Cross-Linking of Gelatin Capsule Shells. Ken Boda Applications Engineer Agilent



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Cross-Linking of Gelatin Capsule Shells Ken Boda Applications Engineer Agilent

Agenda Gelatin and Cross-Linking USP Procedure pre-40(6) 40(6) Revisions to USP <711> and <2040> Failures Prevention of Cross-Linking

What is Gelatin? Hydrolyzed form of collagen Collagen is obtained from various animal by-products Used as a gelling agents in a variety of applications: Food Cosmetics Photography Pharmaceuticals

What is Cross-Linking? Cross-linking is the formation of strong chemical linkages beyond simple hydrogen and ionic bonding between gelatin chains. Reaction is generally irreversible Renders gelatin insoluble Reaction catalyzed by a number of chemical and environmental factors *From USP Stimuli to the Revision Process, Use of Enzymes in the Dissolution Testing of Gelatin Capsules and Gelatin-Coated Tablets Revisions. USP-PF 40(6)

Gelatin Structure Protein with some potentially reactive side chains Often will form helices, etc. Can form covalent and hydrogen bonds between itself and another chain Cross-linking can occur in collagen as condensation products between aldehydes and amines, or between two aldehydes Gelatin more prone to cross-linking than collagen

What can cause Cross-Linking in Gelatin? Aldehydes and Ketones APIs with carbonyl groups or potential aldehyde formation Oxidizing agents Metal Ions Sugars Heat High and Low Humidity Light Looking at it funny (just kidding but it s very reactive)

Cross-Linking Impact Capsule shell opening is delayed or stopped by pellicle formation on the internal or external gelatin surface Visually confirmed with seeing thin membranes or gelatinous masses Cross-linking amount can be determined by other methods NMR, UV/Fluorescence Spectroscopy, MRI, Near IR Spectroscopy

Cross-Linking Impact Lower and/or incomplete dissolution in vitro In severe situations, can lead to problems in vivo as well Cross-linking most commonly seen in stability testing Pictures used courtesy of Vivian Gray, 2014

Current USP Approach to Cross-linking

USP <711> For hard or soft gelatin capsules and gelatin-coated tablets that do not conform to the Dissolution specification, repeat the test as follows. Media < ph 6.8 repeat test with addition of purified pepsin (<750,000 units/l) Media ph 6.8 repeat test with addition of pancreatin (<1750 USP units of protease activity/l)

Pepsin Digestive enzyme in stomach which converts proteins to peptides For cross-linking, this is used to clean gelatin proteins in places other than cross-linking site and allow rupture Typically obtained from glandular layer of hog stomach Peak activity at ph 2, good activity to ~ph 4.5

Pancreatin Mixture of digestive enzymes created by exocrine cells of pancreas Typically porcine/bovine origin Has good protease activity Peak Activity at ph 6.8, good between 6-8

Success with USP <711> Pepsin activity generally felt sufficient to deal with mild to moderate cross-linking Pancreatin able to handle mild cross-linking

Limitations with USP <711> No good enzymes for ph 4-6.8 Surfactant/Enzyme incompatibility SLS and other surfactants can denature enzymes Other enzymes can enhance activity Pancreatin levels too low?

Enzyme Activity in mid-range 120 1.6 100 1.4 80 60 1.2 1 0.8 Peptic Activity % 40 20 0.6 0.4 0.2 Relative Protease Activity 0 0 0 2 4 6 8 10 12

Proposed Changes to <711>

Key Changes New Enzymes! Papain Bromelain Pre-treatment Option Increase in Pancreatin Levels Clarifications

When Enzymes are to be Used <711> changed to indicate the enzymes are to be used only when: Product contains gelatin Product does not meet dissolution specification Evidence of cross-linking is observed Prior to this, no evidence of cross-linking was required

Cross-Linking Evidence Defined in USP <1094> Liquid-Filled Capsules Dissolution Testing and Related Quality Attributes PF 38 (1) Observations (Gelatinous mass, pellicles, swelling w/o rupture) Instrumental Techniques (C13-NMR, FTIR, MRI, etc.) Switching capsule shells with fresh

Failure with Cross-Linking If cross-linking is seen, and failure occurs you DO NOT need to continue testing until the last stage.

Papain Derived from unripe green papaya Commonly used as meat tenderizer, dietary supplement, etc. Digests protein substrates more extensively than pancreatin Optimal ph between 6-7 for most substrates, ph 5 for gelatin Powder stable 2 years at 2-8C

Bromelain From Pineapple Stems Used commonly as meat tenderizer, anti-inflammatory agent, leather tanning, etc. Optimal ph 5-7, stable from ph 3.0-6.5 Powder stable 1.5-3 years at 2-8C

Papain and Bromelain in Dissolution Both suitable for use between ph 4-6.8 Papain used in activity of NMT 550,000 Units/L Activity determination explained in Papain monograph, under Assay Bromelain used in activity of NMT 30 gelatin-digesting units (GDU)/L of dissolution media Activity determination determined in Reagent Specifications, Bromelain

New Enzyme Levels Equivalent to Pepsin Used courtesy of Jian-Hwa Han, Abbvie

Increase in Pancreatin Previous graph also shows reason for increase from 1750 to 2000 units/l Pancreatin has been reported in the past to show a higher failure rate vs. pepsin in cross-linking

Enzyme Choice 9 Pepsin now clarified for use with 8 ph 4.0 7 6 5 4 3 2 1 0 Pancreatin for use with ph 6.8 For ph 4.0 6.8, you can use either Papain or Bromelain

Points of Consideration Enzyme interaction with media/formulation should be confirmed with samples through method development Enzyme(s) should be shown to be effective vs. cross-linked samples Tier 1 vs. Tier 2 with same stressed samples (see USP <1094>) Confirm performance of enzyme(s) to give proper results Use enzyme with best activity Validation of a method should include enzyme use where appropriate

Media Stability Raw powders of enzymes are stable for long periods of time at refrigerated conditions (2-8C) When enzymes are added to media, stability is greatly reduced Media with enzyme should be used within 4 hours of preparation (Jian-Hwa Han, Abbvie) Best to prepare and store buffer, and add enzymes when needed on day of use

Pre-Treatment of Surfactants If surfactants or other ingredients used denature the enzyme, then a pre-treatment step can be used. Similar to 2-stage dissolution Enzyme amount depends on the volume of pre-treatment step, not final dissolution volume Pre-Treatment should be under same dissolution conditions as the rest of the test Should not exceed 15 minutes, and pre-treatment time is part of total test time

Pre-treatment Options Media addition method Media changeover method Apparatus 3

Media Addition Method Perform test with media w/o surfactant (media A) at a lower volume. At end of pre-treatment period, add heated media with surfactant (media B) to end up with total correct volume. Advantages: Single vessel, dosage form doesn t need to be moved Disadvantages: Labor intensive/time consuming Less total units of enzyme in media Enzyme in media for all samples, potential issues for LC analysis

Media Changeover Method Perform Pre-Treatment in Media A. At end of period, move sample to another bath or completely replace media with media B. Advantages: Less labor intensive? Well suited to basket methods More units of enzyme Disadvantages: Still labor intensive Potential mishandling of dosage form May require 2 dissolution units

Bio-Dis Apparatus 3 Method could be developed as an App 3 method If enzymes needed: Perform pre-treatment in row 1 in Media A Row 2 for Media B

Changes to USP <2040> Disintegration and Dissolution of Dietary Supplements Similar revisions to USP <711> regarding new enzymes, higher pancreatin, presoaking, etc. Chewable tablets now require IR dissolution testing (not related to cross-linking) Rupture or Disintegration may be more sensitive test, should be determined on a method to method basis

Failures

What if failure still occurs w/ enzyme? If failure is still seen with enzyme, then you fail. It is not permissible to add additional enzymes or other techniques with a validated method.

Prevention is Key Challenge Product during Method Development Proper formulation development Capsule shell selection Excipients Use HPMC instead? Proper packaging Humidity Light Free Radicals

Capsule Shell Selection Much like API, capsule shells vary from vendor to vendor: Source of collagen Bovine hides/bones Porcine hides/bones Fish skins (kosher/halal) Recycled leather Manufacturing

Excipient Selection Problem Excipients: Corn starch stabilizer can decompose to formaldedye Sugars Polyhydric Alcohols Oxidating agents Sulfated Polysaccharides (chondroitin sulfate) Polyethylene glycol (peroxides/aldehydes) Metal Ions (colorants/dyes)

API Issues? If API is causing cross-linking, you may want to consider a HPMC capsule: No cross-linking Plant derived Able to be enteric coated Higher cost, fewer vendors Limited knowledge compared to gelatin APIs w/ carbonyl groups or potential aldehyde generation are prone to crosslinking

Packaging Selection Protect from humidity Avoid overuse of desiccant Protect from light Bottles w/ Rayon coilers can release furfural Blister packs may be advantageous for sensitive formulations

Cross-Linking Once it starts, it can t stop.

Summary Choice of good capsule shell, packaging, etc. key Pre-treatment now an option Additional enzymes for mid-ph range Challenge method with cross-linked samples Important: This is not official! Comments open until January 31, 2015!

References USP PF 38(1) <1094> Liquid-Filled Capsules Dissolution Testing and Related Quality Attributes USP PF 40(6) - <711> Dissolution and <2040> Disintegration and Dissolution of Dietary Supplements USP PF 40(6) Stimuli to the Revision Process: Use of Enzymes in the Dissolution Testing of Gelatin Capsules and Gelatin-Coated Tablets Revisions USP PF 24(5) Collaborative Development of Two-Tier Dissolution Testing for Gelatin Capsules and Gelatin-Coated Tablets Using Enzyme Containing Media USP Workshop of Dissolution Testing of Capsules, March 24-25 2014, Rockville, MD

Special Thanks Jian-Hwa Han of Abbvie for advice and permission to use graphs