyme after amylase and protease, and its substrate diversity and richness are only second to protease. Lipase has many kinds of substrates; for example, the substrates of lipase contained in wheat can be up to 23 kinds, such as glycerides, phospholipids, glycolipids, etc. Plus, it is different from other hydrolytic enzymes, which have two-phase reaction interfaces of water and oil, so it is more popular.

  2. How to test lipase activity?
    • Immunological methods: Western blot, radioimmunoassays (RIAs), and enzyme-linked immunosorbent assay (ELISA).
    • Physical and chemical methods: Plate methods, colorimetric methods, and titration methods.

Protheragen not only provides diversified lipase products but also focuses on close cooperation with clients. We provide customized product solutions and technical support by understanding our clients' specific needs in obesity research. Feel free to contact us for more information.

References

  1. Barchetta, I.; et al. Angiopoietin-like protein 4 overexpression in visceral adipose tissue from obese subjects with impaired glucose metabolism and relationship with lipoprotein lipase. International Journal of Molecular Sciences. 2020, 21, 7197. (CC BY 4.0)
  2. Van der Ent, F.; et al. Structure and mechanism of a cold-adapted bacterial lipase. Biochemistry. 2022, 61(10): 933-942. (CC BY 4.0)

Lipase Products

Source
Type
Subcategory
Lipase from Candida rugosa, Type VII, ≥700 U/mg
  • CAS No.: 9001-62-1
  • EC No.: 3.1.1.3
  • Source: Candida rugosa
  • Specific Activity: ≥700 U/mg solid
Lipase from <i>Candida rugosa</i>, Type VII, ≥700 U/mg
Lipase from Candida rugosa, ≥40,000 U/mg protein
  • CAS No.: 9001-62-1
  • EC No.: 3.1.1.3
  • Source: Candida rugosa
  • Specific Activity: ≥40,000 U/mg protein
Lipase from <i>Candida rugosa</i>, ≥40,000 U/mg protein
Lipase from Candida rugosa, ≥2 U/mg
  • CAS No.: 9001-62-1
  • EC No.: 3.1.1.3
  • Source: Candida rugosa
  • Specific Activity: ≥2 U/mg
Lipase from <i>Candida rugosa</i>, ≥2 U/mg
Lipase from Candida rugosa, 15-25 U/mg
  • CAS No.: 9001-62-1
  • EC No.: 3.1.1.3
  • Source: Candida rugosa
  • Specific Activity: 15-25 U/mg
Lipase from <i>Candida rugosa</i>, 15-25 U/mg
Lipase from porcine pancreas, Type II
  • CAS No.: 9001-62-1
  • EC No.: 3.1.1.3
  • Source: Porcine pancreas
  • Specific Activity: ≥125 U/mg protein (using olive oil (30 min incubation)); 30-90 U/mg protein (using triacetin)
Lipase from porcine pancreas, Type II
Lipase from porcine pancreas, Type VI-S
  • CAS No.: 9001-62-1
  • EC No.: 3.1.1.3
  • Source: Porcine pancreas
  • Specific Activity: ≥20,000 U/mg protein
Lipase from porcine pancreas, Type VI-S
Lipase from Aspergillus niger, 200 U/g
  • CAS No.: 9001-62-1
  • EC No.: 3.1.1.3
  • Source: Aspergillus niger
  • Specific Activity: ~200 U/g
Lipase from <i>Aspergillus niger</i>, 200 U/g
Lipase from Rhizopus oryzae, 10 U/mg
  • CAS No.: 9001-62-1
  • EC No.: 3.1.1.3
  • Source: Rhizopus oryzae
  • Specific Activity: ~10 U/mg
Lipase from <i>Rhizopus oryzae</i>, 10 U/mg
Lipase from Rhizopus oryzae, ≥30 U/mg
  • CAS No.: 9001-62-1
  • EC No.: 3.1.1.3
  • Source: Rhizopus oryzae
  • Specific Activity: ≥30 U/mg
Lipase from <i>Rhizopus oryzae</i>, ≥30 U/mg
Lipase from wheat germ, Type I
  • CAS No.: 9001-62-1
  • EC No.: 3.1.1.3
  • Source: Wheat (germ)
  • Specific Activity: 5-15 U/mg solid
Lipase from wheat germ, Type I
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